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Analytical Biochemistry | 1985

A method for purifying the platelet membrane glycoprotein IIb-IIIa complex

Laurence A. Fitzgerald; Betty Leung; David R. Phillips

A method has been developed for the rapid isolation of platelet membrane glycoproteins (GP) IIb and IIIa. This method produces an excellent yield and does not require the prior isolation of platelet membranes. Outdated platelets were washed and solubilized in Triton X-100. Concanavalin A affinity chromatography was used to purify a platelet glycoprotein fraction. The concanavalin A-retained glycoproteins were eluted and adsorbed with a heparin-Sepharose column to remove a major contaminant, thrombospondin. Sephacryl S-300 gel filtration was used as the final purification step to remove most fibrinogen and low-molecular-weight contaminants. Wheat germ agglutinin affinity chromatography was used to completely remove trace amounts of fibrinogen. The purified GP IIb and GP IIIa were analyzed by sucrose gradient sedimentation and found to consist of heterodimer complexes.


Experimental Biology and Medicine | 1987

Inhibition of human tumor cell induced platelet aggregation by antibodies to platelet glycoproteins Ib and IIb/IIIa

Irma M. Grossi; Laurence A. Fitzgerald; A Kendall; John D. Taylor; Bonnie F. Sloane; Kenneth V. Honn

Abstract Tumor cell induced platelet aggregation was shown to be inhibited in a dose dependent manner by preincubation of human platelets with antibodies to platelet glycoprtein lb and the llb/llla complex. Combination of antibody to lb and antibody to the llb/llla complex at concentrations which produced half maximal inhibition of platelet aggregation alone caused complete inhibition of tumor cell induced platelet aggregation. Antibodies to platelet glycoproteins lb and the llb/llla complex also inhibited platelet synthesis of thromboxane A2, but not synthesis of 12-hydroxyeicosatrienoic acid. Inhibition of tumor cell induced platelet aggregation with antibodies against platelet glycoproteins suggests a role for these glycoproteins in tumor cell-platelet interactions and possibly platelet facilitated tumor cell metastasis.


Experimental Biology and Medicine | 1988

Lipoxygenase products regulate IRGpIIb/IIIa receptor mediated adhesion of tumor cells to endothelial cells, subendothelial matrix and fibronectin.

Kenneth V. Honn; Irma M. Grossi; Laurence A. Fitzgerald; Lillian A. Umbarger; Clement A. Diglio; John D. Taylor

Abstract Tumor cell adhesion to endothelial cells, subendothelial matrix, and fibronectin is stimulated by the lipoxygenase metabolite of arachidonic acid, 12(S)-HETE, but not by 12(R)-HETE, 5-HETE or 15-HETE. Adhesion is also stimulated by the phorbol ester TPA, an effect inhibited by lipoxygenase but not cyclooxygenase inhibitors.TPA and 12(S)-HETE mediated adhesion is due, in part, to an integrin receptor (i.e., IRGpllb/llla) related to the platelet glycoprotein llb/llla complex and is inhibited by specific monoclonal and polyclonal antibodies against platelet llb/llla. TPA and 12(S)-HETE stimulated adhesion is also inhibited by a lipoxygenase product of linoleic acid; i.e., 13-HODE. These results suggest bidirectional control of tumor cell adhesion by lipoxygenase products of arachidonic acid (increase) and linoleic acid (decrease).


Annals of the New York Academy of Sciences | 1987

The platelet membrane glycoprotein IIb/IIIa complex. Structure, function, and relationship to adhesive protein receptors in nucleated cells.

David R. Phillips; Laurence A. Fitzgerald; Israel F. Chard; Parise Lv

The GPIIb/IIIa complex functions as the aggregation site on the platelet membrane surface. This complex has been purified, characterized biochemically and morphologically, and reconstituted into phospholipid vesicles. Fibrinogen and fibronectin bind to reconstituted GPIIb/IIIa with many of the properties that characterize their binding to intact platelets. The GPIIb/IIIa complex appears to be a member of a widely distributed family of cell-surface glycoproteins that mediate cellular interactions. The terms cytoadhesins30 and integrins39 have been suggested for the members of this family of two-subunit molecules. The aminotermini of the alpha subunits of these molecules have been sequenced and appear to be homologous. Three beta subunits have been identified for this family of receptors, indicating that many alpha subunits have a common beta subunit. The three beta subunits have been sequenced, and there is about a 40 to 50% identity among their amino acid sequences. It thus appears that the receptors mediating cellular interactions have evolved from a common ancestral gene.


Blood | 1988

The platelet membrane glycoprotein IIb-IIIa complex

David R. Phillips; Israel F. Charo; Parise Lv; Laurence A. Fitzgerald


Biochemistry | 1987

Comparison of cDNA-derived protein sequences of the human fibronectin and vitronectin receptor .alpha.-subunits and platelet glycoprotein IIb

Laurence A. Fitzgerald; Mortimer Poncz; Beat Steiner; Stanley C. Rall; Joel S. Bennett; David R. Phillips


Methods in Enzymology | 1992

Platelet membrane glycoprotein IIb-IIIa complex: purification, characterization, and reconstitution into phospholipid vesicles.

David R. Phillips; Laurence A. Fitzgerald; Leslie V. Parise; Beat Steiner


Archive | 1989

Platelet blocking peptides

Israel F. Charo; Laurence A. Fitzgerald; David R. Phillips


Annals of the New York Academy of Sciences | 1983

CALCIUM REGULATION OF GLYCOPROTEINS IIb AND IIIa IN HUMAN PLATELET MEMBRANES

David R. Phillips; Kingo Fujimura; Lisa K. Jennings; Leslie V. Parise; Laurence A. Fitzgerald; Joan E. B. Fox


Archive | 1993

Peptides derived from GPIIIa

Israel F. Charo; Laurence A. Fitzgerald; David R. Phillips

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Parise Lv

University of California

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Leslie V. Parise

University of North Carolina at Chapel Hill

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A Kendall

Wayne State University

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Betty Leung

University of California

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