We are analyzing https://link.springer.com/article/10.1007/s10456-013-9360-y.

Title:
Prostate specific membrane antigen produces pro-angiogenic laminin peptides downstream of matrix metalloprotease-2 | Angiogenesis
Description:
Prostate specific membrane antigen (PSMA) is a pro-angiogenic cell-surface protease that we previously demonstrated regulates blood vessel formation in a laminin and integrin β1-dependent manner. Here, we examine the principal mechanism of PSMA activation of integrin β1. We show that digesting laminin sequentially with recombinant matrix metalloprotease-2 (MMP-2) and PSMA generates small peptides that enhance endothelial cell adhesion and migration in vitro. We also provide evidence that these laminin peptides activate adhesion via integrin α6β1 and focal adhesion kinase. Using an in vivo Matrigel implant assay, we show that these MMP/PSMA-derived laminin peptides also increase angiogenesis in vivo. Together, our results reveal a novel mechanism of PSMA activation of angiogenesis by processing laminin downstream of MMP-2.
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Keywords {🔍}

google, scholar, article, cas, pubmed, cancer, cell, laminin, angiogenesis, biol, matrix, res, prostate, membrane, integrin, tumor, antigen, cells, chem, human, endothelial, peptides, mmp, doijbcm, peptide, extracellular, migration, prostatespecific, metalloproteinase, adhesion, role, expression, growth, breast, specific, conway, hannah, psma, progression, int, yamada, inhibitor, heston, privacy, cookies, content, metalloprotease, access, laminins, nomizu,

Topics {✒️}

pro-angiogenic cell-surface protease prostate-specific membrane antigen month download article/chapter mmp/psma-derived laminin peptides prostate specific antigen endostatin-derived peptide interacts endothelial cell-specific inhibitor extracellular matrix-derived chemoattractant c1-complex autoactivation revealed processing laminin downstream glucocorticoid receptor-mediated suppression integrin β1-dependent manner preliminary research leading related subjects active laminin-1 sequence laminin fragment interactions full article pdf angiogenic blood vessels article angiogenesis aims endothelial cell adhesion potent peptide antagonist laminin α5-chain copper-binding peptides extracellular matrix modulate extracellular matrix macromolecules extracellular matrix degradation anti-angiogenic effects transformed endothelial cells privacy choices/manage cookies vascular extracellular matrix epithelial prostatic cells polymerase chain reaction capillary tube formation matrix-derived inhibitor aging-related alterations regulates actin cytoskeleton van houwelingen ah matrix metalloproteinase expression murine melanoma cells tumor-derived laminin-511 matrix metalloprotease-2 cleavage neuroendocrine prostate carcinogenesis human epidermal cells human hepatocellular carcinoma map kinase signalling sustains endothelial-vegf recombinant matrix metalloprotease-2 cell-substrate adhesion laminin α1 laminin gamma chains

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         description:Prostate specific membrane antigen (PSMA) is a pro-angiogenic cell-surface protease that we previously demonstrated regulates blood vessel formation in a laminin and integrin β1-dependent manner. Here, we examine the principal mechanism of PSMA activation of integrin β1. We show that digesting laminin sequentially with recombinant matrix metalloprotease-2 (MMP-2) and PSMA generates small peptides that enhance endothelial cell adhesion and migration in vitro. We also provide evidence that these laminin peptides activate adhesion via integrin α6β1 and focal adhesion kinase. Using an in vivo Matrigel implant assay, we show that these MMP/PSMA-derived laminin peptides also increase angiogenesis in vivo. Together, our results reveal a novel mechanism of PSMA activation of angiogenesis by processing laminin downstream of MMP-2.
         datePublished:2013-06-18T00:00:00Z
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            Extracellular matrix
            Prostate specific membrane antigen
            Matrix metalloproteases
            Cancer Research
            Biomedicine
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            Cardiology
            Ophthalmology
            Oncology
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      headline:Prostate specific membrane antigen produces pro-angiogenic laminin peptides downstream of matrix metalloprotease-2
      description:Prostate specific membrane antigen (PSMA) is a pro-angiogenic cell-surface protease that we previously demonstrated regulates blood vessel formation in a laminin and integrin β1-dependent manner. Here, we examine the principal mechanism of PSMA activation of integrin β1. We show that digesting laminin sequentially with recombinant matrix metalloprotease-2 (MMP-2) and PSMA generates small peptides that enhance endothelial cell adhesion and migration in vitro. We also provide evidence that these laminin peptides activate adhesion via integrin α6β1 and focal adhesion kinase. Using an in vivo Matrigel implant assay, we show that these MMP/PSMA-derived laminin peptides also increase angiogenesis in vivo. Together, our results reveal a novel mechanism of PSMA activation of angiogenesis by processing laminin downstream of MMP-2.
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         Extracellular matrix
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         Matrix metalloproteases
         Cancer Research
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         Cardiology
         Ophthalmology
         Oncology
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