Collagen in granulation tissues.
Collagen is abundantly synthesized in granulation tissues and reaches a concentration higher than in normal neighbouring tissues. Such newly formed collagen is characterized by an abnormally low solubility and an easy degradation by collagenases and collagenolytic cathepsins. The activities of these two types of enzymes are high (especially collagenases) in tissues of acute inflammations when the granuloma is resorbing. These activities are lower in sub-acute inflammation and the collagen content of the persistent granuloma remains high. The collagen synthesized in granulation tissues is cross linked by hydroxylysino-5-keto-norleucine, the stable cross-link of collagen in embryonic skin. It is progressively replaced by the two aldimine cross links of normal adult skin when the granuloma is resorbed (acute inflammations induced in rats; human normal scars). The cross link of embryonic skin, on the contrary, is permanently present in collagen of tissues of subacute, chronic inflammations (sponge implants in rats, human hypertrophic scars and keloids. Studies of the structure of alpha-chains revealed that type III collagen (embryonic collagen) is present in granulation tissues.
D000818:Animals; D002403:Cathepsins / Q000378:metabolism; D005591:Chemical Fractionation; D003094:Collagen / Q000032:analysis / Q000096:biosynthesis*; D006097:Granulation Tissue / Q000378:metabolism*; D007249:Inflammation / Q000139:chemically induced / Q000201:enzymology; D003012:Microbial Collagenase / Q000378:metabolism; D051381:Rats; D014425:Turpentine / Q000494:pharmacology
D003094:Collagen; D002403:Cathepsins; D003012:Microbial Collagenase; D014425:Turpentine