Collagen partially-degraded

Fig. 21 Bone tissue and membranes 3 weeks after implantation of (a) pure chitosan membrane and (b) chitosan/silica xerogel hybrid membrane. For the histomorphometric analysis, the defect sites were observed at high magnification. The pure chitosan membrane was partially degraded and the remaining part (arrows) was surrounded by collagen fibers (blue), bone marrow, and osteocyte cells (red), as shown in (a). However, the hybrid membrane was almost completely degraded and the defect site (arrows) was replaced by a large number of collagen fibers and fresh new bone (blue), as shown in (b) [216]...

Besides the acceptor collagen, several glycoproteins were tested for acceptor activity, including partially degraded preparations from which sialic acid and galactose had been removed. Only one such preparation, ob-... 

Gelatin is the most widespread water-soluble protein in the body, resulting from partial degradation of water-insoluble collagen. Gelatin has widely... 

With respect to collagen degradation, two zones can be distinguished within a lesion. The innermost layer is partially demineralized and still recalcifiable, and contains intact collagen fibrils. In the outermost layer, however, the integrity of the fibrils and the capacity for remineralization are lost (Ohgushi and Fusayama, 1975). 

HLE demonstrates a vast array of biologic activities besides the degradation of elastin. A partial, and by no means inclusive, list of some of these activities includes degradation of fibronectin [11], laminin [12], collagen and proteoglycans [13], and immunoglobulins (IgM, IgA and secretory IgA) [14] the activation and hydrolysis of complement components and neutrophil complement receptors [15] stimulation of mucus secretion and induction of mucous gland hypertrophy [16] and decreases in ciliary beat frequency and mucociliary clearance [17]. 

Barnes, M. J., Constable, B. J., Morton, L. F., and Kodicek, E., 1970, Studies in vivo on the biosynthesis of collagen and elastin in ascorbic acid-deficient guinea pigs. Evidence for the formation and degradation of a partially hydroxylated collagen, Biochem. J. 119 575-585. 

Heparanase and type IV collagenase activities were assessed by a method described previously [17]. Briefly, H-labeled heparin sulfate (HS) was incubated at 37°C with partially purified heparanase in the presence or absence of chitin derivatives. [ H]HS degradation products in the supernatant were analyzed by size-exclusion chromatography. Heparanase activity was determined by measuring the radioactivity of each fraction. H-labeled type IV collagen was incubated at 37°C for 48 h in the presence or absence of chitin derivatives. Type IV collagenolytic activity was calculated from the radioactivity in the supernatant. 

Fig. 8 in a SCM-chitin III concentration-dependent manner. CM-chitin showed no inhibitory effect at a concentration of 500 xg/mL. SCM-chitin III inhibited HS degradation by partially purified heparanase from B16-BL6 cells as did heparin in a concentration-dependent manner (Fig. 9), whereas CM-chitin had little influence at any of the indicated concentrations, except that of 1000 p.g/mL. On the other hand, degradation of H-labeled type IV collagen was inhibited over a 24-h period by more than 75% after treatment with 400 xg/mL of SCM-chitin III and approximately 20% inhibition after treatment with heparin. Little inhibition was shown by CM-chitin. A summary of the biological functions of SCM-chitin III and heparin are listed in Table 5. 

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