Effects of singlet oxygen on the extracellular matrix protein collagen: Oxidation of the collagen crosslink histidinohydroxylysinonorleucine and histidine
Effects of singlet oxygen on the extracellular matrix protein collagen: Oxidation of the collagen crosslink histidinohydroxylysinonorleucine and histidine
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DOI：
10.1006/abbi.2000.2070
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发表时间：
2000-12-01
影响因子：
3.9
通讯作者：
Madison, SA
中科院分区：
文献类型：
--
作者：
Au, V;Madison, SA
据报道，单线态氧（一种假定的皮肤光损伤因子）与真皮胶原交联组氨酸羟赖氨酸正亮氨酸（HHL）及其前体组氨酸发生反应。使用纯化的 HHL 和牛真皮组织进行反应研究。我们证明单线态氧可以选择性氧化真皮组织中的 HHL 和组氨酸氨基酸残基，并且组氨酸的中间氧化产物会产生新的交联产物。提出了一种新的交联形成机制，涉及对由组氨酸咪唑部分的单线态氧氧化形成的瞬时咪唑酮中间体进行亲核加成。胶原蛋白中这种加合物形成和组氨酸氧化的含义是异常胶原交联的表达、真皮胶原功能的扰动，以及因此改变的真皮状态。 (C) 2000 年学术出版社。
The reaction of singlet oxygen, a putative agent of skin photodamage, with the dermal collagen crosslink histidinohydroxylysinonorleucine (HHL) and its precursor histidine is reported. Reaction studies were performed with both purified HHL and bovine dermal tissue. We demonstrate that singlet oxygen can selectively oxidize HHL and histidine amino acid residues in dermal tissue and that intermediate oxidation products of histidine lead to new crosslink products. A novel mechanism for crosslink formation was proposed to involve nucleophilic addition to a transient imidazolone intermediate formed from singlet oxygen oxidation of the histidine imidazole moiety. The implication for such adduct formation and histidine oxidation in collagen proteins is the expression of aberrant collagen crosslinks, perturbation of the dermal collagen function, and hence an altered dermal state. (C) 2000 Academic Press.