肉芽组织中的胶原蛋白。

Collagen in granulation tissues.

作者信息

Bazin S, Le Lous M, Delaunay A

出版信息

Agents Actions. 1976 Feb;6(1-3):272-6. doi: 10.1007/BF01972221.

DOI:10.1007/BF01972221

PMID:181969

Abstract

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.

摘要

胶原蛋白在肉芽组织中大量合成，其浓度高于相邻的正常组织。这种新形成的胶原蛋白具有异常低的溶解度，并且容易被胶原酶和胶原分解组织蛋白酶降解。当肉芽肿吸收时，这两种酶的活性在急性炎症组织中较高（尤其是胶原酶）。在亚急性炎症中，这些活性较低，持续肉芽肿的胶原蛋白含量仍然很高。肉芽组织中合成的胶原蛋白通过羟赖氨酰-5-酮-正亮氨酸交联，这是胚胎皮肤中胶原蛋白的稳定交联。当肉芽肿吸收时（大鼠诱导的急性炎症；人类正常疤痕），它逐渐被正常成人皮肤的两个醛亚胺交联所取代。相反，胚胎皮肤的交联永久存在于亚急性、慢性炎症组织的胶原蛋白中（大鼠海绵植入物、人类增生性疤痕和瘢痕疙瘩）。对α链结构的研究表明，III型胶原蛋白（胚胎胶原蛋白）存在于肉芽组织中。