COLLAGEN-MEDIATED PLATELET-AGGREGATION - EVIDENCE FOR MULTIVALENT INTERACTIONS OF INTERMEDIATE SPECIFICITY BETWEEN COLLAGEN AND PLATELETS
COLLAGEN-MEDIATED PLATELET-AGGREGATION - EVIDENCE FOR MULTIVALENT INTERACTIONS OF INTERMEDIATE SPECIFICITY BETWEEN COLLAGEN AND PLATELETS
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DOI：
10.1172/jci108856
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发表时间：
1977-01-01
影响因子：
15.9
通讯作者：
CUNNINGHAM, LW
中科院分区：
文献类型：
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作者：
SANTORO, SA;CUNNINGHAM, LW
先前的研究表明，胶原蛋白碳水化合物的高碘酸盐氧化不会影响其聚集血小板的能力。描述了高碘酸盐修饰的胶原蛋白的另一个特征，该特征表明缺乏完整碳水化合物的胶原蛋白完全能够形成原纤维，并且证实了其引发血小板[人类]聚集的能力。尽管碳水化合物含量和氨基酸序列不同，但 I、II 和 III 型纤维状胶原的血小板聚集能力非常相似。单体、胃蛋白酶溶解的 I 型人类胶原蛋白无法有效抑制源自同一分子的预形成原纤维的聚集，这表明血小板对胶原蛋白的亲和力取决于胶原蛋白的先前聚合。胶原蛋白的羟赖氨酰糖苷区域显然不是涉及导致生理聚集的血小板-胶原蛋白相互作用的高度特异性位点，并且必须考虑到涉及结构特异性相对较低的胶原蛋白位点的多重相互作用可能是血小板ADP释放和随后聚集的起始事件。
It was shown previously that periodate oxidation of collagen carbohydrate does not affect its ability to aggregate platelets. An additional characterization of periodate-modified collagen is described which demonstrates that collagen devoid of intact carbohydrate is fully capable of fibril formation, and its capacity to initiate platelet [human] aggregation was confirmed. Platelet aggregating abilities of Types I, II, and III fibrillar collagen are quite similar despite differences in carbohydrate content and amino acid sequence. Monomeric, pepsin-solubilized Type I human collagen was ineffective in inhibiting aggregation by preformed fibrils derived from the same molecule, establishing that the affinity of platelets for collagen depends upon prior polymerization of collagen. The hydroxylysyl glycoside regions of collagen are apparently not highly specific sites involved in platelet-collagen interactions leading to physiological aggregation, and the possiblity must be considered that multiple interactions involving collagen sites of comparatively low structural specificity may be the initiating events in release of platelet ADP and the ensuing aggregation.