Human T lymphocytes synthesize the 92 kDa type IV collagenase (gelatinase B)

Benjamin S. Weeks, H. William Schnaper, Michael Handy, Eva Holloway, Hynda K. Kleinman*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


In order for T cells to exit the circulatory system, traverse the endothelial basement membrane, and arrive in target tissues, these cells must attach to and degrade basement membrane proteins. 12‐O‐tetradecanoylphorbol‐13‐acetate (TPA) has been shown to stimulate lymphoid cell adhesion to basement membrane components. We have used TPA to study the ability of human lymphoid cells to secrete type IV collagenases, enzymes capable of degrading basement membrane proteins. Here, we found that human primary T cells and H‐9 lymphoid cells synthesize the 92 kDa type IV collagenase (gelatinase B) and TPA stimulates the synthesis and secretion of this protease. Peak TPA‐stimulated gelatinase B secretion and mRNA accumulation were observed 9 hours after TPA treatment, while the peak adhesion to type IV collagen was observed only 3 hours after TPA treatment. The protein kinase C inhibitor, H‐7, inhibited TPA‐stimulated gelatinase B secretion. Both the primary T cells and H‐9 lymphoid cells also expressed the mRNA for the tissue inhibitor of metalloproteinase‐1 (TIMP‐1). These data demonstrate that TPA ‐ stimulated lymphoid cells adhere to type IV collagen and subsequently synthesize and secrete gelatinase B and TIMP‐1. We conclude that lymphoid cell extravasation may involve cellular employment of adhesion mechanisms prior to degradation of the matrix, which is similar to the process of extravasation used by metastatic cells. © 1993 Wiley‐Liss, Inc.

Original languageEnglish (US)
Pages (from-to)644-649
Number of pages6
JournalJournal of Cellular Physiology
Issue number3
StatePublished - Jan 1 1993

ASJC Scopus subject areas

  • Physiology
  • Clinical Biochemistry
  • Cell Biology


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