Akiba J, Kakehashi A, Ueno N, Tano Y, Chakrabarti B
Schepens Eye Research Institute, Department of Ophthalmology, Harvard Medical School, Boston, Massachusetts, USA.
Graefes Arch Clin Exp Ophthalmol. 1995 Jul;233(7):430-4. doi: 10.1007/BF00180947.
To understand the molecular events underlying disease-related vitreous gel contraction, the effect of serum components on collagen was investigated.
Bovine vitreous or dermal collagen was incubated with a mixture of transglutaminase (TG; factor XIIIa) and fibronectin (FN), and the biochemical changes of collagen were monitored by gel electrophoresis. In addition, serum-induced changes in the volume of the collagen gel were monitored.
Gel electrophoresis revealed a new high-molecular-weight band (M(r) 240,000) presumably due to intermolecular cross-links of collagen peptides and FN. The serum components also were shown to cause a significant decrease in the volume of the collagen gel. CONCLUSION. Collagen gel contraction could be attributed to the collagen-FN-collagen cross-links catalyzed by TG.
为了解疾病相关玻璃体凝胶收缩的分子机制，研究了血清成分对胶原蛋白的影响。
将牛玻璃体或真皮胶原蛋白与转谷氨酰胺酶（TG；因子ⅩⅢa）和纤连蛋白（FN）的混合物一起孵育，通过凝胶电泳监测胶原蛋白的生化变化。此外，监测血清诱导的胶原蛋白凝胶体积变化。
凝胶电泳显示出现一条新的高分子量条带（相对分子质量240,000），推测是由于胶原蛋白肽与FN之间的分子间交联所致。血清成分还导致胶原蛋白凝胶体积显著减小。结论：胶原蛋白凝胶收缩可能归因于TG催化的胶原蛋白-FN-胶原蛋白交联。
