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PubMed1999

[Vitronectin].

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Female↗
PubMed1999

Design and characterization of orally active Arg-Gly-Asp peptidomimetic vitronectin receptor antagonist SB 265123 for prevention of bone loss in osteoporosis.

The Arg-Gly-Asp (RGD)-binding integrin alpha(V)beta(3) is highly expressed on osteoclasts and has been proposed to mediate cell-matrix adhesion required for osteoclast-mediated bone resorption. Antagonism of this receptor should prevent stable osteoclast adhesion and thereby inhibit bone resorption. We have generated an orally bioavailable, nonpeptide RGD mimetic alpha(v)beta(3) antagonist, SB 265123, which prevents bone loss in vivo when dosed by oral administration. SB 265123 binds alpha(v)beta(3) and the closely related integrin alpha(v)beta(5) with high affinity (K(i) = 3.5 and 1.3 nM, respectively), but binds only weakly to the related RGD-binding integrins alpha(IIb)beta(3) (K(i) >1 microM) and alpha(5)beta(1) (K(i) >1 microM). The compound inhibits alpha(v)beta(3)-mediated cell adhesion with an IC(50) = 60 nM and more importantly, inhibits human osteoclast-mediated bone resorption in vitro with an IC(50) = 48 nM. In vivo, SB 265123 completely blocks bone resorption in a thyroparathyroidectomized rat model of acute bone resorption when dosed at 2.5 mg/kg/h by continuous i.v. infusion. When dosed orally with 3 to 30 mg/kg b.i.d. , in the ovariectomy-induced rat model of osteoporosis, SB 265123 prevents bone resorption in a dose-dependent fashion. This is the first report of an orally active alpha(v)beta(3) antagonist that is effective at inhibiting bone resorption when dosed in a pharmaceutically acceptable fashion. Such a molecule may provide a novel therapeutic agent for the treatment of postmenopausal osteoporosis.

Acetates↗
PubMed1991

Vitronectin.

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Amino Acid Sequence↗
PubMed1988

Terminal complement complex (TCC) and S-protein (vitronectin) on follicular dendritic cells in human lymphoid tissues.

Follicular dendritic cells (FDC) present in germinal centres trap considerable amounts of C3-containing immune complexes (IC). Activation of the terminal pathway of complement (C) on biological membranes normally generates C5b-9(m), which is the membranolytic form of the terminal complement complex (TCC). By contrast, when C activation takes place in the extracellular fluid phase, S-protein binds to C5b-7 and the non-lytic soluble SC5b-9 is formed. In this study deposits of C3d, C5, C9 TCC neoepitope and S-protein were demonstrated by immunohistochemistry on FDC in human tonsils, lymph nodes, spleens, appendices and colonic mucosae. TCC and S-protein were likewise observed on FDC in imprints from tonsils. The identical spatial distribution revealed by paired staining suggested that TCC had been generated in situ. The staining intensity for TCC and S-protein varied in parallel, which suggested that the S-protein may be incorporated in the membrane-bound TCC--perhaps rendering it non-lytic. However, the actual mechanism and function of the observed TCC and associated S-protein deposition needs further elucidation.

Complement Membrane Attack Complex↗
PubMed1989

A novel beta-endorphin binding protein. Complement S protein (= vitronectin) exhibits specific non-opioid binding sites for beta-endorphin upon interaction with heparin or surfaces.

Human beta-endorphin (1-31) (beta H-endorphin) was found to specifically interact with purified complement S protein from human plasma. As found by chemical cross-linking beta H-endorphin bound to both, the 65- and 75-kDa molecular mass forms of S protein. The interaction of S protein with heparin as well as the adsorption of S protein to surfaces led to an almost 10-fold increase of specific binding which was due to the exposure of further beta H-endorphin-binding sites. The interaction of beta H-endorphin with S protein bore characteristics of a ligand-receptor interaction, such as time dependence, reversibility, high affinity, saturability, and structural specificity and was mediated through the non-opioid COOH terminus of the beta H-endorphin molecule. beta H-Endorphin binding to S protein was observed at physiological pH or cation concentrations, indicating that the interaction may well occur in vivo. Our results provide conclusive evidence that interactions of S protein with very different effectors led to similar conformational changes which uniformly resulted in exposure of a highly specific beta H-endorphin binding domain on S protein. With S protein as major beta H-endorphin-binding protein in the periphery, the molecular basis of a widespread system of humoral target sites of the neuroendocrine effector appears to be established. In view of S protein involvement in processes of inflammation and wound repair and beta-endorphin effects on immunocompetent cells, the demonstrated S protein-beta H-endorphin interaction appears to be of considerable functional significance.

Binding Sites↗
PubMed1995

[Vitronectin].

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Humans↗
PubMed1998

CD36 is required for phagocytosis of apoptotic cells by human macrophages that use either a phosphatidylserine receptor or the vitronectin receptor (alpha v beta 3).

In vivo, apoptotic cells are efficiently removed by professional or nonprofessional phagocytes, a process thought to be essential for tissue remodeling and resolution of inflammation. Macrophages recognize apoptotic cells by several mechanisms, including recognition of exposed phosphatidylserine (PS); however, PS recognition on apoptotic cells has not been identified as a feature of human macrophages. The purpose of this study was to determine whether human monocyte-derived macrophages could be stimulated to recognize PS, defined as inhibition of phagocytosis by PS-containing liposomes. We also assessed the potential roles for scavenger receptors, CD14, and lectins. Uptake of apoptotic neutrophils into unstimulated macrophages was blocked about 50% by Arg-Gly-Asp-Ser and anti-alpha(v), and up to 20% by oxidized low density lipoprotein and N-acetylglucosamine, implying a major role for integrin and minor roles for scavenger and lectin receptors. Uptake into macrophages stimulated with beta-1,3-glucan was blocked 50% by PS liposomes and 40% by oxidized low density lipoprotein, suggesting that the macrophages had switched from using integrin to recognition of PS. MEM-18 and 61D3 (anti-CD14 mAbs) were poor inhibitors of apoptotic neutrophil uptake, but good inhibitors of apoptotic lymphocyte uptake. The switch to PS recognition was accompanied by down-regulation of alpha(v)beta3 expression and function. Anti-CD36 blocked uptake into unstimulated or stimulated macrophages, suggesting CD36 involvement not only with the alpha(v)beta3 integrin mechanism (as previously reported) but also with PS recognition. A maximum of 70% inhibition was achieved by combining anti-CD36 with either anti-a(v) or PS liposomes.

Adult↗