Molecular differences of exposed surface proteins on thrombasthenic platelet plasma membranes

Phillips, David R.; Jenkins, C. S. P.; Lüscher, E. F.; Larrieu, M J

doi:10.1038/257599a0

Cited by 147 publications

(72 citation statements)

References 11 publications

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“…Glycoprotein Illa (GPIIIa) is a 91.5 kDa major component of the platelet membrane (Clemetson, 1985;Usobiaga et al, 1987) which together with GPIIb functions as a receptor for fibrinogen (Plow et al, 1986) and other proteins, and plays a primary role in platelet aggregation (Nurden & Caen, 1974;Phillips et al, 1975). GPIIb and GPIIIa have been isolated and characterized in several laboratories, both as individual glycoproteins or as a GPIIb-GPIIIa complex (Leung et al, 1981;McEver et al, 1982;Jennings & Phillips, 1982;Eirin et al, 1986), and specific monoclonal antibodies have been raised to each of them as well as for the complex (McGregor, 1986).…”

Section: Introductionmentioning

confidence: 99%

Tryptic digestion of human GPIIIa. Isolation and biochemical characterization of the 23 kDa N-terminal glycopeptide carrying the antigenic determinant for a monoclonal antibody (P37) which inhibits platelet aggregation

Calvete

Rivas

Maruri

et al. 1988

Biochemical Journal

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Early digestion of pure human platelet glycoprotein Illa (GPIIIa) leads to a single cleavage of the molecule at 23 kDa far from one of the terminal amino acids. Automated Edman degradation demonstrates that GPIIIa and the smaller (23 kDa) tryptic fragment share the same N-terminal amino acid sequence. A further cleavage occurs in the larger fragment (80 kDa), reducing its apparent molecular mass by 10 kDa. The 23 kDa fragment remains attached to the larger ones in unreduced samples. Stepwise reduction of early digested GPIIIa with dithioerythritol selectively reduces the single disulphide bond joining the smaller (23 kDa) to the larger (80/70 kDa) fragments. Two fractions were obtained by size-exclusion chromatography of early digested GPIIIa after partial or full reduction and alkylation. The larger-size fraction contains the 80/70 kDa fragments, while the 23 kDa fragment is isolated in the smaller. The amino acid compositions of these fractions do not differ very significantly from the composition of GPIIIa; however the 23 kDa fragment contains only 10.2% by weight of sugars and is richer in neuraminic acid. Disulphide bonds are distributed four in the 23 kDa glycopeptide and 20-21 in the 80/70 kDa glycopeptide. The epitope for P37, a monoclonal antibody which inhibits platelet aggregation [Melero & Gonzailez-Rodriguez (1984) Eur. J. Biochem. 141, 421-427] is situated within the first 17 kDa of the N-terminal region of GPIIIa, which gives a special functional interest to this extracellular region of GPIIIa. On the other hand, the epitopes for GPIIIa-specific monoclonal antibodies, P6, P35, P40 and P97, which do not interfere with platelet aggregation, are located within the larger tryptic fragment (80/70 kDa). Thus, the antigenic areas available in the extracellular surface of GPIIIa for these five monoclonal antibodies are now more precisely delineated.

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Section: Introductionmentioning

confidence: 99%

Tryptic digestion of human GPIIIa. Isolation and biochemical characterization of the 23 kDa N-terminal glycopeptide carrying the antigenic determinant for a monoclonal antibody (P37) which inhibits platelet aggregation

Calvete

Rivas

Maruri

et al. 1988

Biochemical Journal

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“…Both GpIIb and GpIIIa are glycosylated [11,12] and form a heterodimeric complex non-covalently linked to the rough endoplasmic reticulum [13]. In Glanzmann's thrombasthenia they are both absent, leading to a lack of aggregation in response to common platelet agonists [14,15]. The GpIb/IX/V (CD42), otherwise vWF receptor, is also unique for the MK lineage, even though similar proteins may be expressed by activated endothelial cells in response to cytokines [16].…”

Section: Antigenic Targetsmentioning

confidence: 99%

SLE Thrombocytopenia: From Peripheral Platelet Destruction to Central Hemopoietic Defect

Ziakas¹

2008

TOHJ

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“…netic understanding of the disease process and for rational therapy. "quaking" mice and phillips et (30) used 1251: 3 ~-l~~~ dase-labeled platelet membranes to demonstrate glycoprotein ab-…”

Section: Double Labeling Techniquesmentioning

confidence: 99%

Searching for Molecular Abnormalities in Genetic Diseases by the Use of a Double Labeling Technique. I. Rationale, Techniques, and Initial Evaluation

Pena

Wrogemann

1978

Pediatr Res

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Molecular differences of exposed surface proteins on thrombasthenic platelet plasma membranes

Cited by 147 publications

References 11 publications

Tryptic digestion of human GPIIIa. Isolation and biochemical characterization of the 23 kDa N-terminal glycopeptide carrying the antigenic determinant for a monoclonal antibody (P37) which inhibits platelet aggregation

Tryptic digestion of human GPIIIa. Isolation and biochemical characterization of the 23 kDa N-terminal glycopeptide carrying the antigenic determinant for a monoclonal antibody (P37) which inhibits platelet aggregation

SLE Thrombocytopenia: From Peripheral Platelet Destruction to Central Hemopoietic Defect

Searching for Molecular Abnormalities in Genetic Diseases by the Use of a Double Labeling Technique. I. Rationale, Techniques, and Initial Evaluation

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