Activation profiles and regulatory cascades of the human kallikrein-related peptidases.

Activation profiles and regulatory cascades of the human kallikrein-related peptidases. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Activation profiles and regulatory cascades of the human kallikrein-related peptidases. Abstract Text:

Hyesook Yoon,Gurunathan Laxmikanthan,Jihun Lee,Sachiko I Blaber,Aaron Rodriguez,Joshua M Kogot,Isobel A Scarisbrick,Michael Blaber,Hyesook Yoon,Gurunathan Laxmikanthan,Jihun Lee,Sachiko I Blaber,Aaron Rodriguez,Joshua M Kogot,Isobel A Scarisbrick,Michael Blaber,

The human kallikrein (KLK)-related peptidases are the largest family of serine peptidases, comprising 15 members (KLK1-15) and with the majority (KLK4-15) being identified only within the last decade. Members of this family are associated with important diseased states (including cancer, inflammation, and neurodegeneration) and have been utilized or proposed as clinically important biomarkers or therapeutic targets of interest. All human KLKs are synthesized as prepro-forms that are proteolytically processed to secreted pro-forms via the removal of an amino-terminal secretion signal peptide. The secreted inactive pro-KLKs are then activated extracellularly to mature peptidases by specific proteolytic release of their amino-terminal propeptide. Although a key step in the regulation of KLK function, details regarding the activation of the human pro-KLKs (i.e. the KLK "activome") are unknown, to a significant extent, but have been postulated to involve "activation cascades" with other KLKs and endopeptidases. To characterize more completely the KLK activome, we have expressed from Escherichia coli individual KLK propeptides fused to the amino terminus of a soluble carrier protein. The ability of 12 different mature KLKs to process the 15 different pro-KLK peptide sequences has been determined. Various autolytic and cross-activation relationships identified using this system have subsequently been characterized using recombinant pro-KLK proteins. The results demonstrate the potential for extensive KLK activation cascades and, when combined with available data for the tissue-specific expression of the KLK family, permit the construction of specific regulatory cascades. One such tissue-specific cascade is proposed for the central nervous system.

Activation profiles and regulatory cascades of the human kallikrein-related peptidases. Publishing Authors By Initials

H Yoon,G Laxmikanthan,J Lee,SI Blaber,A Rodriguez,JM Kogot,IA Scarisbrick,M Blaber,H Yoon,G Laxmikanthan,J Lee,SI Blaber,A Rodriguez,JM Kogot,IA Scarisbrick,M Blaber,

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

Activation profiles and regulatory cascades of the human kallikrein-related peptidases. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 31852-64

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 6

MONTH: 09

YEAR: 2007

Activation profiles and regulatory cascades of the human kallikrein-related peptidases. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Activation profiles and regulatory cascades of the human kallikrein-related peptidases. Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: Activation profiles and regulatory cascades of the human kallikrein-related peptidases. Information

Substance Name:

Registry Number:

Grant and Affiliation Information for Activation profiles and regulatory cascades of the human kallikrein-related peptidases.

AFFILIATION: Department of Biomedical Sciences, Florida State University, Tallahassee, Florida 32306-4300, USA.

Country: United States

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biol Chem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Activation profiles and regulatory cascades of the human kallikrein-related peptidases Related Publications

• A Logical OR Redundancy within the Asx-Pro-Asx-Gly Type I beta-Turn Motif.
• Activation profiles and regulatory cascades of the human kallikrein-related peptidases.
• Mutagenesis of the crystal contact of acidic fibroblast growth factor.
• The autolytic regulation of human kallikrein-related peptidase 6.