Soluble THSD7A is an N-glycoprotein that promotes endothelial cell migration and tube formation in angiogenesis.

<h4>Background</h4>Thrombospondin type I domain containing 7A (THSD7A) is a novel neural protein that is known to affect endothelial migration and vascular patterning during development. To further understand the role of THSD7A in angiogenesis, we investigated the post-translational modi...

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Autores principales:	Meng-Wei Kuo, Chian-Huei Wang, Hsiao-Chun Wu, Shing-Jyh Chang, Yung-Jen Chuang
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/354c861b62dc4ed1ba5e77faa947d057
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spelling	oai:doaj.org-article:354c861b62dc4ed1ba5e77faa947d0572021-11-18T07:32:08ZSoluble THSD7A is an N-glycoprotein that promotes endothelial cell migration and tube formation in angiogenesis.1932-620310.1371/journal.pone.0029000https://doaj.org/article/354c861b62dc4ed1ba5e77faa947d0572011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22194972/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Thrombospondin type I domain containing 7A (THSD7A) is a novel neural protein that is known to affect endothelial migration and vascular patterning during development. To further understand the role of THSD7A in angiogenesis, we investigated the post-translational modification scheme of THS7DA and to reveal the underlying mechanisms by which this protein regulates blood vessel growth.<h4>Methodology/principal findings</h4>Full-length THSD7A was overexpressed in human embryonic kidney 293T (HEK293T) cells and was found to be membrane associated and N-glycosylated. The soluble form of THSD7A, which is released into the cultured medium, was harvested for further angiogenic assays. We found that soluble THSD7A promotes human umbilical vein endothelial cell (HUVEC) migration and tube formation. HUVEC sprouts and zebrafish subintestinal vessel (SIV) angiogenic assays further revealed that soluble THSD7A increases the number of branching points of new vessels. Interestingly, we found that soluble THSD7A increased the formation of filopodia in HUVEC. The distribution patterns of vinculin and phosphorylated focal adhesion kinase (FAK) were also affected, which implies a role for THSD7A in focal adhesion assembly. Moreover, soluble THSD7A increased FAK phosphorylation in HUVEC, suggesting that THSD7A is involved in regulating cytoskeleton reorganization.<h4>Conclusions/significance</h4>Taken together, our results indicate that THSD7A is a membrane-associated N-glycoprotein with a soluble form. Soluble THSD7A promotes endothelial cell migration during angiogenesis via a FAK-dependent mechanism and thus may be a novel neuroangiogenic factor.Meng-Wei KuoChian-Huei WangHsiao-Chun WuShing-Jyh ChangYung-Jen ChuangPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 12, p e29000 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Meng-Wei Kuo Chian-Huei Wang Hsiao-Chun Wu Shing-Jyh Chang Yung-Jen Chuang Soluble THSD7A is an N-glycoprotein that promotes endothelial cell migration and tube formation in angiogenesis.
description	<h4>Background</h4>Thrombospondin type I domain containing 7A (THSD7A) is a novel neural protein that is known to affect endothelial migration and vascular patterning during development. To further understand the role of THSD7A in angiogenesis, we investigated the post-translational modification scheme of THS7DA and to reveal the underlying mechanisms by which this protein regulates blood vessel growth.<h4>Methodology/principal findings</h4>Full-length THSD7A was overexpressed in human embryonic kidney 293T (HEK293T) cells and was found to be membrane associated and N-glycosylated. The soluble form of THSD7A, which is released into the cultured medium, was harvested for further angiogenic assays. We found that soluble THSD7A promotes human umbilical vein endothelial cell (HUVEC) migration and tube formation. HUVEC sprouts and zebrafish subintestinal vessel (SIV) angiogenic assays further revealed that soluble THSD7A increases the number of branching points of new vessels. Interestingly, we found that soluble THSD7A increased the formation of filopodia in HUVEC. The distribution patterns of vinculin and phosphorylated focal adhesion kinase (FAK) were also affected, which implies a role for THSD7A in focal adhesion assembly. Moreover, soluble THSD7A increased FAK phosphorylation in HUVEC, suggesting that THSD7A is involved in regulating cytoskeleton reorganization.<h4>Conclusions/significance</h4>Taken together, our results indicate that THSD7A is a membrane-associated N-glycoprotein with a soluble form. Soluble THSD7A promotes endothelial cell migration during angiogenesis via a FAK-dependent mechanism and thus may be a novel neuroangiogenic factor.
format	article
author	Meng-Wei Kuo Chian-Huei Wang Hsiao-Chun Wu Shing-Jyh Chang Yung-Jen Chuang
author_facet	Meng-Wei Kuo Chian-Huei Wang Hsiao-Chun Wu Shing-Jyh Chang Yung-Jen Chuang
author_sort	Meng-Wei Kuo
title	Soluble THSD7A is an N-glycoprotein that promotes endothelial cell migration and tube formation in angiogenesis.
title_short	Soluble THSD7A is an N-glycoprotein that promotes endothelial cell migration and tube formation in angiogenesis.
title_full	Soluble THSD7A is an N-glycoprotein that promotes endothelial cell migration and tube formation in angiogenesis.
title_fullStr	Soluble THSD7A is an N-glycoprotein that promotes endothelial cell migration and tube formation in angiogenesis.
title_full_unstemmed	Soluble THSD7A is an N-glycoprotein that promotes endothelial cell migration and tube formation in angiogenesis.
title_sort	soluble thsd7a is an n-glycoprotein that promotes endothelial cell migration and tube formation in angiogenesis.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/354c861b62dc4ed1ba5e77faa947d057
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Soluble THSD7A is an N-glycoprotein that promotes endothelial cell migration and tube formation in angiogenesis.

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