Enzymatic profiling of human kallikrein 14 using phage-display substrate technology
Details
Serval ID
serval:BIB_93DAD1932B51
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Enzymatic profiling of human kallikrein 14 using phage-display substrate technology
Journal
Biological Chemistry
ISSN
1431-6730
Publication state
Published
Issued date
03/2005
Peer-reviewed
Oui
Volume
386
Number
3
Pages
291-8
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Mar
Research Support, Non-U.S. Gov't --- Old month value: Mar
Abstract
The human KLK14 gene is one of the newly identified serine protease genes belonging to the human kallikrein family, which contains 15 members. KLK14 , like all other members of the human kallikrein family, is predicted to encode for a secreted serine protease already found in various biological fluids. This new kallikrein is mainly expressed in prostate and endocrine tissues, but its function is still unknown. Recent studies have demonstrated that KLK14 gene expression is up-regulated in prostate and breast cancer tissues, and that higher expression levels correlate with more aggressive tumors. In this work, we used phage-display substrate technology to study the substrate specificity of hK14. A phage-displayed random pentapeptide library with exhaustive diversity was screened with purified recombinant hK14. Highly specific and sensitive substrates were selected from the library. We show that hK14 has dual activity, trypsin- and chymotrypsin-like, with a preference for cleavage after arginine residues. A SwissProt database search with selected sequences identified six potential human protein substrates for hK14. Two of them, laminin alpha-5 and collagen IV, which are major components of the extracellular matrix, have been demonstrated to be hydrolyzed efficiently by hK14.
Keywords
Bacteriophages/genetics
Cloning, Molecular
Collagen Type IV/metabolism
Extracellular Matrix Proteins/metabolism
Humans
Hydrolysis
Kallikreins/genetics/*metabolism
Kinetics
Laminin/metabolism
Substrate Specificity
Pubmed
Web of science
Create date
21/01/2008 16:10
Last modification date
20/08/2019 14:56