Cloning, purification, and characterization of a non-collagenous anti-angiogenic protein domain from human alpha1 type IV collagen expressed in Sf9 cells

Protein Expression and Purification
Chandra S Boosani, Akulapalli Sudhakar

Abstract

alpha1(IV)NC1, a cleavage fragment of the carboxy terminal non-collagenous human alpha1 chain of type IV collagen, is derived from the extracellular matrix specifically by MMP-2. Recently we determined the in vitro and in vivo anti-angiogenic activity of alpha1(IV)NC1 and presently, its role in cancer therapy is under evaluation. To characterize alpha1(IV)NC1 as a potential candidate for drug development and to test its efficacy in animal models, an effective method to produce a purified active form of alpha1(IV)NC1 is needed. In the present study, expression of alpha1(IV)NC1 in Sf9 cells using baculovirus expression system was discussed, this method was found to be effective in the production of a functionally active soluble form of the recombinant protein. The purified protein showed its characteristic activities such as inhibiting cell proliferation, migration, and tube formation in endothelial cells.

References

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Citations

Nov 13, 2013·Protein Expression and Purification·Venugopal GundaYakkanti A Sudhakar
Jun 28, 2012·Chinese Medical Sciences Journal = Chung-kuo I Hsüeh K'o Hsüeh Tsa Chih·Yi Lv, Jin-Ping Zheng
Oct 28, 2008·Medical Hypotheses·Ying YinJian-Min Si
Mar 29, 2014·Scientific Reports·Yakkanti Akul SudhakarSmita C Pawar
Jan 1, 2007·Gene Regulation and Systems Biology·Akulapalli Sudhakar, Chandra S Boosani
Jan 1, 2008·Clinical Medicine. Oncology·Chandra Shekhar Boosani, Akulapalli Sudhakar
May 22, 2020·Matrix Biology : Journal of the International Society for Matrix Biology·Lisandra E de Castro Brás, Nikolaos G Frangogiannis

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