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PMID: 8132824 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Distribution of the matrix metalloproteinases stromelysin, gelatinases A and B, and collagenase in Crohn's disease and normal intestine.

Journal of clinical pathology ·Vol. 47 ·No. 2 ·1994-02-00 ·Pages 113-6

Bailey CJ, Hembry RM, Alexander A, Irving MH, Grant ME, Shuttleworth CA

Abstract

To investigate the role of the matrix metalloproteinases (MMPs) in the connective tissue changes seen in the intestine in Crohn's disease. Indirect immunofluorescence microscopy using specific antibodies to the MMPs (collagenase, gelatinase A and B, and stromelysin) were used to assess the distribution of these enzymes in normal and diseased intestine. In normal intestine the matrix metalloproteinases were confined to a few isolated inflammatory cells, but in Crohn's disease, the inflammatory infiltrate was associated with increased numbers of polymorphonuclear leucocytes which stained positive for gelatinase B. Stromelysin was also detected extracellularly on the connective tissue matrix in regions of smooth muscle cell proliferation and mucosal degradation. Interestingly, in ulcerative colitis, another inflammatory bowel disease, stromelysin was localised in the lamina propria in regions of mucosal loss. The increased numbers of inflammatory cells containing gelatinase B, and the localisation of extracellular stromelysin in regions of fibrosis and mucosal degradation, suggest that these enzymes have a role in the pathological changes seen in Crohn's disease. In cases of ulcerative colitis stromelysin was also detected on the lamina propria in regions of mucosal loss, and seems to be associated with the connective tissue changes that precede mucosal loss.

MeSH Terms
Colitis, Ulcerative/enzymology Collagenases/metabolism Crohn Disease/enzymology Extracellular Matrix/enzymology Fluorescent Antibody Technique Gelatinases/metabolism Humans Intestines/enzymology Matrix Metalloproteinase 3 Metalloendopeptidases/metabolism
Chemicals
Collagenases Gelatinases Metalloendopeptidases Matrix Metalloproteinase 3
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Bailey C J
School of Biological Sciences, University of Manchester Medical School.
Hembry R M
Alexander A
Irving M H
Grant M E
Shuttleworth C A
References (14)
14 references, click to expand
  1. Sequence specificity of human skin fibroblast collagenase. Evidence for the role of collagen structure in determining the collagenase cleavage site.
    J Biol Chem. 1987 May 5;262(13):6221-6 PMID: 3032960
  2. Role of collagenase in colonic anastomoses: a reappraisal.
    Br J Surg. 1988 Apr;75(4):330-4 PMID: 2833978
  3. Characterization of gelatinase from pig polymorphonuclear leucocytes. A metalloproteinase resembling tumour type IV collagenase.
    Biochem J. 1989 Mar 1;258(2):463-72 PMID: 2539808
  4. The tissue metalloproteinase family and the inhibitor TIMP: a study using cDNAs and recombinant proteins.
    Ann Rheum Dis. 1990 Jun;49 Suppl 1:469-79 PMID: 2197998
  5. Type IV collagenases in tumor invasion and metastasis.
    Cancer Metastasis Rev. 1990 Dec;9(4):289-303 PMID: 1965794
  6. Stromelysin in tumor progression and metastasis.
    Cancer Metastasis Rev. 1990 Dec;9(4):305-19 PMID: 2097083
  7. Comparison of human stromelysin and collagenase by cloning and sequence analysis.
    Biochem J. 1986 Dec 15;240(3):913-6 PMID: 3030290
  8. Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP).
    Biochem J. 1991 Jul 1;277 ( Pt 1):277-9 PMID: 1649600
  9. Metalloproteinases and their inhibitors in matrix remodeling.
    Trends Genet. 1990 Apr;6(4):121-5 PMID: 2132731
  10. Binding of latent and high Mr active forms of stromelysin to collagen is mediated by the C-terminal domain.
    J Cell Sci. 1991 Aug;99 ( Pt 4):789-95 PMID: 1770006
  11. Metalloproteinases from rabbit bone culture medium degrade types IV and V collagens, laminin and fibronectin.
    Biochem J. 1981 Dec 1;199(3):807-11 PMID: 7041891
  12. Purification and characterization of a rabbit bone metalloproteinase that degrades proteoglycan and other connective-tissue components.
    Biochem J. 1983 Mar 1;209(3):741-52 PMID: 6347180
  13. Immunolocalization of tissue inhibitor of metalloproteinases (TIMP) in human cells. Characterization and use of a specific antiserum.
    J Cell Sci. 1985 Feb;73:105-19 PMID: 3894382
  14. Purification and characterization of human 72-kDa gelatinase (type IV collagenase). Use of immunolocalisation to demonstrate the non-coordinate regulation of the 72-kDa and 95-kDa gelatinases by human fibroblasts.
    Biol Chem Hoppe Seyler. 1991 Apr;372(4):287-96 PMID: 1647782
Article Info
Journal
Journal of clinical pathology
Abbr.
J Clin Pathol
ISSN
0021-9746
Published
1994-02-00
Pages
113-6
Language
English
Region
England
NLM ID
0376601
PMCID
PMC501822
Subset
IM
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