ArticleClinical & experimental metastasis1992
Inhibition of tumor invasion and extracellular matrix degradation by ubenimex (bestatin).
Article in Clinical & experimental metastasis, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 63 citations in OpenAlex.
- Naturally based pyrazoline derivatives as aminopeptidase N, VEGFR2 and MMP9 inhibitors: design, synthesis and molecular modeling.RSC advances · 2024Article
- Ubenimex combined with Albendazole for the treatment ofFrontiers in veterinary science · 2024Article
- Development of Hydroxamate Derivatives Containing a Pyrazoline Moiety as APN Inhibitors to Overcome Angiogenesis.Molecules (Basel, Switzerland) · 2022Article
- Asymmetric biomimetic transamination of α-keto amides to peptides.Nature communications · 2021Article
- Serum APN/CD13 as a novel diagnostic and prognostic biomarker of pancreatic cancer.Oncotarget · 2016Article
- MT95-4, a fully humanized antibody raised against aminopeptidase N, reduces tumor progression in a mouse model.Cancer science · 2015Article
- Cysteine cathepsins S and L modulate anti-angiogenic activities of human endostatin.The Journal of biological chemistry · 2011Article
- Aminopeptidase N (CD13) as a target for cancer chemotherapy.Cancer science · 2011Review
- Aminopeptidase-N/CD13 (EC 3.4.11.2) inhibitors: chemistry, biological evaluations, and therapeutic prospects.Medicinal research reviews · 2006Review
- Aminopeptidase inhibitors bestatin and actinonin inhibit cell proliferation of myeloma cells predominantly by intracellular interactions.Cancer letters · 2002Article
- Possible contribution of aminopeptidase N (APN/CD13) to invasive potential enhanced by interleukin-6 and soluble interleukin-6 receptor in human osteosarcoma cell lines.Clinical & experimental metastasis · 1999Article
- Regulation of the expression of aminopeptidase A, aminopeptidase N/CD13 and dipeptidylpeptidase IV/CD26 in renal carcinoma cells and renal tubular epithelial cells by cytokines and cAMP-increasing mediators.Clinical and experimental immunology · 1998Article
- Rapid mitogen-induced aminopeptidase N surface expression in human T cells is dominated by mechanisms independent of de novo protein biosynthesis.Immunobiology · 1997Article
- Induction of the membrane alanyl aminopeptidase gene and surface expression in human T-cells by mitogenic activation.The Biochemical journal · 1996Article
- Biology of metastasis and its clinical implications: renal-cell cancer.World journal of urology · 1996Review
- Human melanoma invasion and metastasis enhancement by high expression of aminopeptidase N/CD13.Clinical & experimental metastasis · 1995Article
- Tumor cell attachment to laminin promotes degradation of the extracellular matrix and cell migration in high-metastatic clone cells of RCT sarcoma in vitro.Japanese journal of cancer research : Gann · 1995Article
- Modulation of urokinase and urokinase receptor gene expression in human renal cell carcinoma.The American journal of pathology · 1995Article
- Serum levels of laminin, type IV collagen and type III procollagen peptide as markers for detection of metastasis.Japanese journal of cancer research : Gann · 1994Article
- Expression of aminopeptidase N on human choriocarcinoma cells and cell growth suppression by the inhibition of aminopeptidase N activity.Japanese journal of cancer research : Gann · 1994Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have investigated the effect of the immunomodulator ubenimex (hereafter referred to as bestatin) on the enzymatic degradation of the extracellular matrix by human renal cell carcinoma SN12M cells during the invasive process. The invasion of SN12M cells into reconstituted basement membrane (Matrigel) was inhibited by the presence of bestatin in a concentration-dependent manner. However, bestatin did not have any effect on tumor cell adhesion and migration to the extracellular matrices which may be involved in tumor cell invasion. Bestatin inhibited the degradation of type IV collagen by tumor cells, but not by tumor-conditioned medium (TCM), in a concentration-dependent manner. We also found that bestatin inhibited hydrolysing activities towards substrates of aminopeptidases in SN12M cells. Since bestatin was found to inhibit aminopeptidase activity, the inhibition of tumor invasion by bestatin is likely to be associated with its action as an enzyme inhibitor. Bestatin only slightly inhibited tumor cell plasmin activity, which can lead to the conversion of the latent collagenase to the active form, but this slight effect was not significant. The zymography of TCM from SN12M cells showed that the treatment of tumor cells with bestatin resulted in the disappearance of the 68 kDa type IV collagenase-enzyme level (active form) and slight reduction of the 72 kDa type IV collagenase-enzyme level (latent form). These results indicated that bestatin may inhibit tumor cell invasion through a mechanism involving its inhibitory action on aminopeptidases in tumor cells, suggesting that the aminopeptidase may partly be associated with the conversion of a latent form of type IV procollagenase to an active form or the secretion of the collagenases from tumor cells.
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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.