The importance of the Viet Cong in the Communist victory in the Second Indochina War Essay Example for Free

The importance of the Viet Cong in the Communist victory in the Second Indochina War Essay Assess the importance of the Viet Cong in the Communist victory in the Second Indochina War. The Second Indochina War, which was waged throughout 1964-75, was an undefined success for the Communist cause. Whilst this result was derived from a combination of both intrinsic and international factors, due credit must be given to the extremely vital role that the ‘Viet Cong’ successfully executed. Whilst the ‘Viet Cong’ may have resembled a dynamic and competent fighting force, the foundation of their infamous reputation was primarily based upon their use of guerilla warfare tactics. These tactics, unlike conventional warfare, involved a combination of unpredictable and even primitive military strategies which is reflected in the maxim â€Å"When the enemy advances, withdraw; when he defends, harass; when he withdraws, pursue.†[1] Such tactics enabled Communist forces of the NLF to become an elusive and deadly arch-rival. To further enhance their military capabilities, Communist forces excavated a vast network of underground tunnels which were reinforced with concrete, in an effort to survive artillery bombardment as well as air strikes sanctioned under operations ‘Barrel Roll’ as well as ‘Rolling Thunder.’ As seen in ‘Source 1’ the Viet Cong also implemented various booby trap systems using punji stakes, mines and deep pits in an effort to maim and potentially kill US and ARVN forces. These tactics were extremely successful for they not only accounted for â€Å"73% of total US casualties and 11% of combat deaths†[2] but they also denied the victims of such acts any targets to shoot at, for the VC usually deserted the area. What enhanced the success of such tactics was that when these maimed soldiers returned home, they took with them a demoralizing message of the atrocities occurring in Vietnam. The psychological victory of the TET offensive, January 1968, also highlighted the strategic importance of the Viet Cong. The battle, which lasted all of a few days, involved a major deployment of VC and other Communist forces against 36 major towns within South Vietnam. The offensive concluded with the VC symbolically siegeing the US embassy in Saigon in a deliberate ploy to both humiliate and expose the US’s inability to quell the spread of Communism. Despite the fact that the VC were crippled after the almost suicidal battle, the event represented a major turning point in the Vietnamese conflict. As a result, the following night international broadcasts were made which expressed the flawed nature of LBJ’s foreign policy. Consequently the guerrilla tactics implemented by the ‘Viet Nam Cong San’ were vital to the success of the Communist regime for they gradually wore US and ARVN forces down in a war of attrition and psychological victories. Another contributing factor to the Communist victory was their ability to engage in a ‘total war of attrition.’ This concept of ‘total war’, which was described by General Ludendorff in 1935, involves â€Å"the complete mobilization of all resources, including policy and social systems, to the winning of war.†[3] The Viet Cong fulfilled this concept for not only did they sacrifice their material possessions, but more importantly their lives. Whilst the VC were obviously devoted to the cause, unfortunately this was not a uniform policy throughout all Communist units, for many individuals had personal agendas to fulfill, often involving the black-market. The well known phrase â€Å"Soldiers by night, farmers by day†[4] epitomized the Communist people’s whole hearted commitment to the cause. This contrast in roles was a valuable tool for it ensured that the home front remained productive, whilst also enabling the Viet Cong to dissolve back into society after combat, so as to fight another day. What furthered the importance of the Viet Cong’s ‘total war’ strategy was that allied soldiers would often exterminate whole villages in retribution for fallen comrades, often killing unarmed civilians. Evidence of this can be seen in My Lai massacre of 1968, in which 450 women and children were executed for ‘harboring’ VC forces. Source 2, a quote by Robert McNamara, accurately summarizes the repercussions of such a successful Communist strategy stating, â€Å"The picture of the world’s greatest superpower killing 1,000 non-combatants a week, while trying to pound a tiny backward nation into submission†¦ is not a pretty one.†[5] In comparison to the committed nature of the Communist forces it appears that the United States fought a limited war which was justified by Lyndon Johnson in 1965 for Vietnam was only a â€Å"little piss-ant country.† [6] Unlike the VC who were quoted to â€Å"take on tanks, if necessary, with bows and arrows†[7] the US were always too concerned over the repercussions of their actions rather than having a committed aim to quell the ongoing conflict. Throughout the conflict it is obvious that US Foreign Policy was always â€Å"fighting with one hand behind its back†[8] due to LBJ’s attempts to maintain his ‘guns and butter’ approach which involved balancing civil works as well as ‘prolonging’ the Communist conflict. The United States incapacity to end the conflict was further highlighted by their fear of provoking Soviet or Chinese involvement. On many occasions, US forces had the ability to severely cripple the Communist campaign, but yet their incompetence always seemed to get the better of them which is why they never ‘got the bloody job done.’ The ‘Viet Nam Cong San’ ability to seduce the ‘hearts and minds’ of the Vietnamese home front was a vital stepping stone to the Communist victory. As a result of the intimate contact that NLF forces had with villagers throughout the conflict, an almost unbreakable bond was formed. Unlike the Allies who attempted to indoctrinate and relocate villagers through the use of ‘strategic hamlet programs’, as well as the NVA who were renowned for the use of shock tactics, the VC successfully offered support and protection in a passive manner. Consequently the VC’s relationship with villagers was extremely valuable for it often resulted in the donation of intelligence, concealment and in some cases converted soldiers. The importance of this relationship is highlighted in the quote â€Å"By 1967 US personnel couldn’t breathe without the NLF actively knowing.†[9] In comparison, the United States public was rife with division over the Vietnamese conflict. This division in America exposed the US politician’s inability to even win the hearts and minds of its own people let alone a competing nation. An extract of Source 3, â€Å"War is not simply a conflict between armies; more and more it is a struggle between competing social systems†[10] highlights the United States need for civil unity. However the anti-war movements, highlighted by the Kent State University killings as well as the ongoing debate between the ‘doves’ and the ‘hawks’, did not permit the stable and devout home front that was required to achieve victory. The final, and in a sense the most crucial, factor highlighting the importance of the Viet Cong was their strict observance to a program of logical and decisive aims. Unlike the Americans, who it seemed only aimed to â€Å"prolong the life of a corrupt and inefficient political system†[11] the NLF, of which the VC are a member, had a clear program of ambitions. Source 4 is a reliable document which illustrates such goals, the first and foremost being to â€Å"Overthrow the camouflaged colonial regime of the American imperialists and the dictatorial power of Ngo Dinh Diem.†[12] Consequently the Viet Cong’s progressive strategies were extremely important for they not only dictated the path the conflict would take, but also when and by what means they should engage in combat. In comparison to the VC’s established goals, an American author, William Broyles Jr, stated that â€Å"There was no single goal in Vietnam; there were 2.8 million goals, one for every A merican who served there†¦ the end one being to get out of Vietnam†[13] In hindsight, the dynamic role that the Viet Cong played throughout the Vietnamese conflict was vital to the Communist victory. Whilst the Viet Cong did match the large scale fighting of the NVA, its effective use of guerrilla warfare substantially crippled both the moral and fighting capabilities of the US and ARVN. Their selfless dedication to a state of ‘total war’ and their capacity to win the hearts and minds of the people essentially laid the foundations upon which Communist forces were able to launch a successful final campaign. Finally, their unwavering devotion to the Communist cause arguably provided the defining blow to the foreign imperialist’s occupation of South Vietnam. ________________ [1] ‘The Vietnam Experience; FIGHTING FOR TIME’ [2] ‘VIETNAM; THE VALOUR AND THE SORROW’ [3] http://www.spartacus.schoolnet.co.uk/ [4] ‘ATLAS OF CONFLICTS; THE VIETNAM WAR’ [5] ‘ATLAS OF CONFLICTS; THE VIETNAM WAR’ [6] ‘CONFLICT IN INDOCHINA 1954-1979’ [7] ‘Contested Spaces; CONFLICT IN INDOCHINA’ [8] ‘VIETNAM; THE VALOUR AND THE SORROW’ [9] ‘VIETNAM; THE VALOUR AND THE SORROW’ [10] ‘THE AGE OF WAR; The United States Confronts the World’ [11] ‘VIETNAM; THE VALOUR AND THE SORROW’ [12] ‘Contested Spaces; CONFLICT IN INDOCHINA’ [13] ‘ATLAS OF CONFLICTS; THE VIETNAM WAR’

Structural and Functional Properties of Tendons

Structural and Functional Properties of Tendons Chapter One Literature Review 1.0 Introduction Tendons are dynamic structures; their extracellular matrices are continuously being synthesised and broken down over the course of an individual’s lifetime. The macromolecules, namely collagen, proteoglycans, hyaluronan and the non-collagenous proteins form the extracellular matrix of tendons. In normal tendon exists a fine balance between the synthesis and degradation of these macromolecules resulting in a strong healthy tendon. It is evident that damage to tendons, such as in overuse tendinopathy results in changes to the levels and types of macromolecules present in tendon with decreased levels of collagen and increased levels of proteoglycans, hyaluronan and non-collagenous proteins, causing a weakened tendon that is prone to rupture. These degenerative features have thus far been partially characterised. By identifying the levels and various types of macromolecules present in normal tendons and tendons exhibiting overuse tendinopathy an understanding of the basis of the condition can be determined and possible ways of preventing or ameliorating tendon degeneration can be considered. The terms overuse tendinopathy and pathological tendon will be used interchangeably throughout this study. This literature review will attempt to define and characterise the structural and functional properties of tendon and will discuss the current literature regarding the levels, types, synthesis and catabolism of macromolecules present in the extracellular matrix of tendons and also attempt to define and characterise the pathological aspects of overuse tendinopathies. Chapter Two of this thesis will dictate the materials and methodology used in these studies. Chapters Three, Four and Five will present the results of this thesis. Finally, chapter Six will include the discussion and discuss any limitations and future considerations. 1.1 Synovial Joint Joints are articulations found between adjacent parts of bone that allow controlled frictionless movement (for review see; Mankin Radin, 1997). In the human body there are three different types of joints and these are grouped according to the type of movement they make. They include the freely movable joints (synovial joints; i.e., most joints of the extremities such as the knee joint), slightly movable (cartilaginous joints; i.e., the vertebrae and ribs) and those that are immovable (fibrous joints; i.e., the skull). The majority of the joints found in the human body are synovial joints (for review see; Mankin Radin, 1997). There are six different types of synovial joints including the ball-and-socket joints, hinge joints, saddle joint, pivot joint, gliding joints and condyloid joints. A synovial joint contains a joint cavity that is enclosed by a fibrous capsule linking the adjoining bones. This joint capsule is lined by a synovial membrane that secretes a lubricating and nutritious fluid called synovial fluid that is rich in albumin and hyaluronan. The surface of each bone is typically covered with articular hyaline cartilage or in some circumstances fibrocartilage. In addition, the joint capsule is supported by accessory structures such as tendons and ligaments, which provide stability to the synovial joint (Sledge et al., 2001). 1.1.1 Articular Cartilage Articular cartilage covers the adjoining ends of bones in joints and has a white colour (for review see; Mankin Radin, 1997). It is a tissue that is devoid of blood and nerves and provides a wear resistant surface with low frictional properties for the joint and attains its nutrients via diffusion from the synovium into the synovial fluid (for review see; Mankin Radin, 1997). Furthermore, articular cartilage is resilient and flexible. This allows articular cartilage to withstand large compressive and tensile forces as well as allowing it to distribute load on subchondral bone during joint loading (Kempson, 1980) even though it is only a few millimetres thick (Hardingham, 1998). Its biomechanical properties are dependent on the structural composition of the extracellular matrix, which is comprised of water (70-80%), collagens (predominantly Type II collagen), proteoglycans (predominantly aggrecan) and non-collagenous proteins (Kuettner et al., 1991; Poole, 1997). The predominant cell type present in articular cartilage is called the chondrocyte. These cells are responsible for the maintenance, synthesis and degradation of all the extracellular matrix components (Kuettner et al., 1991; Buckwalter Mankin, 1998). Mature articular cartilage can be divided up into four zones including the superficial (tangential) zone, the middle (transitional) zone, the deep (radial) zone and the zone of calcified cartilage (Huber et al., 2000). The organisation and composition as well as mechanical properties of the extracellular matrix varies within these zones. The deeper zones have high proteoglycan levels and low cellularity whereas the more superficial zones contain low proteoglycan levels and increased cellularity (Aydelotte et al., 1988; Buckwalter Mankin, 1998). 1.1.2 Joint Capsule and Ligament The joint capsule is a fibrous connective tissue that is attached to the skeletal parts of a joint beyond their articular surfaces. The principal function of the joint capsule is to seal the joint space and to supply stability by limiting movement (for review see; Mankin Radin, 1997). Most joint capsules are strengthened by ligaments. Ligaments act together with the joint capsule and the peri-articular muscles to provide stability to the joint preventing excessive movements. They permit free movements when lax, but can stop unwanted movements when tight by virtue of their high tensile strength. Occasionally joint capsules are strengthened by tendons, such as the extensor tendon in the finger joint. The joint capsule and ligaments proceed to hold the bones together and to guide and limit joint movements. Ligaments attach one bone with another bone and have a limited vascular and neural supply which enable them to repair relatively well after damage (Bray et al., 1990). The knee joint is a good example of different types of ligaments. The medial collateral ligament fuses with the joint capsule, and the cruciate ligaments and the lateral collateral ligament, which are both completely independent of the joint capsule. 1.1.3 Synovial Membrane The synovial membrane (synovium) lines the non-articular surfaces of a joint such as the joint capsule and ligaments, and is responsible for secreting and absorbing synovial fluid, which contains hyaluronan (Mason et al., 1999). Synovial fluid lubricates the joint and provides at least partly for the nutrition of articular cartilage, invertebral discs and menisci. The synovial extracellular matrix acts as a scaffolding to support synoviocytes and plays an important role in cell migration and differentiation. It is mostly composed of collagen particularly Type III collagen, with smaller amounts of proteoglycans such as decorin and biglycan (Mason et al., 1999), non-collagenous proteins such as fibronectin, elastin and lamina, hyaluronic acid as well as lipids, serum proteins and electrolytes (Hirohata Kobayashi, 1964). The synovial membrane has only been detected in vertebrate animals (Henderson Edwards, 1987). Furthermore, synovial tissue is not arranged into discrete layers, but rather represents a continuum from surface to deep zones. The extracellular matrix of the synovial membrane varies in composition from its surface to its deep zones (Hirohata Kobayashi, 1964). 1.1.4 Tendon Tendons are dense fibrous connective tissues found between muscles and bones (for review see; Benjamin Ralphs, 1997). The primary role of tendon is to absorb and transmit force generated by muscle to the bone to provide movement at a joint. In addition tendons operate as a buffer by absorbing forces to limit muscle damage. Each individual muscle has two tendons, one that is proximal and the other distal. The attachment of the proximal tendon of a muscle to bone is called a muscle origin and that of the distal tendon an insertion. A normal tendon has a bright white colour and a fibroelastic texture and enables resistance to mechanical forces. Tendons come in many shapes and this is most likely due to their function, they can be round or oval in cross section or they can come in the form of flattened sheets, fan shaped, ribbon shaped or cylindrical in shape (for review see; Benjamin Ralphs, 1997). In a muscle like the quadriceps which creates strong forces the tendons are short and broad, while those that are involved in more delicate movements like the finger flexors, long and thin tendons are present (Kannus, 2000). Tendons are arranged in a hierarchical fashion (see Figure 1.1). A group of collagen fibres form a primary fibre bundle or subfascicle; this is the basic unit of tendon. A group of subfascicles form secondary bundles or fascicles, which form tertiary bundles constituting the tendon as a whole. The primary, secondary and tertiary bundles are encased in a thin connective tissue reticulum called the endotenon (Elliott, 1965; Kastelic et al., 1978; Rowe, 1985). The endotenon carries blood vessels, nerves and lymphatics to deeper areas of the tendon (Elliott, 1965; Hess et al., 1989). The whole tendon is surrounded by an epitenon, which is a dense fibrillar network of collagen (Jozsa et al., 1991). The epitenon is contiguous with the endotenon and like the endotenon is rich in blood vessels, nerves and lymphatics (Hess et al., 1989). Many tendons are surrounded by a connective tissue called the paratenon. Paratenon allows free movement of the tendon against the surrounding tissues (Schatzker Branemark, 1969; Hess et al., 1989). The myotendinous junction is the site of union with a muscle, and the osteotendinous junction is the site of union with a bone (Kannus, 2000). In tendon, blood vessels represent between 1-2% of the entire extracellular matrix (Lang, 1960; Lang, 1963). Some blood vessels may originate from the perimysium at the musculotendinous junction and blood vessels from the osteotendinous junction (Schatzker Branemark, 1969; Carr Norris, 1989; Clark et al., 2000). At rest, rabbit tendons have been shown to have blood flow of around one-third that of muscle, and it is known that blood flow in tendon increases with exercise and during healing in animals (Backman et al., 1991). The oxygen consumption of tendons is 7.5 times lower than that of skeletal muscles (Vailas et al., 1978). 1.1.5 Tendon Extracellular Matrix The major cell type present in tendon is the fibroblast (also known as tenocytes; Ross et al., 1989; Schweitzer et al., 2001; Salingcarnboriboon et al., 2003), which are embedded within an extracellular matrix (see Figure 1.2). These cells are sparsely distributed, comprising only 5% of the dry weight of adult tendon (Ross et al., 1989; Schweitzer et al., 2001; Salingcarnboriboon et al., 2003). These cells lie in longitudinal rows and have many cell extensions that extend into the extracellular matrix (McNeilly et al., 1996). Fibroblasts are responsible for the synthesis and degradation of all the macromolecular components that make up the extracellular matrix of tendon, including the most abundant macromolecule present in tendon, collagen, as well as proteoglycans, hyaluronan and non-collagenous proteins (Vogel Heinegard, 1985; Curwin, 1997; O’Brien, 1997). The extracellular matrix is made up of parallel bundles of collagen aligned longitudinally (60-85% of tendon dry weight) associated with elastin fibres which constitutes approximately 1-2% of the dry weight of tendon (Tipton et al., 1975; Hess et al., 1989; Jozsa et al., 1989; Curwin, 1997; Kirkendall Garrett, 1997; O’Brien, 1997). Tendon consists of 55-70% water, most of which is associated with proteoglycans in the extracellular matrix (Elliott, 1965; Vogel, 1977; Merrilees Flint, 1980; Riley et al., 1994b; Vogel Meyers, 1999). The proteoglycan content of tendons is approximately 1% of dry weight of tendons (O’Brien, 1997).Water and proteoglycans have important lubricating and spacing roles in tendons that allow collagen fibres to glide over one another (Amiel et al., 1984). The structure, composition and the organisation of the tendon matrix is crucial for the physical properties that tendons posses (Riley, 2004). The collagen component gives tendon its great tensile strength (Scott, 2003) whereas it is the proteoglycan component of the tendon matrix that enables tendons to withstand compressive load (Schonherr et al., 1995), while elastin fibres increase tendon extensibility (Scott, 2003). 1.1.6 Tendon cells The cell population of tendon has so far been poorly characterised (for review see; Riley, 2000), the majority of tendon cells have the appearance of fibroblasts (also known as tenocytes) and constitute about 90-95% of the cells present in tendon (Ross et al., 1989; Schweitzer et al., 2001; Salingcarnboriboon et al., 2003). The remaining 5% to 10% of cells present in tendon are chondrocyte-like cells (fibrochondrocytes), which are mostly present in the fibrocartilaginous regions of tendon where tendon attaches to bone. Also present in tendon are some mast cells, capillary endothelial cells, smooth muscle cells and nerve cells (Hess et al., 1989; Jozsa Kannus, 1997). Fibrocartilage cells are large and have an oval shape and they are often packed with intermediate filaments (Merrilees Flint, 1980; Ralphs et al., 1991). Tendon cells are linked to one another via gap junctions (McNeilly et al., 1996; Ralphs et al., 1998), allowing cell-to-cell interactions (McNeilly et al., 1996). Fibroblasts have a branched cytoplasm surrounding an elliptical, speckled nucleus. The rough endoplasmic reticulum and the Golgi apparatus are well developed with few mitochondria in the cytoplasm (Ippolito et al., 1980; Moore De Beaux, 1987). Like other connective tissue cells, fibroblasts are derived from mesenchyme. It is believed that in tendon there are a small number of mesenchymal stem cells that have the ability to differentiate into chondrogenic, osteogenic and adipogenic cells if the conditions allow (Salingcarnboriboon et al., 2003). Tendons have been shown to respond to mechanical load by modifying their extracellular matrix (Banes et al., 1988; Ehlers Vogel, 1998; Buchanan Marsh, 2002; Lavagnino Arnoczky, 2005). Tendon cells receive their vascular supply from the surrounding paratenon. Tendons were once considered almost static and unable to participate in repair. However, the activity of tendon cells has been shown to be active throughout an individual’s life as they express various matrix components (Chard et al., 1987; Ireland et al., 2001; Riley et al., 2002). Regional differences in cell morphology and activity exists in tendons, synovial-like cells that are found in the endotenon and epitenon surround the main fibre bundles (Banes et al., 1988). A greater proliferative capacity and a different matrix synthetic activity is characteristic of these synovial-like cells compared to the fibroblasts within the fibres, and are the first cells to respond following acute tendon injury (Gelberman et al., 1986; Banes et al., 1988; Garner et al., 1989; Gelberman et al., 1991; Khan et al., 1996b). Tendon Extracellular Matrix Macromolecules The following section will discuss the major extracellular matrix proteins and their roles in tendon. This will include the major constituent of tendon, collagen, the small and large proteoglycans and the non-collagenous proteins as well as hyaluronan. This section will also discuss the synthesis of collagens, proteoglycans and hyaluronan. 1.2.1 Collagens Collagen is the most copious protein present in the extracellular matrix of connective tissues and accounts for approximately 90% of the total protein of tendons, or 65% to 75% of the dry weight of tendons (von der Mark, 1981; O’Brien, 1992). There are currently 28 different collagen types (numbered I-XXVIII) present in vertebrates with at least 42 different alpha chains (Veit et al., 2006) with this number continuing to mount (Brown Timpl, 1995; Aumailley Gayraud, 1998). Collagen molecules can be defined as an extracellular protein that contains at least one triple helical domain (van der Rest Bruckner, 1993). Collagen provides the tendon with its structural integrity as well as assisting in various physiological functions. Collagen consists of three polypeptide alpha chains, which combine to form a homotrimer (three identical alpha chains) or a heterotrimer (two or three different alpha chains). Covalent bonds known as collagen cross-links develop between individual collagen molecules in a collagen fibre (Eyre et al., 1984; Bailey et al., 1998; Bailey, 2001; Brady Robins, 2001). The collagen arrangement gives tendon its great tensile strength. Cross-links are formed from a pathway of different chemical reactions that result in divalent cross-links that join two polypeptide chains, to multivalent, i.e. tri- or even tetravalent, cross-links (Bailey Lapiere, 1973; Eyre et al., 1984). These cross-links come about from enzymatic modification of lysine or hydroxylysine residues by the copper-dependent enzyme lysine oxidase (Robins, 1988). Collagens are divided into two subgroups, the fibrillar and non-fibrillar collagens. Non-fibrillar collagens can be further divided into seven subfamilies including microfibril collagens, fibril-associated collagens with interrupted helices (FACIT) collagens, network collagens, MULTIPLEXIN collagens (proteins with multiple triple helix domains and interruptions), basement membrane-associated collagens, transmembrane-associated collagens and epithelium-associated collagens (von der Mark, 1999). The non-fibrillar collagens present in tendon include Types IV, VI, IX, X, XII and XIV (von der Mark, 1999). The fibrillar collagens present in tendon include, Types I, II, III, V and XI (Kielty et al., 1993; Kadler et al., 1996; Fukuta et al., 1998; von der Mark, 1999). The fibrillar collagens contain a continuous triple helix domain, 300 nm in length, capable of undergoing the staggered, lateral associations required to form fibrils (Mayne, 1997). The resulting fibrils provide the structural support for tissues. All the fibril-forming collagens have a similar structure and size, being composed of a large, continuous central triple-helical domain (COL1) of approximately 1000 amino-acid residues Collagen Type Structure type Distribution Function I Fibril forming Occurs in most tissues, tendon, bone, skin etc Main component of tendon, skin, bone, dentin, cartilage, ligament etc II Fibril forming Hyaline cartilage, invertebral disc Restricted to fibrocartilage; forms less-organised meshwork III Fibril forming Vessels, kidney, liver, skin, tendon Normally restricted to endotenon; forms smaller less organised fibrils IV Forms meshwork Basement membranes, tendon Basement membrane of tendon blood vessels V Fibril forming Skin, bone Core of Type I collagen fibril forms template for fibrillogenesis VI Beaded filaments Vessels, skin, intervertebral disc Cell associated found in seams between fibrils VII Epithelial-associated Dermoepidermal junction Forms anchoring fibrils in the skin VIII Microfibril Descements membrane in the cornea Forms a lattice IX FACIT Hyaline cartilage, vitreous humour, tendon Cell and matrix interactions with Type II collagen fibril surface X Forms meshwork Growth plate, tendon Restricted to insertion fibrocartilage XI Fibril forming Hyaline cartilage Core of Type II collagen fibril forms template for fibrillogenesis XII FACIT Embryonic tendon and skin, periodontal ligament Mediates cell/matrix interactions with Type I collagen fibril surface XIII Transmembrane Endothelial cells Adhesion of cells to basement membranes XIV FACIT Foetal skin, tendon Mediates cell/matrix interactions with Type I collagen fibril surface XV Multiplexin Blood vessels Stabilizes skeletal muscle cells and microvessels XVI FACIT Skin, Cartilage XVII Transmembrane Skin, cornea, lung Connects epithelial cells to the matrix XVIII Multiplexin Endothelial cells, liver, eye Needed for normal development of the eye XIX FACIT Basement membranes Forms radially distributed aggregates XX FACIT Corneal epithelium, skin, cartilage and tendon Binds to collagen fibrils XXI FACIT Many tissues Matrix assembly of vascular networks in blood vessel formation XXII Fibril forming Tissue junctions Interacts with components of microfibrils XXIII Transmembrane Metastatic tumour cells, heart retina Cell adhesion, Binds to heparin XXIV Fibril forming Expressed in tissues containing Type I collagen Developing bone and cornea Regulating Type I collagen fibrillogenesis XXV Transmembrane Neurons May play a role in adherens junctions between neurons XVI Testis and ovary of adult tissues Development of the reproductive tissues XVII Fibril forming Cartilage, ear, eye and lung Unknown XVIII Basement membranes around Schwann cells in the peripheral nervous system. Unknown flanked by a variable amino-terminal domain of about 50-520 amino acid residues and a highly conserved non-triple-helical carboxyl-terminal domain of about 250 amino acid residues (for reviews see; Kielty et al., 1993; Fichard et al., 1995; Pihlajaniemi Rehn, 1995; Prockop Kivirikko, 1995; Bateman et al., 1996). The amino- and carboxyl-terminal extensions are commonly referred to as amino- and carboxyl- propeptides, respectively. The C-propeptide is called the NC1 domain, whereas the amino-propeptide is divided into sub-domains. The first is a short sequence (NC2) that links the major triple helix to the minor one (COL2) and a globular amino-terminal end (NC3) that shows structural and splicing variations. Collagen Types II, IX, X and XI (Fukuta et al., 1998) are present at specific sites within the fibrocartilage region of tendon, found at the bone insertion and where the tendon is subjected to shear forces or compression (Fukuta et al., 1998; Waggett et al., 1998). Collagen Types II, IX, X and XI were once thought to occur only in cartilage (Visconti et al., 1996; Fukuta et al., 1998; Riley, 2000). It has now been shown that these collagens are found in the fibrocartilaginous regions of tendon, which wraps under bone. Their presumed function is to help resist compression and shear forces at these sites (Visconti et al., 1996; Fukuta et al., 1998; Waggett et al., 1998). Collagen also plays an important role in attaching tendons to bone. Where the tendon attaches to bone, tendons commonly widen and give way to fibrocartilage, a transformation where the aligned fibres originating from the tendon are separated by other collagen fibres arranged in a three dimensional network surrounding rounded cells (Liu et al., 1995). This arrangement helps to transmit tensile forces onto a broad area and reduces the chance of failure under excessive loading. The following review will focus on the collagens that are known to exist in tendon; this includes collagen Types I-VI, IX-XII and XIV. 1.2.1.1 Type I Collagen Type I collagen is the predominant and most studied collagen type present in the extracellular matrix of tendon, ligament and bone representing approximately 95% of the total collagen content or 60% of the tendon dry weight (Evans Barbenel, 1975; von der Mark, 1981; Riley et al., 1994b; Rufai et al., 1995). It is synthesized by a number of cell types such as fibroblasts, osteocytes and odontoblasts. Type I collagen consists of two ÃŽ ±1(I) chains and a shorter ÃŽ ±2(I) chain (Kielty et al., 1993), these two chains are products of separate genes and are not a posttranslational modification of a single molecule (for review see; Kivirikko Prockop, 1995). The two ÃŽ ±1(I) and one ÃŽ ±2(I) chains of a monomer of Type I collagen are primarily comprised of approximately 338  repeating tripeptide sequences of Gly-X-Y in which X is frequently proline and Y is frequently hydroxyproline (OHPr). The ends of the ÃŽ ±1(I) and one ÃŽ ±2(I) chains consist of short telopeptides of between 11-26 amino acids per chain. In longitudinal sections, the monomers are arranged in fibrils in a head-to-head-to-tail orientation. Each Type I collagen molecule consists of a long central helical region with a short non-helical domain on both the amino- and carboxyl-terminal ends. In tendon, the Type I collagen-containing fibril, organized into fibres (fibril bundles), is the major element responsible for structure stabilization and the mechanical attributes of this tissue. The fibril contains collagen molecules assembled into a quarter-staggered array, and this striated fibril has a 67 nm periodicity (for review see; Kadler et al., 1996; Orgel et al., 2006). Each alpha chain consists of a repeating triplet of glycine and two other amino acids marked as (Gly-X-Y)n. It is the glycine residues located in every third position that makes it possible for the three alpha chains to coil around the other. It has a molecular weight of 290 kDa. When viewing collagen fibrils under the light microscope they have a crimped appearance, during tendon loading the crimp stretches and the fibrils become aligned, and after loading the crimp will reappear, this is an important elastic component that tendon possesses (O’Brien, 1992). The Type I collagen ÃŽ ± chains contain approximately 290 residues of OHPr per molecule. Proline and OHPr constitute 20% to 25% of all amino acid residues of Type I collagen. The parallel arranged bundles formed by the Type I collagen fibrils gives tissues a high tensile strength with limited elasticity, and therefore is suitable for force transmission. The Type I collagen molecule has the ability to form microfibrils (filaments) as well as larger units of the fibrils or fibres (for review see; Kivirikko Prockop, 1995). The diameter of the collagen fibril is usually between 20 nm and 150 nm but can range up to 300 nm, this depends on the stage of development (Dyer Enna, 1976; Jozsa et al., 1984; Fleischmajer et al., 1988). 1.2.1.2 Type II Collagen The homotrimeric Type II collagen molecule was first discovered in cartilage by Miller and Matukas in 1969 who extracted collagen from cartilage in an experiment that involved pepsin digestion. Type II collagen, although most commonly found in articular and hyaline cartilage is also expressed in tendon particularly around the fibrocartilaginous region and consists of three identical ÃŽ ±1(II) chains (Eyre et al., 1992) which forms a meshwork structure that gives Type II collagen the ability to entrap the negatively charged proteoglycan molecules, thereby resisting the swelling pressure of proteoglycans. Each Type II collagen chain has a molecular weight of approximately 95 kDa. The entire collagen Type II molecule is shaped like a thin rod and is 300 nm long and 1.5 nm wide and has a total combined molecular weight of 295 kDa. This molecule is essential in connective tissues that are subjected to compression such as tendon and articular cartilage. Type II collagen molecules consists of a long central helical region flanked at its amino- and carboxyl-terminus by short non-helical regions termed amino and carboxyl telopeptides (Eyre et al., 1992). As with all fibrillar collagens, Type II collagen molecules are arranged in a quarter-staggered array to form collagen fibrils. Lateral associations of these collagen fibrils forms collagen fibres (Mayne, 1997). In tendon, collagen Types IX and XI as well as the proteoglycans decorin, fibromodulin and lumican inhibit collagen Type II fibril formation reducing fibril thickness (Vogel et al., 1984; Hedbom Heinegard, 1989; Hedbom Heinegard, 1993). 1.2.1.3 Type III Collagen Type III collagen is the second most abundant collagen present in tendon, representing up to 10% of the total collagen content in various tendons (Hanson Bentley, 1983; Riley et al., 1994b). Type III collagen is a thin collagen fibre consisting of three ÃŽ ±1(III) chains with a molecular weight of 290 kDa. In tendon most Type III collagen is found in the endotenon and epitenon (Duance et al., 1977), and is also found in between Type I collagen fibril bundles in aging tendons and at the insertion (Kumagai et al., 1994). It can also be found in skin, blood vessels, ligament and internal organs such as the gastro-intestinal tract but is not found in bone (Epstein Munderloh, 1978; McCullagh et al., 1980; Amiel et al., 1984). It strengthens the walls of hollow structures like the intestines and uterus. The fibrils of Type III collagen have a generally thinner diameter compared with Type I collagen fibrils (Lapiere et al., 1977; for review see; Kadler et al., 1996), however the triple helical domain is longer in length being composed of 340 amino acid repeats compared to 338 amino acid repeats in Type I collagen. In the early repair of the injured tendon, Type III collagen fibrils are quickly synthesized to restore strength and elasticity (Williams et al., 1984; Dahlgren et al., 2005). However, the fibrils do not have the same tensile strength quality as Type I collagen and so lack the functional properties needed in a tendon experiencing maximal load. The repair processes continues with Type III fibrils slowly being replaced by Type I collagen fibrils in an attempt to normalize the properties of the tendon (Duance et al., 1977; Williams et al., 1984; Dahlgren et al., 2005). Type III collagen contains high levels of OHPr and glycine. It has been reported that these high levels of glycine may cause localised helix instability resulting in increased susceptibility to proteolytic cleavage and rapid turnover of the extracellular matrices containing this collagen (Linsenmayer, 1991). The frequency of Type III collagen is considered to be an indicator of tissue age, and is common in the early stages of healing and scar tissue formation where it provides mechanical strength to the matrix (Burgeson Nimni, 1992). 1.2.1.4 Type IV Collagen The non-fibrillar collagen, Type IV (Bailey et  al., 1979), is a basement membrane-associated collagen (Light Champion, 1984) composed of triple helical isoforms consisting of six genetically distinct chains [ÃŽ ±1(IV) to ÃŽ ±6(IV)]. Each chain is characterised by a long collagenous domain of approximately 1400 amino acid residues of Gly-X-Y repeats, that are interrupted at several sites by a short non-collagenous sequence and approximately 15 amino acid residue non-collagenous amino-terminus, and an approximately 230 amino acid residue non-collagenous domain at the carboxyl-terminus (Mayne, 1997). Type IV collagen has been reported to represent approximately 2% of the total collagen content of tendon (Ahtikoski et al., 2003). Unlike the fibrillar collagens discussed so far this collagen does not form fibrillar aggregates but are directly incorporated into the basement membrane without any prior excision of the pro-peptide extensions. Type IV collagen is found uniquely in the basement membrane of tendon blood vessels (von der Mark, 1981) where it forms a key structural compo

The Myth Of Mental Illness Philosophy Essay

The Myth Of Mental Illness Philosophy Essay Has Psychiatry got it that wrong or is Thomas Szazs deluded. This question begs to be answered throughout the pages of the The Myth of Mental Illness. Thomas Szazs boldly lays bare psychiatric fallacies in about 263 pages, with ambitious agenda, which has had a significant imprint on Psychiatric history irrespective of all attempts to relegate it to the annals of history (Buchanan-Barker and Barker, 2009). Szazs whose work is used freely by psychiatric academics is often referred to as Psychiatric Philosopher (Hoeller, 1997 and Breeding, 2011). The main argument of this book is that mental illness is a social construct and what psychiatrists label as mental illness is in fact deviant behaviour (Szazs, 2010). Furthermore, Szasz believes that in the absence of empirically observable biological pathology, certain mental illnesses such as schizophrenia should not be termed an illness. Mental illness has no scientific or medical basis and therefore cannot be called a disease. This hypothesis is based on the premise that unlike pneumonia which presents recognisable symptoms all over the world, mental illness does not. Hallucination is classified as a disorder in the western world but highly valued in other parts of the world (Szazs, 2010). The book is academic, aimed at challenging the foundations of American Psychiatry and perhaps the words of Benjamin Rush who declared in the 18th Century that mental illness has hitherto been shrouded in mystery and his intension to make mental illness like any disease of the human body (Szasz, 2005). Part one, The Myth of Mental Illness is an analysis of the background of 1950 psychiatric theory and practice. Part two, Foundations of a Theory of Personal Conduct proffers an alternative stance on mental illness and how to eloquently express views about it. Szazs firmly believes that mental illness does not exist and that the notion of illness only applies to bodily abnormalities that can be proved by physical and chemical methods (Szasz, 2010). In Mental illness the brain when dissected does not reveal an ailing part. Therefore, internal or neurological illness should not be suggested even if the mental illness resembles physical illness because in such a case mental illness should be viewed as a metaphor (Pickering, 2006). Farrell (1979) however vies this strand of argument positing that Szazs point disintegrates when it is acknowledged that mental illness can refer to psychological defects. Szasz further argues that until recently, illness was defined as a physical disorder and had to be physically and chemically proven in the structure of a body. New diseases have conformed to this criteria and therefore Psychiatry should not be an exception (Pickard, 2009). Szasz marries structural and functional aberrations consequently combining function and behaviour. The function of the brain, for example or the brain systems are placed in the same category as the behaviour of a person and compared to physical and chemical changes. In todays scientific world this view is difficult to digest. Szasz propounds that somatic symptoms should not be attributed to physio-chemical defects in the body as this disorder is learned. This argument casts a shadow on all other mental illnesses and subsequently renders all Psychiatric terminology, diagnosis and treatment needless. Psychiatry is not medical intervention but a social and moral service which should not be forced on anyone (Szasz, 2010). The other premise of Szaszs argument is that medical diagnosis is subject to a physician judgement. This judgement usually correlates with the demonstration of a corresponding physiochemical disorder which cannot be applied in mental health. Psychiatrists therefore make diagnosis which cannot be verified. This gives the psychiatrist power over the patient as the psychiatrist is the only one who can verify this illness. Mental illness in the eyes of Szasz is not discovered as with other natural illnesses but invented by psychiatrist from peoples behaviours (Szazs, 2010). Szazs proffers that whereas mentally ill people were classified as malingerers some years back they are now seen as patients entitled to privileges and welfare benefits. This is not necessarily an improvement but a ploy that negatively affects the value of life which in effect revert mentally ill people social status to malingerers of the 21st century. Such a label induces stigma, discrimination, lame excuses for failure and bad behaviour. Some of these views are not akin to only Szasz. Bracken and Thomas (2010) elucidates how Michael Foucault a French philosopher and Szasz have challenged leading views on psychiatry. Foucault like Szazs asserts that mentally ill people are institutionalised because of moral and economic factors. Furthermore, he challenges deep-seated opinions of mental illness, reason and questions why leper houses were replaced with institutions for mentally ill people (Foucault, 2006). Influenced by post philosophers such as Michael Heidegger, Foucaults transformative practice, knowledge that contravenes dominating games of truth, power relations and shades of partiality is closely knitted to the philosophy of Heidegger (Rayner, 2007). However, Ratcliffe (2010) challenges Bracken and Thomass critique of arguments between Foucault and Szazs stating that they are worlds apart. Gijswijt-Hofstra and Porter (1998) asserts that even though there are other critics of psychiatry their views are often ambiguous. Critics such as Ronald Laing, a Scottish psychiatrist decisively wrote about mental illness subscribing to the view that madness was a natural way of ridding oneself from infuriating situations. Therefore, psychotic episodes should be allowed to run its natural courses rather than people being degraded by being arrested, curbed, confined and forcibly medicated in hospitals (Laing, 1986). Scott (2011) decries Gijswijt-Hofstra and Porters point by indicating that Laings views for example about mental healthcare and choice is not out of date or insignificant. Thomas Szazs, Michel Foucault, David Cooper and Ronald Laing may have contributed enormously to intellectual debates on mental patient care and choice but I beg to differ because of inequality in societies and the lack of resources to support and protect the dignity and life of the mentally ill and the community they live in. Where lies dignity when the mentally ill become dishevelled, vagrant and walk about stark naked in places like Africa? Regardless of the above, the strengths of this book although ambiguous at times outweigh its weaknesses. The hardnosed attitude towards patient care and choice makes a must reading for every psychiatric student as it brings to the fore challenging questions about diagnosis and the expansion of the Diagnostic and Statisical Manual of Mental Disorders.

Airships :: essays research papers

Airships INDEX PROLOGUE 2 TYPES OF AIRSHIP 2 RIGID AIRSHIP 2 NONRIGID AIRSHIP 3 HISTORY OF RIGID AIRSPS 3 HISTORY OF NONRIGID AIRSHIPS 4 AIRSHIPS TODAY 5 HINDENBURG 6 HINDENBURG DISASTER 7 PROLOGUE An airship is a type of lighter-than-air aircraft with propulsion and steering systems, it is used to carry passengers and cargo. It obtains its buoyancy from the presence of a lighter-than-air gas such as hydrogen or helium. The first airship was developed by the French, called a ballon dirigible, it could be steered and could also be flown against the wind. TYPES OF AIRSHIP Two basic types of airship have been developed: the rigid airship, the shape of which is fixed by its internal structure; and the nonrigid blimp, which depends on the pressure created by a series of air diaphragms inside its gas space to maintain the shape of its fabric hull. Inventors sought to combine the best features of these models in a semirigid type, but it met with only limited success. Today only the nonrigid airship is used. Rigid Airship The rigid airship's structure resembled a cage that enclosed a series of balloons called gas cells. These cells were tailored to fit the cylindrical space and were secured in place by a netting that transmitted the lifting force of their gas to the structure. Each gas cell had two or more valves, which operated automatically to relieve pressure when the gas expanded with altitude, the valves could also be operated manually so that the pilot could release gas whenever desired. Also on board was a ballast system that used water as ballast. On the ground this ballast served to make the airship heavier than air. When part of it was released, the airship ascended to a cruising altitude where the engines supplied propulsion, and further ballast could be released to gain more altitude. As fuel was consumed, the airship became lighter and tended to climb. This was countered in hydrogen-inflated airships by simply releasing gas into the atmosphere. The method was uneconomical, however, with helium-inflated airships, and they were therefore equipped with ballast generators, apparatuses that condensed moisture out of the engines' exhaust gases to compensate for fuel that was consumed. But this ballast-generating equipment was expensive, complex, heavy, and difficult to maintain and was thus one of the most serious disadvantages of airships filled with the safer but more expensive helium. Nonrigid Airship In contrast to the rigid airship, the nonrigid blimp has no internal structure to maintain the shape of its hull envelope, which is made of two or three plies of cotton, nylon, or dacron impregnated with rubber for gas tightness. Inside the gas space of the hull are two or more air diaphragms called ballonets that

Extinct Animals Research: Woolly Mammoth :: essays research papers fc

Extinct Animals Research: Woolly Mammoth   Ã‚  Ã‚  Ã‚  Ã‚  We have learned much about the Woolly Mammoth almost more than any other dinosaur that has been identified. Due to the fact that the Woolly Mammoth so closely resembles today's elephants, care for them would most probably require most of the same factors to keep it alive. Since the Woolly Mammoth has been extinct for 4000 years, it is difficult to tell exactly what they lived on, but we can hypothesize.   Ã‚  Ã‚  Ã‚  Ã‚  The Woolly Mammoth lived during the Ice Age, so if alive today, it must be kept in a tundra environment. For food, only basic tundra vegetation is necessary. Due to the thick pelt that the Woolly Mammoth has, any known Ice Age temperatures would suffice since the thick fur protects the animal in any extreme temperatures.   Ã‚  Ã‚  Ã‚  Ã‚  Large enclosures would not be needed as they would be for a normal elephant since the Woolly Mammoth is only three meters high. The huge tusks would allow it to scavenge for its own food, so no special feedings would be necessary. Feedings would also be needed on a less frequent basis since the Woolly Mammoth, much like today's camels, keeps under its sloping back a thick layer of blubber as nutrition when food was not needed.   Ã‚  Ã‚  Ã‚  Ã‚  The problem in keeping a creature such as the Woolly Mammoth in a zoo- like surrounding would be poachers. Due to the endangerment of such a magnificent species, poachers of pelts and ivory would most certainly be after it's huge tusks and thick furs, so it would be necessary to post guards around it's cage at all times.   Ã‚  Ã‚  Ã‚  Ã‚  A large-scale habitat would be constructed for this creature since, during the period it lived, the Pleistocene, there were no restrictions on the places it could roam to. There was nothing stopping this beast from stomping along to wherever it wanted to go. A Woolly Mammoth might find it peculiar to be stuck in a twenty foot ice field with no predators or other animals whatsoever.

Importance of Sports Essay

Sports such as football or baseball involve lots of physical activities. Sports and exercises help in strengthening and toning the muscles and bones in the body. In short, the importance of sports for kids is that it keeps them in an excellent shape. When children or adults plays team sports, be it cricket or hockey, they learn to work in groups. They learn that if the team wins, they win and if the team loses, they lose. This way they learn how to work in groups. Thus, the importance of sports for kids is that they understand what is team spirit and thus, when they grow and actually start working, it will help them immensely in building relationships with their co-workers, and also to work in harmony with others. Sports makes people mentally strong. Success and failure are both parts of sports as well as life. A sportsman knows that there will be times when he will win matches, there will also be times when he will lose them. A sportsperson knows how to handle defeat and thus, treats success and failure equally. This is an important life lesson too, which sports can teach a person. Besides this, another importance of sports for children or for adults is that it teaches them how to handle competition, and be fearless when facing the adversaries. Children and adolescents ooze with physical energy. When they are involved in sports, their physical energies are used up in a constructive way. Teenage is such an impressionable age, if adolescents are given free time they might get involved in wrong activities or may fall in bad company or may also display anti-social behavior. Thus, the importance of sports in society is that it keeps adolescents from becoming anti-social elements, who might otherwise disturb the delicate fabric of society. Here’s hoping that now you know what is the importance of sports. Besides being important for kids, taking up a sports career in adult life, has its own benefits. A sportsperson often travels to other countries to play matches and in the process, learns a great deal about the cultures of these countries. Even the spectators or TV viewers are thoroughly entertained while watching professional sports, making it an excellent recreational activity.

Economy of Russian

In recent times, Russian presses have been full of articles analyzing the Russian economy and making forecasts, most of them pessimistic. Many would say the Russian economy has failed miserably in the past one hundred years. After the 1917 Revolution, an attempt was made by the Communists to create an economy based on socialist principles. The thought was that the capitalist system led to a chaotic economy, cruel exploitation of workers and unemployment. The Russian socialist economy rests on the basic principles formed by Karl Marx: A centrally planned economy. This â€Å"planned economy† would be in use for the next sixty years. â€Å"In 1929-1930, under the process of collectivization, the land of Russia became state-owned and cooperatively-owned. There was no longer any private land ownership.† (Torchinsky, 48) The state became the monopolist of the economy. Economy planning bodies worked out the famous â€Å"Five-year plans.† The plans regulated everything from production of aircraft to nails and even eggs. They believed that since the means of production belonged to the state, and hence, collectively, to the people, (because a socialist state is a state belonging to the people) the state should control everything. This was to include planning, financing, and salaries. Under this system, â€Å"people are to be content and peacefully work for the benefit of society.† (Diller, 168) The Socialist economic theory assumed that people would work hard because they were working for the collective good, and hence their own good; therefore there would be no reason for them to be lazy or dishonest. Thus, the defects of capitalism would not show its face. â€Å"The five-year economic plans would make it possible to wisely distribute society†s resources and to promote development.† (Flint, 17) However, over the long term, this style of economy seems to have failed in Russia. At certain times-for instance, in restoring the national economy after World War 1, the Civil War, and World War II, â€Å"The states rigid economic monopoly achieved certain successes, but later the basic principles of socialist economic management became an insuperable obstacle blocking economic progress in the Soviet Union and in Russia.† (Flint, 12) Abolishing private ownership of businesses and land killed people†s desire to succeed or to create and increase their own property. The driving force of personal gain was absent from all work activity by the people. The socialist lifestyle assumed that tireless and selfless labor for the benefit of society would succeed. Under this system, there was no reason for the common man, or anyone who was not a fanatical supporter of socialism, to work hard or to improve or create anything. Everything disappeared into the state†s bottomless pockets. â€Å"A person could work well or badly-either way, he received the same meager wages.† (Torchinskii, 51) Many people were satisfied, but some did not work for many years, yet were still guaranteed their wages or salaries by the state. Centralized planning also had a ruinous effect. â€Å"Workers and peasants merely had to fulfill the orders passed from ‘above† regardless of their practicality.† (Hughes, 33) This sometimes resulted in goods being produced that no one needed and seed being sown into barren or frozen soil. Personal initiative was neither encouraged nor expected. As the years passed, the economic situation steadily worsened. For some time, â€Å"the country lived on ‘petrodollars† by selling oil and gas at low prices.† (Flint, 19) Rivalry in the arms race with the United States devoured tremendous wealth; plus a lot of money and energy was spent on supporting â€Å"friendly Communist regimes in Asia, Africa, the Caribbean, and Central and South America.† (Flint, 19) At the 28th Party Congress in 1991, when the delegates started talking at last about the critical economic situation and the necessity of reforms, it was already too late. â€Å"The collapse of the Soviet Union in the early 1990†³s, and the rupture of economic ties between the former Soviet republics that once constituted an economic whole exacerbated the economic downslide, which rapidly became critical.† (Diller, 121) In the early 1990†³s, production continued to decline. Economic contacts weakened with other republics of the former Soviet Union. The balance of payments crisis increased. There was a lack of funds, especially hard currency, necessary for purchasing raw materials. â€Å"As a result of inflation, the purchasing capacity of the population fell and inventories grew.† (Torchinskii, 51) Although the situation in Russia is very difficult, positive aspects offer hope for a recovery. The privatization process in different industries is progressing, though with great difficulties. The agricultural industry is waiting for the transference of land to the peasants-a very risky step that could either save the country or ruin it completely. Russia has to create a successful agricultural base to thrive economically. â€Å"As of July 1, 1993, the number of private farms in Russia was 258,000; they occupied a territory of 27 million acres.† (Flint, 33) Most farmland is still controlled by former state farms or collectives, but now they are reconstructed to be joint-stock companies. Agricultural output and grain production has been declining since the early 1990†³s. Russia†s military defense industry includes aircraft building, rocket manufacturing, and the space industry. In all of these industries, Russia has a major place in the world market. Russia is also a leading arms producer and supplies countries all over the world. One of the most widely used assault rifles, the AK47, was even invented in Russia. â€Å"This remains the basic weapon of the Russian Army and of many other Communist countries.† (Hughes, 53) Finally, the country has immense manpower-the people who are able and want to work despite many decades of nearly losing the habit. There can be no doubt that regeneration is not far away. â€Å"Russia†s labor resources constituted 86.2 million people in 1992, or 58 percent of the population.† (Flint, 65) In 1993, this number was 85.7 million. The number of people in Russia that are actually employed has been dropping steadily since the early 1990†³s. In conclusion, the economy of Russia is by no means the epitome of a great economy, but many of the resources they have do help. Many people have tried to help boost the Russian economy, (Gorbachev, Stalin, Lenin, Yeltsin, and the Tzar) but all of them had their many moments of failures. The new â€Å"Commonwealth of Independent States† or the CIS has worked hard to make new plans for an economy that can rise to the occasion and become the best it has ever been before. With their abundance of natural resources, manpower, and knowledgeable people, Russia can become a major power quickly, but all they need is a guiding hand.