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Surface collagen

Figure 3.24. Diagram of the collagen fibrils in cartilage, collagen fibrils in cartilage are composed of a core of types XI and II collagen with zone type IX on the surface. Collagen fibrils are connected to each other and to the cell surface by proteoglycans. Figure 3.24. Diagram of the collagen fibrils in cartilage, collagen fibrils in cartilage are composed of a core of types XI and II collagen with zone type IX on the surface. Collagen fibrils are connected to each other and to the cell surface by proteoglycans.
Staatz WD, Walsh JJ, Pexton T, Santoro SA The a2pi integrin cell surface collagen receptor binds to the al(I>CB3 peptide of collagen. J Biol Chem 265 4778-4781,1990... [Pg.92]

Skeletal tissue mineralization (bone formation) is initiated by osteoblasts, which secrete the osteoid matrix (Fig. 9.4). They express type I procollagen in secretory vesicles together with matrix vesicles that pinch off from the membrane. The matrix vesicles are pushed away from the cell surface, possibly by the flow of fluid containing calcium and phosphate ions that are also transported through the cell from the extracellular fluid on the outer surface. Collagen fibers develop further away from the cell surface than from fibroblasts. [Pg.134]

Airway cross-sections have the nominal anatomy shown in Fig. 5.16. Airway surface liquid (AST), primarily composed of mucus gel and water, surrounds the airway lumen with a thickness thought to vary from 5 to 10 mm. AST lies on the apical surface of airway epithelial cells (mostly columnar ciliated epithelium). This layer of cells, roughly two to three cells thick in proximal airways and eventually thinning to a single cell thickness in distal airways, rests along a basement membrane on its basal surface. Connective tissue (collagen fibers, basement membranes, elastin, and water) lies between the basement membrane and airway smooth muscle. Edema occurs when the volume of water within the connective tissue increases considerably. Interspersed within the smooth muscle are respiratory supply vessels (capillaries, arteriovenous anastomoses), nerves, and lymphatic vessels. [Pg.200]

The properties described above have important consequences for the way in which these skeletal tissues are subsequently preserved, and hence their usefulness or otherwise as recorders of dietary signals. Several points from the discussion above are relevant here. It is useful to ask what are the most important mechanisms or routes for change in buried bones and teeth One could divide these processes into those with simple addition of new non-apatitic material (various minerals such as pyrites, silicates and simple carbonates) in pores and spaces (Hassan and Ortner 1977), and those related to change within the apatite crystals, usually in the form of recrystallization and crystal growth. The first kind of process has severe implications for alteration of bone and dentine, partly because they are porous materials with high surface area initially and because the approximately 20-30% by volume occupied by collagen is subsequently lost by hydrolysis and/or consumption by bacteria and the void filled by new minerals. Enamel is much denser and contains no pores or Haversian canals and there is very, little organic material to lose and replace with extraneous material. Cracks are the only interstices available for deposition of material. [Pg.92]

The ability of these peptidomimetic collagen-structures to adopt triple helices portends the development of highly stable biocompatible materials with collagenlike properties. For instance, it has been found that surface-immobilized (Gly-Pro-Meu)io-Gly-Pro-NH2 in its triple-helix conformation stimulated attachment and growth of epithelial cells and fibroblasts in vitro [77]. As a result, one can easily foresee future implementations of biostable collagen mimics such as these, in tissue engineering and for the fabrication of biomedical devices. [Pg.24]

The collagen shield, fabricated from procine scleral tissue, is a spherical contact lens-shaped film whose thickness can be made to vary from 0.027 to 0,071 mm. It has a diameter of 14.5 mm and a base curve of 9 mm. Once the shield is hydrated by tear fluid and begins to dissolve, it softens and conforms to the corneal surface. Dissolution rates can be varied from 2 to as long as 72 hr by exposing the shields to ultraviolet radiation in order to achieve varying degrees of crosslinking. [Pg.236]

Molecules released by exocytosis fall into three categories (1) They can attach to the cell surface and become peripheral proteins, eg, antigens. (2) They can become part of the extracellular matrix, eg, collagen and glycosaminoglycans. (3) They can enter extracellular fluid and signal other cells. Insulin, parathyroid hormone, and the catecholamines are all packaged in gran-... [Pg.430]

The same ceUs that secrete collagen also secrete fi-bronectin, a large glycoprotein present on cell surfaces, in the extracellular matrix, and in blood (see below). Fi-bronectin binds to aggregating precollagen fibers and alters the kinetics of fiber formation in the pericellular matrix. Associated with fibronectin and procollagen in... [Pg.537]

Chondronectin May play role in binding type II collagen to surface of cartilage. [Pg.551]

The cornea is the first structure of the eye to be in contact with incident light. It is composed of five distinct layers lying parallel to its surface the outer epithelium, which is continuous with the epithelial layers of the conjunctiva the epithelial basal lamina the keratocyte-containing stroma, which is a collagen structure arranged so that it is transparent Descemet s membrane and, finally, the endothelium adjacent to the aqueous humour. [Pg.128]


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See also in sourсe #XX -- [ Pg.26 ]




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