Non-Triple Helical Form of Type IV Collagen α1 Chain
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 s...
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pubmed-49457372016-07-20 Non-Triple Helical Form of Type IV Collagen α1 Chain Sugiyama, Hiroaki Tokunaka, Kazuhiro Hayashi, Toshihiko Imamura, Yasutada Morita, Makoto Yamato, Masayuki Article 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. Elsevier 2015-12-09 /pmc/articles/PMC4945737/ /pubmed/27441234 http://dx.doi.org/10.1016/j.heliyon.2015.e00051 Text en © 2015 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
repository_type |
Open Access Journal |
institution_category |
Foreign Institution |
institution |
US National Center for Biotechnology Information |
building |
NCBI PubMed |
collection |
Online Access |
language |
English |
format |
Online |
author |
Sugiyama, Hiroaki Tokunaka, Kazuhiro Hayashi, Toshihiko Imamura, Yasutada Morita, Makoto Yamato, Masayuki |
spellingShingle |
Sugiyama, Hiroaki Tokunaka, Kazuhiro Hayashi, Toshihiko Imamura, Yasutada Morita, Makoto Yamato, Masayuki Non-Triple Helical Form of Type IV Collagen α1 Chain |
author_facet |
Sugiyama, Hiroaki Tokunaka, Kazuhiro Hayashi, Toshihiko Imamura, Yasutada Morita, Makoto Yamato, Masayuki |
author_sort |
Sugiyama, Hiroaki |
title |
Non-Triple Helical Form of Type IV Collagen α1 Chain |
title_short |
Non-Triple Helical Form of Type IV Collagen α1 Chain |
title_full |
Non-Triple Helical Form of Type IV Collagen α1 Chain |
title_fullStr |
Non-Triple Helical Form of Type IV Collagen α1 Chain |
title_full_unstemmed |
Non-Triple Helical Form of Type IV Collagen α1 Chain |
title_sort |
non-triple helical form of type iv collagen α1 chain |
description |
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. |
publisher |
Elsevier |
publishDate |
2015 |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4945737/ |
_version_ |
1613609611159404544 |