A monoclonal antibody to human platelet glycoprotein IIIa detects a related protein in cultured human endothelial cells.

Thiagarajan, Perumal; Shapiro, Sandor S.; Levine, Elliot M.; DeMarco, Luiz; Yalçın, A. Süha

doi:10.1172/jci111789

Cited by 120 publications

(48 citation statements)

References 44 publications

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“…Membrane proteins similar to GP Ilb-Ila are found in white blood cells (40) and endothelial cells (41,42); TSP is synthesized and secreted by monocytes (43) and endothelial cells (44); and GMP-140 is present in endothelial cells (45). Therefore in whole blood, these antigens may not be only derived from platelets.…”

Section: Resultsmentioning

confidence: 99%

Platelet surface glycoproteins. Studies on resting and activated platelets and platelet membrane microparticles in normal subjects, and observations in patients during adult respiratory distress syndrome and cardiac surgery.

George¹,

Pickett²,

Saucerman³

et al. 1986

J. Clin. Invest.

451

164

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The accurate definition of surface glycoprotein abnormalities in circulating platelets may provide better understanding of bleeding and thrombotic disorders. Platelet surface glycoproteins were measured on intact platelets in whole blood and platelet membrane microparticles were assayed in cell-free plasma using 125I-monoclonal antibodies. The glycoproteins (GP) studied were: GP lb and GP Ilb-Illa, two of the major intrinsic plasma membrane glycoproteins; GMP-140, an a-granule membrane glycoprotein that becomes exposed on the platelet surface following secretion; and thrombospondin (TSP), an a-granule secreted glycoprotein that rebinds to the platelet surface. Thrombin-induced secretion in normal platelets caused the appearance of GMP-140 and TSP on the platelet surface, increased exposure of GP Ilb-Illa, and decreased antibody binding to GP lb. Patients with adult respiratory distress syndrome had an increased concentration of GMP-140 and TSP on the surface of their platelets, demonstrating in vivo platelet secretion, but had no increase of platelet microparticles in their plasma. In contrast, patients after cardiac surgery with cardiopulmonary bypass demonstrated changes consistent with membrane fragmentation without secretion: a decreased platelet surface concentration of GP lb and GP 1Ib with no increase of GMP-140 and TSP, and an increased plasma concentration of platelet membrane microparticles. These methods will help to define acquired abnormalities of platelet surface glycoproteins.

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Section: Resultsmentioning

confidence: 99%

Platelet surface glycoproteins. Studies on resting and activated platelets and platelet membrane microparticles in normal subjects, and observations in patients during adult respiratory distress syndrome and cardiac surgery.

George¹,

Pickett²,

Saucerman³

et al. 1986

J. Clin. Invest.

451

164

View full text Add to dashboard Cite

show abstract

“…In contrast, Thiagarajan et al (33) used both a monoclonal and a polyclonal antibody, each having specificity for only GPUIa, to detect a related protein in endothelial ceils. Though these authors suggested that a GPl/b-like molecule was unlikely to be present in cultured endothelium, their argument was in part based upon their unpublished observations that the anti-platelet GPllb-specific monoclonal antibody, Tab (19,20), was unreactive with endothelial cells.…”

Section: Discussionmentioning

confidence: 99%

“…Based upon the resuits shown in Figs. 1 and 2, we adopted the convention suggested by Thiagarajan et al (33) to term the endothelial cell analogue of platelet GPIIb-IIIa, EC GPIIb, and EC GPffla, respectively.…”

Section: Identification Of Platelet Membrane Gpiib and Gpiiia Analogumentioning

confidence: 99%

“…on other cell types, including human erythroleukemia cell lines (7,32) and avian thrombocytes (15), as well. In particular, Thiagarajan et al have recently described the synthesis and expression of a GPllla analogue in cultured human endothelial cells (33). Interestingly, they could not detect the presence of a GPIIb-like molecule using any of the methods used in their study3 Since most of the functions ascribed to GPIIIa in human platelets require its calcium-dependent association with GPI/b, we were interested in investigating whether GPI/b is present in endothelial cells, and whether it is associated with GPIIIa, as it is in platelets.…”

mentioning

confidence: 99%

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Synthesis by cultured human umbilical vein endothelial cells of two proteins structurally and immunologically related to platelet membrane glycoproteins IIb and IIIa.

Newman¹,

Kawai²,

Montgomery³

et al. 1986

The Journal of Cell Biology

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“…However, in addition to the nearly 1 ϫ 10 6 molecules of PECAM-1 present on their cell surface (24), HUVECs also express 100,000 copies of the integrin ␣ v ␤ 3 (25) as well as abundant levels of heparan sulfate and chondroitin sulfate (26,27). ␣ v ␤ 3 has previously been shown not to be involved in PECAM-1 proteoliposome (14) or PECAM-1/IgG (19) binding.…”

Section: Interaction Of Pecam-1/igg With Cells Correlates With Cellmentioning

confidence: 99%

Cell Surface Glycosaminoglycans Do Not Serve as Ligands for PECAM-1

Sun¹,

Paddock²,

Visentin³

et al. 1998

Journal of Biological Chemistry

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Previous studies have suggested that PECAM-1 mediates cellular interactions via both homophilic and heterophilic adhesive mechanisms. Cell surface glycoaminoglycans have been implicated as one of the heterophilic ligands for PECAM-1. To determine whether PECAM-1 is capable of interacting directly with glycosaminoglycans, we examined the adhesive properties of multiple monovalent and multivalent forms of this adhesion molecule. We found that the binding of a bivalent PECAM-1/IgG chimeric protein or multivalent PECAM-1-containing proteoliposomes to multiple different cell lines was 1) strictly dependent upon cell surface expression of PECAM-1 and 2) unaffected by the presence of excess heparin or heparan sulfate. The extracellular domain of PECAM-1 failed to interact specifically with heparinSepharose, 3 H-labeled heparin, or a heparin-bovine serum albumin conjugate. In addition, an amino acid sequence motif inadvertently created by the juxtaposition of PECAM-1 and IgG sequences within the hinge region of certain PECAM-1/IgG chimeric constructs was found to confer glycosaminoglycan binding properties not normally present within the extracellular domain of the native molecule. Together, these data suggest that the mechanism by which heparin is able to affect PECAM-1-dependent cell-cell adhesion is indirect and occurs via inhibition of events that occur downstream from PECAM-1 engagement.PECAM-1 (CD31) is a 130-kDa member of the Ig gene superfamily that is constitutively expressed on the surface of circulating platelets, monocytes, neutrophils, and selected T cell subsets. It is also present at relatively high concentration at the cell junctions of all continuous endothelium, both in vivo and in cell culture (for a recent review on the biology of PECAM-1, see Ref. 1). Because of its presence on these vascular cells, PECAM-1 has been implicated in mediating a number of cellular interactions, most notably those that take place between leukocytes and the vessel wall during the process of transendothelial migration (2-9) and between adjacent endothelial cells during the process of angiogenesis (10 -12).A number of different cell surface components have been implicated as counterreceptors or cellular targets for PECAM-1. Albelda et al. (13) found that PECAM-1 became concentrated at cell-cell borders only if both cells expressed PECAM-1, and they were the first to propose, based on this observation, that PECAM-1-mediated cellular interactions might operate homophilically, i.e. via PECAM-1/PECAM-1 intermolecular contacts. In support of this hypothesis, PECAM-1-containing proteoliposomes were recently shown to be able to self-associate in a concentration-dependent, divalent cationindependent, manner (14), providing direct experimental support that PECAM-1 is capable of interacting with itself. Homophilic binding activity requires amino-terminal Ig homology domains 1 and 2 (14, 15), and specific residues within Ig domain 1 that participate in PECAM-1/PECAM-1 interactions have recently been identified by Newton et al. (16). ...

show abstract

A monoclonal antibody to human platelet glycoprotein IIIa detects a related protein in cultured human endothelial cells.

Abstract: We have previously described a series of monoclonal

Cited by 120 publications

References 44 publications

Platelet surface glycoproteins. Studies on resting and activated platelets and platelet membrane microparticles in normal subjects, and observations in patients during adult respiratory distress syndrome and cardiac surgery.

Platelet surface glycoproteins. Studies on resting and activated platelets and platelet membrane microparticles in normal subjects, and observations in patients during adult respiratory distress syndrome and cardiac surgery.

Synthesis by cultured human umbilical vein endothelial cells of two proteins structurally and immunologically related to platelet membrane glycoproteins IIb and IIIa.

Cell Surface Glycosaminoglycans Do Not Serve as Ligands for PECAM-1

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