BIOSYNTHESIS AND MATURATION OF SKIN COLLAGEN IN SCLERODERMA, AND EFFECT OF D-PENICILLAMINE
BIOSYNTHESIS AND MATURATION OF SKIN COLLAGEN IN SCLERODERMA, AND EFFECT OF D-PENICILLAMINE
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DOI：
10.1016/s0140-6736(74)92494-5
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发表时间：
1974-01-01
期刊：
影响因子：
168.9
通讯作者：
BAILEY, AJ
中科院分区：
文献类型：
--
作者：
HERBERT, CM;JAYSON, MIV;BAILEY, AJ
对活动性硬皮病患者皮肤胶原蛋白的分析显示，存在高比例的可还原醛亚胺键交联。这些分子间交联，这是负责胶原纤维的高拉伸强度，被取代的更稳定的不可还原的交联在成熟过程中。因此，成年患者皮肤中可还原交联的存在确定了新的胶原蛋白正在皮肤中沉积。在老年斑块和非活动性疾病的中心缺乏可还原的交联，表明患病皮肤比正常皮肤成熟得更快。由于硬皮病的症状部分是由于皮肤增厚和僵硬，新形成的胶原蛋白的不稳定交联的裂解可以软化皮肤并缓解症状。D-青霉胺可以裂解键并部分抑制胶原蛋白合成，在两个病例中，发现在疾病的活动状态下治疗在临床和生化方面有效。在非活动性疾病中观察到不同的模式，在此阶段D-青霉胺没有帮助。
Analysis of skin collagen from patients with active scleroderma revealed the presence of a high proportion of reducible aldimine bond cross-links. These intermolecular cross-links, which are responsible for the high tensile strength of collagen fibres, are replaced by more stable non-reducible cross-links during maturation. Hence the presence of the reducible cross-links in the skin adult patients establishes that new collagen is being laid down in the skin. The absence of reducible cross-links in the centre of older plaques and in inactive disease, suggests that the diseased skin matures more rapidly than normal skin. Since the symptoms of scleroderma are partly due to thickening and rigidity of the skin, cleavage of the labile cross-links of newly formed collagen may soften the skin and relieve the symptoms. D-penicillamine can cleave bonds and partially inhibit collagen synthesis, and in two cases treatment in the active state of the disease was found to be clinically and biochemically effective. A different pattern was observed in inactive disease, and at this stage D-penicillamine is not helpful.