IMR Press / FBE / Volume 3 / Issue 4 / DOI: 10.2741/E350

Frontiers in Bioscience-Elite (FBE) is published by IMR Press from Volume 13 Issue 2 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
Identification of protein-protein interactions of human HtrA1
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1 Department of Biochemistry, Section of Pathology, Second University of Naples, Italy
2 Institute of Cardiology, Catholic University, Rome, Italy
3 Department of Medicine and Public Health, Second University of Naples, Naples, Italy
4 Victoria Johnson Research Center and VCU Pauley Heart Center, Virginia Commonwealth University, Richmond, VA, USA
5 Department SAFU, National Cancer Institute,Regina Elena, Rome, Italy
6 Department of Development of Therapeutic Programs, National Cancer Institute, Regina Elena, Rome, Italy

*Author to whom correspondence should be addressed.

Academic Editor: Antonio Giordano

Front. Biosci. (Elite Ed) 2011, 3(4), 1493–1499; https://doi.org/10.2741/E350
Published: 1 June 2011
(This article belongs to the Special Issue Gene targets for modulating cell growth)
Abstract

The human heat shock protein HtrA1, a member of the HtrA family of serine proteases, is a evolutionarily highly conserved factor which displays a widespread pattern of expression. The yeast two-hybrid technique was employed to identify new cellular proteins physically interacting with HtrA1, and thus potential targets of this serine protease. An enzymatically inactive HtrA1 point mutant, HtrA1-S328A, was generated and used as bait in a yeast two-hybrid system. Fifty-two plasmids were isolated from primary positive yeast clones. Subsequent sequencing and BLAST analysis revealed cDNAs encoding for 13 different proteins. These putative binding partners of HtrA1 appeared to be a) components of extracellular matrix; b) factors related to signal pathways, and c) unknown proteins. Among the 13 positive clones identified and reported here, it is worth of note that the interaction of HtrA1 with tubulin and collagen (extracellular matrix proteins) and with tuberin (cytoplasmic protein) is confirmed by other studies, and this further supports previous findings in which HtrA1 can be found active as an intracytoplasmic protein or as secreted protein as well.

Keywords
HtrA1
Cancer
Two-hybrid
Protein-protein Interaction
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