Isolation of human platelet plasma membranes with polylysine beads.

Kinoshita, Tadatoshi; Nachman, Ralph L.; Minick, R

doi:10.1083/jcb.82.3.688

Cited by 30 publications

(6 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The resolution of nine to 12 membrane-bound glycoproteins in this study compares well with the identification of nine glycoproteins (Phillips & Poh Agin, 1977a), ten glycoproteins (Andersson & Gahmberg, 1978) and 11 glycoproteins (Kinoshita et al, 1979) when galactose oxidase/NaB3H4 has been used previously to label platelets. Seven glycoproteins were detected after using diazotized 251I-labelled di-iodosulphanilic acid as a surface label (George et al, 1978) and routinely only four to six glycoproteins can be detected by PAS-staining of gels (see, for example, Kinoshita et al, 1979). Two glycosylated polypeptides (glycoproteins 1 B and 2B) have been isolated by lectin affinity chromatography.…”

Section: Discussionsupporting

confidence: 61%

Interactions between platelet-surface glycoproteins. Identification of glycoproteins capable of binding to platelet surfaces

Bowles¹,

Brunton²

1982

Biochemical Journal

View full text Add to dashboard Cite

1. Platelets have been isolated from plasma and their surface glycoconjugates radioactively-labelled using galactose oxidase and NaB3H4. 2. Conditions have been defined for optimal labelling of glycoproteins and a membrane fraction enriched in plasma membrane has been prepared and characterized by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. 3. Desialylated glycoproteins that act as receptors to peanut agglutinin and lentil lectin have been purified from a detergent extract of plasma membrane. 4. Two glycosylated polypeptides that are able to bind to the surfaces of platelets have been identified and some characteristics of the binding have been investigated.

show abstract

Section: Discussionsupporting

confidence: 61%

Interactions between platelet-surface glycoproteins. Identification of glycoproteins capable of binding to platelet surfaces

Bowles¹,

Brunton²

1982

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…Meanwhile another method for platelet membrane preparation according to Kinoshita et al (30) based on binding of membranes onto polylysine-tagged beads was also tested but turned out to be unsuitable for the enrichment of pure platelet membrane proteins (data not shown). In contrast the original protocol based on ultrasonication lysis and preclearing on sorbitol gradients facilitated additional purification steps.…”

Section: Resultsmentioning

confidence: 99%

The Human Platelet Membrane Proteome Reveals Several New Potential Membrane Proteins

Moebius¹,

Zahedi²,

Lewandrowski³

et al. 2005

Molecular & Cellular Proteomics

152

134

View full text Add to dashboard Cite

We present the first focused proteome study on human platelet membranes. Due to the removal of highly abundant cytoskeletal proteins a wide spectrum of known platelet membrane proteins and several new and hypothetical proteins were accessible. In contrast to other proteome studies we focused on prefractionation and purification of membranes from human platelets according to published protocols to reduce sample complexity and enrich interesting membrane proteins. Subsequently protein separation by common one-dimensional SDS-PAGE as well as the combined benzyldimethyl-n-hexadecylammonium chloride/SDS separation technique was performed prior to mass spectrometry analysis by nano-LC-ESI-MS/MS. We demonstrate that the application of both separation systems in parallel is required for maximization of protein tagging out of a complex sample.

show abstract

“…The 3H-labeled platelet suspensions (2 X 109 platelets/ml) were exposed to either elastase (0-300 nM) or (39). After electroblotting, the nitrocellulose was incubated overnight at 4°C in phosphate-buffered saline (PBS, 100 mM NaCl, 38 mM Na2HPO4, 12.5 mM NaH2PO4, pH 7.4) containing 5% bovine serum albumin (Sigma Chemical Co., essentially fatty acid free) and 3 mM NaN3.…”

Section: Methodsmentioning

confidence: 99%

Human neutrophil elastase modulates platelet function by limited proteolysis of membrane glycoproteins.

Brower¹,

Levin²,

Garry³

1985

J. Clin. Invest.

114

View full text Add to dashboard Cite

During blood coagulation human polymorphonuclear leukocytes release elastase in amounts that can exceed 100 nmol/liter. We therefore studied the effect of elastase on platelet structure and function. Physiologic concentrations of elastase specifically inhibited thrombin-induced platelet aggregation and ristocetininduced agglutination of washed platelets in a time-and dosedependent manner. This was associated with a decrease in the number of high affinity thrombin binding sites on the platelet surface (analysis by "Ligand" program) from 31 per platelet to 12 per platelet (P < 0.05). As analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, treatment of 3H-labeled platelets with elastase resulted in a decrease in the percent glycoprotein at 130,000-150,000 Mr = and an increase in the percent protein at M, = 102,000. The supernatant from elastase-treated platelets contained a Mr = 88,000 glycoprotein not found in the supernatant from untreated platelets. Immunoprecipitation studies with monoclonal antiglycoprotein lb demonstrated that treatment of whole platelets with physiologic concentrations of elastase resulted in proteolytic cleavage of glycoprotein lb. Elastase treatment of glycoprotein immunoisolated with monoclonal antiglycoprotein lb antibody resulted in formation of a glycopeptide with the same electrophoretic mobility as the M, = 102,000 membrane-related glycopeptide.In contrast, analysis by Western blot technique using antiglycoprotein IIb and IIIa antibodies demonstrated that elastase did not degrade glycoproteins IIb or Ila.We conclude that elastase inhibition of thrombin-induced platelet stimulation is accompanied by (a) a reduction in the number of thrombin binding sites per platelet and (b) proteolysis of glycoprotein lb.

show abstract

Isolation of human platelet plasma membranes with polylysine beads.

Cited by 30 publications

References 30 publications

Interactions between platelet-surface glycoproteins. Identification of glycoproteins capable of binding to platelet surfaces

Interactions between platelet-surface glycoproteins. Identification of glycoproteins capable of binding to platelet surfaces

The Human Platelet Membrane Proteome Reveals Several New Potential Membrane Proteins

Human neutrophil elastase modulates platelet function by limited proteolysis of membrane glycoproteins.

Contact Info

Product

Resources

About