Interactions of serine proteases with cultured fibroblasts.

D. D. Cunningham, W. E. Van Nostrand, David Farrell, C. H. Campbell

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

This review summarizes the mechanisms by which several serine proteases, particularly urokinase, thrombin, and elastase, interact with cultured fibroblasts. Many of these studies were prompted by findings that interactions of these proteases with cells and the extracellular matrix are important in a number of physiologic and pathologic processes. Two main pathways have been identified for specific interactions of these proteases with fibroblasts. One involves surface binding sites for the free protease that appear to bind only one particular protease. An unusual feature collectively shared by the binding sites for urokinase, thrombin, and elastase is that the bound protease is not detectably internalized by the fibroblasts. The other pathway by which serine proteases interact with fibroblasts involves proteins named protease nexins (PNs). Three PNs have been identified. They are secreted by fibroblasts and inhibit certain serine proteases by forming a covalent complex with the protease catalytic site serine. The complexes then bind back to the fibroblasts via the PN portion of the complex and are internalized and degraded. Recent studies showing that the fibroblast surface and extracellular matrix accelerate the inactivation of thrombin by PN-1 support the hypothesis that the PNs control protease activity at and near the cell surface. The PNs differ from plasma protease inhibitors in their molecular properties, absence in plasma, site of synthesis, and site of clearance of the inhibitor:protease complexes.

Original languageEnglish (US)
Pages (from-to)281-291
Number of pages11
JournalJournal of Cellular Biochemistry
Volume32
Issue number4
StatePublished - 1986
Externally publishedYes

Fingerprint

Protease Nexins
Serine Proteases
Fibroblasts
Peptide Hydrolases
Thrombin
Proteins
Pancreatic Elastase
Urokinase-Type Plasminogen Activator
Protease Inhibitors
Extracellular Matrix
Binding Sites
Plasmas
Pathologic Processes
Serine
Catalytic Domain

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology

Cite this

Cunningham, D. D., Van Nostrand, W. E., Farrell, D., & Campbell, C. H. (1986). Interactions of serine proteases with cultured fibroblasts. Journal of Cellular Biochemistry, 32(4), 281-291.

Interactions of serine proteases with cultured fibroblasts. / Cunningham, D. D.; Van Nostrand, W. E.; Farrell, David; Campbell, C. H.

In: Journal of Cellular Biochemistry, Vol. 32, No. 4, 1986, p. 281-291.

Research output: Contribution to journalArticle

Cunningham, DD, Van Nostrand, WE, Farrell, D & Campbell, CH 1986, 'Interactions of serine proteases with cultured fibroblasts.', Journal of Cellular Biochemistry, vol. 32, no. 4, pp. 281-291.
Cunningham, D. D. ; Van Nostrand, W. E. ; Farrell, David ; Campbell, C. H. / Interactions of serine proteases with cultured fibroblasts. In: Journal of Cellular Biochemistry. 1986 ; Vol. 32, No. 4. pp. 281-291.
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