Human blood platelet protein map established by two‐dimensional polyacrylamide gel electrophoresis

Gravel, Patricia; Sanchez, Jean‐Charles; Walzer, Claude; Golaz, Olivier; Hochstrasser, Denis F.; Balant, L; Hughes, Graham J.; Garcı́a-Sevilla, Jesús A.; Guimón, José

doi:10.1002/elps.11501601191

Cited by 65 publications

(34 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Two-dimensional gel electrophoresis (2D-GE) (30), which separates proteins by both size and charge, is the basis of many current proteomic techniques but has been used for many years to study platelet biology (31,32). Initial studies using reducing and nonreducing gels resulted in the naming of many of the platelet glycoproteins and the identification of protein defects in patients with inherited bleeding disorders (2).…”

Section: Proteomicsmentioning

confidence: 99%

Platelet genomics and proteomics in human health and disease

Macaulay

Carr²,

Gusnanto³

et al. 2005

Journal of Clinical Investigation

150

100

View full text Add to dashboard Cite

Proteomic and genomic technologies provide powerful tools for characterizing the multitude of events that occur in the anucleate platelet. These technologies are beginning to define the complete platelet transcriptome and proteome as well as the protein-protein interactions critical for platelet function. The integration of these results provides the opportunity to identify those proteins involved in discrete facets of platelet function. Here we summarize the findings of platelet proteome and transcriptome studies and their application to diseases of platelet function.

show abstract

Section: Proteomicsmentioning

confidence: 99%

Platelet genomics and proteomics in human health and disease

Macaulay

Carr²,

Gusnanto³

et al. 2005

Journal of Clinical Investigation

150

100

View full text Add to dashboard Cite

show abstract

“…Initial studies of the platelet proteome focused on characterizing proteins in resting platelets through combinations of 2-dimensional electrophoresis (2-DE) and in-gel protein detection using monoclonal antibodies. [52][53][54] Although successful, these approaches were limited by the dynamic range of platelet proteins, coupled with the cost and sensitivity of immunodetection. Similar techniques were subsequently applied to establish a platelet protein map and to characterize tyrosine-phosphorylated proteins in resting platelets.…”

Section: Platelet Proteomic Analysesmentioning

confidence: 99%

Proteomic approaches to dissect platelet function: half the story

Gnatenko

Perrotta

Bahou

2006

Blood

View full text Add to dashboard Cite

Platelets play critical roles in diverse hemostatic and pathologic disorders and are broadly implicated in various biological processes that include inflammation, wound healing, and thrombosis. Recent progress in high-throughput mRNA and protein profiling techniques has advanced our understanding of the biological functions of platelets. Platelet proteomics has been adopted to decode the complex processes that underlie platelet function by identifying novel platelet-expressed proteins, dissecting mechanisms of signal or metabolic pathways, and analyzing functional changes of the platelet proteome in normal and pathologic states. The integration of transcriptomics and proteomics, coupled with progress in bioinformatics, provides novel tools for dissecting platelet biology. In this review, we focus on current advances in platelet proteomic studies, with emphasis on the IntroductionHuman blood platelets play important roles in fundamental biological processes, including thrombosis, inflammation, wound repair, and stroke. Although they are anucleate and lack nuclear DNA, platelets retain small amounts of megakaryocyte-derived mRNA. 1,2 Platelets also contain rough endoplasmic reticulum and polyribosomes, thus retaining the capacity for protein biosynthesis from cytoplasmic mRNA. 3 Quiescent platelets display minimal translational activity, although platelet activation leads to the rapid translation of preexisting mRNA, 4 with the release or derivation of platelet-secreted proteins, cytokines, exosomes, and microparticles.The traditional paradigm that platelet mRNA content is invariant and gradually declines with cell senescence was challenged when signal-dependent pre-mRNA splicing was identified in platelets. 5 Signal-dependent splicing provides a mechanism for altering the repertoire of translatable messages in response to cellular activation/stimulation. Furthermore, platelets have essential components of a functional spliceosome and selected unspliced pre-mRNAs. These spliceosomes retain a unique ability to splice pre-mRNA in the cytoplasm (as opposed to the typical nuclear location), a capability not described in any other mammalian cell. This discovery emphasizes that the molecular mechanisms of platelet function cannot be optimally dissected without accurate platelet transcript profiling.Modern postgenomic, high-throughput approaches allow integrated studies of molecular components (at the RNA and the protein levels) involved in cell function. Platelets represent an attractive, simplified model for these studies because they lack nuclear DNA and because their genome consists of a small subset of megakaryocyte-derived mRNA transcripts. This complete pool of platelet RNAs is significantly smaller than the transcriptome of a nucleated cell. 6 The entire pool of platelet proteins constitutes the platelet proteome: the initially static, but functionally dynamic, protein interactions that occur with platelet activation. In this review, we focus on recent applications of proteomic and transcriptomic technologies to...

show abstract

“…A 2-D reference map is an annotated image of a specific sample in which separated spots are marked by several microanalytical techniques and which can be used as a source of mapped proteins for spot identification in other samples; computer-aided gel comparison represents a rapid and feasible method for protein identification on the basis of corresponding electrophoretic coordinates between experimental gels and annotated 2-D reference maps available via the Internet. This approach has been widely used for protein identification in human tissues and body fluids (Bjellqvist et al, 1994;Gravel et al, 1995;Bini et al, 1997;Liberatori et al, 1997), as well as for identification of proteins shared by tissues belonging to closely related species, e.g., mammals (Corbett et al, 1995). In this way, a total of 22 proteins have been tentatively identified by matching with a 2-D reference map of human brain proteins (Langen et al, 1999).…”

Section: Table 1 Description Of Immunoreactive Spotsmentioning

confidence: 99%

Hypoxic Response of Synaptosomal Proteins in Term Guinea Pig Fetuses

1999

Journal of Neurochemistry

View full text Add to dashboard Cite

Early events in the hypoxia-induced response trigger tyrosine phosphorylation cascades involving a large number of enzymes and substrates. The resolving power of advanced two-dimensional gel electrophoresis, followed by immunoblotting with specific antibodies to phosphotyrosine, has been used to analyze hypoxia-induced modifications in guinea pig brain synaptosomes. These procedures, in conjunction with computer-aided image analysis, are useful in the differential display of gene products, providing comparison at the level of posttranslationally modified products. Studies were performed in cerebral cortical synaptosomes from three normoxic and three hypoxic newborn guinea pigs. To filter off background noise consisting of nonreproducible migrating protein spots, only reproducible features of electrophoretic patterns were considered. Immunoreactivity patterns obtained with anti-phosphotyrosine antibodies proved to be different in normoxic and hypoxic synaptosomes: of a total of 130 immunoreactive spots, 49 were tyrosinephosphorylated in hypoxic synaptosomes only and 20 in the normoxic ones only. Our data suggest that hypoxia extensively remodels the signaling pathway by switching off tyrosine phosphorylation of some cellular components (i.e., ␣-internexin) and switching on tyrosine phosphorylation of some other proteins (i.e., heat shock cognate 70, aconitase, 2Ј,3Ј-cyclic nucleotide 3Ј-phosphodiesterase, and pyruvate kinase).

show abstract

Human blood platelet protein map established by two‐dimensional polyacrylamide gel electrophoresis

Cited by 65 publications

References 40 publications

Platelet genomics and proteomics in human health and disease

Platelet genomics and proteomics in human health and disease

Proteomic approaches to dissect platelet function: half the story

Hypoxic Response of Synaptosomal Proteins in Term Guinea Pig Fetuses

Contact Info

Product

Resources

About