<b>BINDING OF HUMAN PLACENTAL RIBONUCLEASE INHIBITOR TO EXTRACELLULAR MATRIX </b><b>MOLECULES </b>
نویسندگان
چکیده
منابع مشابه
Human placental ribonuclease inhibitor abolishes both angiogenic and ribonucleolytic activities of angiogenin.
Human placental ribonuclease inhibitor (PRI) abolishes both the ribonucleolytic activity of angiogenin toward 28S and 18S rRNA and its angiogenic activity on the chicken embryo chorioallantoic membrane. Treatment of the angiogenin-PRI complex with p-hydroxymercuribenzoate releases enzymatically active angiogenin. Assays measuring competition between angiogenin and bovine pancreatic ribonuclease...
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Human angiogenin (ANG) is a homologue of bovine pancreatic ribonuclease (RNase A) that induces neovascularization. ANG is the only human angiogenic factor that possesses ribonucleolytic activity. To stimulate blood vessel growth, ANG must be transported to the nucleus and must retain its catalytic activity. Like other mammalian homologues of RNase A, ANG forms a femtomolar complex with the cyto...
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The ribonuclease inhibitor protein (RI) binds to members of the bovine pancreatic ribonuclease (RNase A) superfamily with an affinity in the femtomolar range. Here, we report on structural and energetic aspects of the interaction between human RI (hRI) and human pancreatic ribonuclease (RNase 1). The structure of the crystalline hRI x RNase 1 complex was determined at a resolution of 1.95 A, re...
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Recirculation of normal and neoplastic lymphocytes occurs via binding to the endothelial luminar surface, followed by extravasation and the subsequent interaction of the cells with components of the underlying basement membrane and stromal extracellular matrix (ECM). To identify matrix constituents that could be involved in the tissue dissemination of neoplastic B cells, we have examined the ab...
متن کاملMolecular recognition of human angiogenin by placental ribonuclease inhibitor--an X-ray crystallographic study at 2.0 A resolution.
Human placental RNase inhibitor (hRI), a leucine-rich repeat protein, binds the blood vessel-inducing protein human angiogenin (Ang) with extraordinary affinity (Ki <1 fM). Here we report a 2.0 A resolution crystal structure for the hRI-Ang complex that, together with extensive mutagenesis data from earlier studies, reveals the molecular features of this tight interaction. The hRI-Ang binding i...
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ژورنال
عنوان ژورنال: Biomedical Research
سال: 1993
ISSN: 0388-6107,1880-313X
DOI: 10.2220/biomedres.14.123