Non-Triple Helical Form of Type IV Collagen α1 Chain. Issue 4 (December 2015)

• Record Type: Journal Article
• Authors: Sugiyama, Hiroaki; Tokunaka, Kazuhiro; Hayashi, Toshihiko; Imamura, Yasutada; Morita, Makoto; Yamato, Masayuki
• Is Part Of: Heliyon. Volume 1:Issue 4(2015)
• Publication Date: 2015-12
• Subjects: Biological sciences -- Cell biology -- Adhesion structures -- Pathology in cell biology; Research -- Periodicals; Medical sciences -- Periodicals; Natural history -- Periodicals; Social sciences -- Periodicals; Earth sciences -- Periodicals; Physical sciences -- Periodicals; 507.2
• DOI: 10.1016/j.heliyon.2015.e00051
• Languages: English
• ISSNs: 2405-8440

Abstract

Abstract: Type IV collagen with a triple-helical structure composed of three α chains is a major component of basement membrane. Previously, we reported that non-triple helical form of type IV collagen α1 chain (NTHα1(IV)) was isolated from human placenta and the culture media of human cells. In the present study, we report on the localization of NTH α1(IV) with a monoclonal antibody #370, exclusively reactive for the nascent chain, in the rabbit tissues. The staining was found on the basement membrane of blood vessels, of endomysium, of nerve, and of kidney but not on epithelial basement membrane. In a rabbit angiogenic model, #370 antibody staining was exclusively observed in neovascular tip region of endothelial cells, where no staining with anti-type IV collagen antibody was seen. Distinct localizations suggest that NTHα1(IV) is produced and stably deposited in endothelial cells and the surroundings under physiological conditions with some physiological roles in relation to the dynamics of vascular system.