ArticleThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society2013
Tissue- and cell-specific co-localization of intracellular gelatinolytic activity and matrix metalloproteinase 2.
Article in The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 20 citations in OpenAlex.
- Gel Diffusion-Based Gelatin Zymography to Analyze MMP-2 and MMP-9 Activity in Cell Culture.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Enhancement of anti-tumor activity in melanoma using arginine deiminase fused with 30Kc19α protein.Applied microbiology and biotechnology · 2022Article
- Inhibition of the extracellular signal-regulated kinase pathway reduces the inflammatory component in nucleus pulposus cells.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2022Article
- MMP-2 and Notch signal pathway regulate migration of adipose-derived stem cells and chondrocytes in co-culture systems.Cell proliferation · 2017Article
- Article
- Matrix-metalloproteinases as targets for controlled delivery in cancer: An analysis of upregulation and expression.Journal of controlled release : official journal of the Controlled Release Society · 2017Review
- Is there new hope for therapeutic matrix metalloproteinase inhibition?Nature reviews. Drug discovery · 2014Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Matrix metalloproteinase 2 (MMP-2) is a proteolytic enzyme that degrades extracellular matrix proteins. Recent studies indicate that MMP-2 also has a role in intracellular proteolysis during various pathological conditions, such as ischemic injuries in heart and brain and in tumor growth. The present study was performed to map the distribution of intracellular MMP-2 activity in various mouse tissues and cells under physiological conditions. Samples from normal brain, heart, lung, liver, spleen, pancreas, kidney, adrenal gland, thyroid gland, gonads, oral mucosa, salivary glands, esophagus, intestines, and skin were subjected to high-resolution in situ gelatin zymography and immunohistochemical staining. In hepatocytes, cardiac myocytes, kidney tubuli cells, epithelial cells in the oral mucosa as well as in excretory ducts of salivary glands, and adrenal cortical cells, we found strong intracellular gelatinolytic activity that was significantly reduced by the metalloprotease inhibitor EDTA but not by the cysteine protease inhibitor E-64. Furthermore, the gelatinolytic activity was co-localized with MMP-2. Western blotting and electron microscopy combined with immunogold labeling revealed the presence of MMP-2 in different intracellular compartments of isolated hepatocytes. Our results indicate that MMP-2 takes part in intracellular proteolysis in specific tissues and cells during physiological conditions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.