ArticleMolecular pharmaceutics
In vitro evaluation of functional interaction of integrin alphavbeta3 and matrix metalloprotease-2.
Article in Molecular pharmaceutics. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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Who cites it
4 citing papers in PubMed, 10 citations in OpenAlex.
- Dual targeting of integrin αvβ3 and matrix metalloproteinase-2 for optical imaging of tumors and chemotherapeutic delivery.Molecular cancer therapeutics · 2014Article
- In-house preparation of hydrogels for batch affinity purification of glutathione S-transferase tagged recombinant proteins.BMC biotechnology · 2012Article
- Effects of molecular weight and loading on matrix metalloproteinase-2 mediated release from poly(ethylene glycol) diacrylate hydrogels.The AAPS journal · 2012Article
- Improving matrix metalloproteinase-2 specific response of a hydrogel system using electrophoresis.International journal of pharmaceutics · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Integrin alphavbeta3 and matrix metalloprotease-2 (MMP-2) are two established molecular targets of angiogenesis. Basic understanding of various forms of functional interaction of integrin alphavbeta3 and active MMP-2 may be used to develop therapeutic approaches. Based upon the idea that integrins are present on the surface of invasive cells and MMP-2 may be localized to this and other cell-surface receptors, we investigated the hypothesis that integrin binding will alter cleavage of MMP-2 substrates. To investigate this hypothesis, integrin-binding and MMP-2 cleavable motifs were combined in a single peptide, MMP-RGD, designed with fluorescent probes for monitoring peptide cleavage. MMP-RGD was bound to integrin alphavbeta3 with equal affinity compared to the integrin-binding motif and was cleaved with equal specificity by active MMP-2. MMP-RGD bound to human umbilical vein endothelial cells (HUVECs). MMP-2 from HUVECs cleaved MMP-RGD, but the cleavage was not altered due to integrin binding. Our results indicate that integrin alphavbeta3 and active MMP-2 may not be as functionally collaborative for substrate cleavage as expected based on the current knowledge of their cell surface colocalization.
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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.