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Measurement of Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases in Blood and Tissues: Clinical and Experimental Applications
Author(s) -
ZUCKER STANLEY,
HYMOWITZ MICHELLE,
CONNER CATHLEEN,
ZARRABI HOSEIN M.,
HUREWITZ ADAM N.,
MATRISIAN LYNN,
BOYD DOUGLAS,
NICOLSON GARTH,
MONTANA STEVE
Publication year - 1999
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1999.tb07687.x
Subject(s) - matrix metalloproteinase , medicine , rheumatoid arthritis , gelatinase , metastasis , colorectal cancer , prostate cancer , cancer , cancer research
The balance between production and activation of MMPs and their inhibition by TIMPs is a crucial aspect of cancer invasion and metastasis. On the basis of the concept that MMPs synthesized in tissues seep into the bloodstream, we have examined MMP levels in the plasma of patients with cancer. In colorectal, breast, prostate, and bladder cancer, most patients with aggressive disease have increased plasma levels of gelatinase B. In patients with advanced colorectal cancer, high levels of either gelatinase B or TIMP complex were associated with shortened survival. We propose that these assays may be clinically useful in characterizing metastatic potential in selected kinds of cancer. In rheumatoid arthritis and systemic lupus erythematosus (SLE), serum and plasma levels of stromelysin‐1 were ∼ 3‐5‐fold increased. Fluctuating serum stromelysin‐1 levels in SLE did not correspond with change in disease activity. In SLE, stromelysin‐1 may be a component of the chronic tissue repair process rather than being responsible for inciting tissue damage. On the basis of these observations, we conclude that measurement of plasma/serum MMP and TIMP levels may provide important data for selecting and following patients considered for treatment with drugs that interfere with MMP activity.