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Open AccessJournal ArticleDOI

Isolation of the thrombospondin membrane receptor.

TLDR
An 88-kD membrane glycoprotein present in platelets, endothelial cells, monocytes, and a variety of human tumor cell lines that is the membrane binding site for TSP is identified and isolated and may function as the cellular TSP receptor.
Abstract
Thrombospondin (TSP), a 450-kD multifunctional glycoprotein with a broad tissue distribution, is secreted upon platelet stimulation, binds to the activated platelet surface, and supports platelet aggregation. We have identified and isolated an 88-kd membrane glycoprotein present in platelets, endothelial cells, monocytes, and a variety of human tumor cell lines that is the membrane binding site for TSP. Endogenous platelet TSP binding to thrombin- and ionophore-stimulated human platelets was inhibited in the presence of the monoclonal antibody OKM5. TSP binding to C32 melanoma cells and HT1080 fibrosarcoma cells was specific and also inhibitable with OKM5 Mab. Cell labeling followed by specific immunoprecipitation demonstrated biosynthesis of a single 88-kD glycoprotein. Binding of TSP to the isolated membrane protein was specific and saturable. These studies identify an 88-kD membrane glycoprotein that reacts with the monoclonal antibody, OKM5, and may function as the cellular TSP receptor.

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PPARγ Promotes Monocyte/Macrophage Differentiation and Uptake of Oxidized LDL

TL;DR: It is demonstrated that the nuclear receptor PPARγ is induced in human monocytes following exposure to oxLDL and is expressed at high levels in the foam cells of atherosclerotic lesions, and it is suggested that endogenous PParγ ligands may be important regulators of gene expression during atherogenesis.
Journal ArticleDOI

Inferences, questions and possibilities in Toll-like receptor signalling

TL;DR: The Toll-like receptors are the key proteins that allow mammals — whether immunologically naive or experienced — to detect microbes and many inflammatory processes, both sterile and infectious, may depend on TLR signalling.
Journal ArticleDOI

CD36, a Scavenger Receptor Involved in Immunity, Metabolism, Angiogenesis, and Behavior

TL;DR: CD36 binds to several major classes of ligands, including the matrix protein thrombospondin, long-chain fatty acids, and oxidized phospholipids and lipoproteins; in different contexts, it serves to regulate angiogenesis, innate immune responses, fatty acid metabolism, and sensory responses to fatty acids.
Journal ArticleDOI

Expression cloning of SR-BI, a CD36-related class B scavenger receptor.

TL;DR: SR-BI and CD36 define a second class of scavenger receptors, designated class B, whose predicted protein sequence of 509 amino acids is approximately 30% identical to those of the four previously identified family members.
Journal ArticleDOI

Thrombospondin cooperates with CD36 and the vitronectin receptor in macrophage recognition of neutrophils undergoing apoptosis.

TL;DR: Newly defined roles for TSP and CD36 in phagocytic clearance of senescent neutrophils, which may limit inflammatory tissue injury and promote resolution are indicated.
References
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Journal ArticleDOI

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
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Ligand: a versatile computerized approach for characterization of ligand-binding systems.

TL;DR: This approach provides two major advantages compared with other available methods: it uses an exact mathematical model of the ligand-binding system, thereby avoiding the possible biases introduced by several commonly used approximations and it uses a statistically valid, appropriately weighted least-squares curve-fitting algorithm with objective measurement of goodness of fit.
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Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule

TL;DR: The ability of fibronectin to bind cells can be accounted for by the tetrapeptide L-arginyl-glycyl- L-aspartyl-L-serine, a sequence which is part of the cell attachment domain of fibronsectin and present in at least five other proteins.
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Identification and isolation of a 140 kd cell surface glycoprotein with properties expected of a fibronectin receptor

TL;DR: Affinity chromatography on wheat germ agglutinin-Sepharose showed that the 140 kd protein is a glycoprotein and, in combination with the fibronectin fragment chromatography, gave highly enriched preparations of the 140Kd protein.
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Platelet membrane glycoprotein IIb/IIIa: member of a family of Arg-Gly-Asp--specific adhesion receptors

TL;DR: The results establish the existence of a family of adhesion receptors that recognize the sequence Arg-Gly-Asp, which corresponds to the cell adhesion site in fibronectin and is also present in the alpha chain of fibrinogen.
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