MMP-14 Exhibits Greater Expression, Content and Activity Compared to MMP-15 in Human Renal Carcinoma
Jazyk angličtina Země Švýcarsko Médium electronic
Typ dokumentu srovnávací studie, časopisecké články
PubMed
39125675
PubMed Central
PMC11312297
DOI
10.3390/ijms25158107
PII: ijms25158107
Knihovny.cz E-zdroje
- Klíčová slova
- MMP-14, MMP-15, cancer, renal carcinoma, transmembrane metalloproteinases,
- MeSH
- dospělí MeSH
- karcinom z renálních buněk * metabolismus patologie enzymologie MeSH
- lidé středního věku MeSH
- lidé MeSH
- matrixová metaloproteinasa 14 * metabolismus MeSH
- matrixová metaloproteinasa 15 * metabolismus genetika MeSH
- nádory ledvin * patologie metabolismus enzymologie MeSH
- senioři MeSH
- Check Tag
- dospělí MeSH
- lidé středního věku MeSH
- lidé MeSH
- mužské pohlaví MeSH
- senioři MeSH
- ženské pohlaví MeSH
- Publikační typ
- časopisecké články MeSH
- srovnávací studie MeSH
- Názvy látek
- matrixová metaloproteinasa 14 * MeSH
- matrixová metaloproteinasa 15 * MeSH
- MMP14 protein, human MeSH Prohlížeč
- MMP15 protein, human MeSH Prohlížeč
Membrane-type metalloproteinases (including MMP-14 and MMP-15) are enzymes involved in the degradation of extracellular matrix components. In cancer, they are involved in processes such as cellular invasion, angiogenesis and metastasis. Therefore, the aim of this study was to evaluate the expression, content and activity of MMP-14 and MMP-15 in human renal cell carcinoma. Samples of healthy kidney tissue (n = 20) and tissue from clear-cell kidney cancer (n = 20) were examined. The presence and contents of the MMPs were assessed using Western blot and ELISA techniques, respectively. Their activity-both actual and specific-was evaluated using fluorimetric analysis. Both control and cancer human kidney tissues contain MMP-14 and MMP-15 enzymes in the form of high-molecular-weight complexes. Moreover, these enzymes occur in both active and latent forms. Their content in cancer tissues is very similar, but with a noteworthy decrease in content with an increase in the kidney cancer grade for both membrane-type metalloproteinases. Even more notable is the highest content of the investigated enzymes represented by MMP-14 in the control tissues. Considering the actual and specific activity outcomes, MMP-14 dominates over MMP-15 in all of the investigated tissues. Nevertheless, we also noted a significant enhancement of the activity of both metalloproteinases with an increase in the grade of renal cancer. The expression and activity of both enzymes were detected in all examined renal cancer tissues. However, our findings suggest that transmembrane metalloproteinase 14 (MMP-14) plays a much more significant and essential role than MMP-15 in the studied renal carcinoma tissues. Therefore, it seems that MMP-14 could be a promising target in the diagnosis, prognosis and therapy of renal cell carcinoma.
Department of Biochemical Diagnostics Medical University of Białystok 15 269 Białystok Poland
Department of Neurodegeneration Diagnostics Medical University of Bialystok 15 269 Białystok Poland
Department of Urology and Oncological Urology Medical University of Lublin 20 059 Lublin Poland
Department of Urology Charles University and University Hospital Motol 150 06 Praha Czech Republic
Department of Urology Medical University of Białystok 15 276 Białystok Poland
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