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Studies on the function and biosynthesis of oxodesmosine, new cross-linking amino acid of elastin

弹性蛋白新型交联氨基酸氧化锁链素的功能及生物合成研究

基本信息

批准号：
04660301
负责人：
SUYAMA Kyozo
金额：
$ 1.34万
依托单位：
Tohoku University
依托单位国家：
日本
项目类别：
Grant-in-Aid for General Scientific Research (C)
财政年份：
1992
资助国家：
日本
起止时间：
1992 至 1993
项目状态：
已结题

来源：
https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-04660301/
关键词：
Oxodesmosine Isooxodismosine Elastin Crosslink Amino Acid Desmosine 架〓アミノ酸大動脈

项目摘要

Elastin is one of the connective tissue protain found in virtually every tissue and organs of mature animals and is major constituent of blood vessels and certain ligaments and other compliant tissues such as lung and skin. Elastin is primarily synthesized during physiological development by such cells as the vascular smooth muscle and fibroblast as a soluble precursor, tropoelastin. Several pairs of deaminated lysyl residues in each tropoelestin molecule are involved in a set of spontaneous condensation reactions that lead to the formation of crosslinking amino acids. In our experiments, we isolated two new crosslinking amino acids having N-substituted dihydrooxopyridine structure named oxodesmosine and isooxodesmosine from bovine aorta elastin. Both oxodesmosine and isooxodesmosine were very hygroscopic, white solid with faint yellow tinges, soluble in aqueous solvents. Structural analysis of both amino acids were done by UV, NMR and MS.It might be deduced from the structure of N-substituted dihydrooxopyridine skeleton that these new amino acids are metabolic intermediate of major pyridinium crosslinking amino acids, desmosine and isodesmosine. The in vivo synthesis of both amino acids were probably took place by oxydation of desmosine and isodesmosine as intermediate for further decompositions of such crosslinks. Although the mechanical details are not clear, one must invoke the cyclization, accompany with decarboxylation reaction during acid hydrolysis to form cyclopentene skeleton.

弹性蛋白是一种结缔组织蛋白，几乎存在于成熟动物的所有组织和器官中，是血管和某些韧带以及其他顺应性组织(如肺和皮肤)的主要成分。在生理发育过程中，弹性蛋白主要由血管平滑肌和成纤维细胞等细胞合成，作为可溶的前体原弹性蛋白。每个tropoelestn分子中的几对脱氨基赖氨基残基参与了一系列自发的缩合反应，导致交联型氨基酸的形成。在我们的实验中，我们从牛主动脉弹性蛋白中分离到了两个新的具有N-取代二氢氧代吡啶结构的交联型氨基酸，分别命名为氧桥粒和异氧桥粒。草桥素和异氧桥连素都是吸湿性很强的白色固体，略带黄色，易溶于水。对两种氨基酸进行了UV、核磁共振和MS结构分析，根据N-取代二氢氧并吡啶骨架的结构推测，这两种新氨基酸是吡啶类主要交联型氨基酸桥连和异桥联的代谢中间体。这两种氨基酸的体内合成可能是通过桥连素和异桥桥素的氧化作用进行的，作为进一步分解这种交联物的中间产物。虽然机械细节尚不清楚，但必须启动环化反应，伴随着酸解过程中的脱羧基反应形成环戊烯骨架。