Suppressed Expression but Not Activity of Collagenases MMP-1 and MMP-13 in Human Renal Carcinoma.


Journal

Pathobiology : journal of immunopathology, molecular and cellular biology
ISSN: 1423-0291
Titre abrégé: Pathobiology
Pays: Switzerland
ID NLM: 9007504

Informations de publication

Date de publication:
2019
Historique:
received: 21 11 2018
accepted: 11 03 2019
pubmed: 28 5 2019
medline: 18 12 2019
entrez: 27 5 2019
Statut: ppublish

Résumé

Collagenases are enzymes starting collagen degradation. The role of collagenases in renal carcinoma development is not well understood. Evaluation of collagen content and collagenase expression and activity in human kidney cancers. Collagen content was measured by the hydroxyproline assay. The expression and the content of collagenases were evaluated by Western blotting and ELISA. Fluorogenic substrate was used to measure enzyme activity. Collagen content significantly decreases with the progression of kidney cancer. Both collagenases are first present in high molecular complexes in both control and cancer tissue. The healthy part of the kidney contains similar amounts of both collagenases. Collagenase content decreased significantly in tumor tissue with increasing cancer stage. MMP-13 activity is much higher than that of MMP-1 in all tissues investigated. We observed increasing collagenase activity (MMP-1 and MMP-13) with increasing renal cancer grade. The lower content and higher activity of the collagenases investigated in cancer tissue indicate that most of these enzymes are in active form in renal carcinoma. The lower collagen content in cancer tissue can be explained at least in part by increased collagenase activity.

Sections du résumé

BACKGROUND BACKGROUND
Collagenases are enzymes starting collagen degradation. The role of collagenases in renal carcinoma development is not well understood.
OBJECTIVE OBJECTIVE
Evaluation of collagen content and collagenase expression and activity in human kidney cancers.
METHODS METHODS
Collagen content was measured by the hydroxyproline assay. The expression and the content of collagenases were evaluated by Western blotting and ELISA. Fluorogenic substrate was used to measure enzyme activity.
RESULTS RESULTS
Collagen content significantly decreases with the progression of kidney cancer. Both collagenases are first present in high molecular complexes in both control and cancer tissue. The healthy part of the kidney contains similar amounts of both collagenases. Collagenase content decreased significantly in tumor tissue with increasing cancer stage. MMP-13 activity is much higher than that of MMP-1 in all tissues investigated. We observed increasing collagenase activity (MMP-1 and MMP-13) with increasing renal cancer grade.
CONCLUSIONS CONCLUSIONS
The lower content and higher activity of the collagenases investigated in cancer tissue indicate that most of these enzymes are in active form in renal carcinoma. The lower collagen content in cancer tissue can be explained at least in part by increased collagenase activity.

Identifiants

pubmed: 31129674
pii: 000499499
doi: 10.1159/000499499
doi:

Substances chimiques

Collagen 9007-34-5
MMP13 protein, human EC 3.4.24.-
Matrix Metalloproteinase 13 EC 3.4.24.-
MMP1 protein, human EC 3.4.24.7
Matrix Metalloproteinase 1 EC 3.4.24.7
Hydroxyproline RMB44WO89X

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

201-207

Informations de copyright

© 2019 S. Karger AG, Basel.

Auteurs

Grzegorz Młynarczyk (G)

Department of Medical Biochemistry, Medical University of Białystok, Białystok, Poland, mlynarz36@yahoo.pl.
Department of Urology, Medical University of Białystok, Białystok, Poland, mlynarz36@yahoo.pl.

Jacek Kudelski (J)

Department of Urology, Medical University of Białystok, Białystok, Poland.

Barbara Darewicz (B)

Department of Urology, Medical University of Białystok, Białystok, Poland.

Marta Bruczko-Goralewska (M)

Department of Medical Biochemistry, Medical University of Białystok, Białystok, Poland.

Lech Romanowicz (L)

Department of Medical Biochemistry, Medical University of Białystok, Białystok, Poland.

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Classifications MeSH