What question did this study set out to answer?

To determine whether synthetic triple-helical peptide models of type V collagen can serve as selective substrates for tracking active matrix metalloproteinase-2 and -9.

May 1, 2003Journal of Biological ChemistryOpen Access

Selective Hydrolysis of Triple-helical Substrates by Matrix Metalloproteinase-2 and -9

View Full Paper

Ask AI

Bookmark

Authors

JLJanelle L. Lauer‐FieldsThe University of Texas at San Antonio TSThilaka SritharanFlorida Atlantic University MSM. Sharon StackUniversity of Notre Dame

Discussion

Member takes

Implication

In vitro analysis demonstrates selective triple-helical peptide cleavage by gelatinases in melanoma models, highlighting a targeted method to track active matrix metalloproteinases.

Key Points

To determine whether synthetic triple-helical peptide models of type V collagen can serve as selective substrates for tracking active matrix metalloproteinase-2 and -9.
Synthesized triple-helical peptide models of the type V collagen cleavage site [alpha1(V)436-450 THP and fluorogenic alpha1(V)436-447 fTHP] to evaluate cleavage by MMP-1, -2, -3, -9, -13, and -14.
Determined kinetic efficiency values (kcat/Km) for MMP-2 and MMP-9 cleavage of alpha1(V)436-447 fTHP.
Assayed triple-helical peptidase activity in melanoma cells stimulated via alpha(2)beta(1) integrin engagement.
Both MMP-2 and MMP-9 cleaved alpha1(V)436-447 fTHP specifically at the Gly-Val bond, with kcat/Km values of 14,002 s^-1 M^-1 and 5,449 s^-1 M^-1, respectively.
Neither triple-helical peptide model was hydrolyzed by MMP-1, MMP-3, MMP-13, or MMP-14.
Integrin alpha(2)beta(1) binding in melanoma cells stimulated triple-helical peptidase activity, with >95% of the total activity originating from non-MMP-2 and non-MMP-9 enzymes.

Cite This Study

Lauer‐Fields et al. (2003) studied this question.

synapsesocial.com/papers/6a81cc471ece0ba82ce1b4cf https://doi.org/10.1074/jbc.m211330200

View Full Paper

Ask AI

Bookmark

Implication

In vitro analysis demonstrates selective triple-helical peptide cleavage by gelatinases in melanoma models, highlighting a targeted method to track active matrix metalloproteinases.

Selective Hydrolysis of Triple-helical Substrates by Matrix Metalloproteinase-2 and -9

Discussion

Member takes

Implication

Key Points

Cite This Study

Selective Hydrolysis of Triple-helical Substrates by Matrix Metalloproteinase-2 and -9

Discussion

Member takes

Implication

Key Points

Cite This Study

Also Consider

Also Consider