Background
Platelets are small anucleated blood particles that play a key role in the control of bleeding. Platelets need to be activated to perform their functions and participate in hemostasis. The process of activation is accompanied by vast protein reorganization and posttranslational modifications. The goal of this study was to identify changes in proteins in platelets activated by different agonists. Platelets were activated by three different agonists - arachidonic acid, collagen, and thrombin. 2D SDS-PAGE (pI 4-7) was used to separate platelet proteins. Proteomes of activated and resting platelets were compared with each other by Progenesis SameSpots statistical software; and proteins were identified by nanoLC-MS/MS.

/pdf/proteome-changes-in-platelets-activated-by-arachidonic-acid-4ukn6l9tqi.pdf

Proteome changes in platelets activated by arachidonic acid, collagen, and thrombin.

The ABCC4 membrane transporter modulates platelet aggregation.

Sodium-hydrogen exchanger as a channel for regulation of intracellular pH might be a crucial modulator of sperm capacitation and motility. Three members of this family have been identified in spermatozoa. A novel protein testis-specific sodium-hydrogen exchanger named mtsNHE was cloned in the present study. The mtsNHE localizing on principle piece of sperm flagellum contained 12 predicted transmembrane regions without cytoplasmic fragment at carboxyl terminus. Hydrophilic region was common in the sodium-hydrogen exchanger family members. Polyclonal antibodies to trans-membrane region significantly reduced sperm motility, acrosome reaction and ratio of in vitro fertilization. By in-pouring the antibodies in sperm solution, intracellular pH and calcium concentration were decreased. Muscle injection of female mice with the specific gene vaccine of mtsNHE, significantly stepped down fertility rate. Considering its specific expression and involvement in the regulation of fertility, the mtsNHE might be a potential target molecule for developing a new male contraceptive.

A novel testis-specific Na+/H+ exchanger is involved in sperm motility and fertility.

Understanding the molecular mechanisms of platelet activation and aggregation is of high interest for basic and clinical hemostasis and thrombosis research. The central platelet protein interaction network is involved in major responses to exogenous factors. This is defined by systemsbiological pathway analysis as the central regulating signaling cascade of platelets (CC). The CC is systematically compared here between mouse and human and major differences were found. Genetic differences were analysed comparing orthologous human and mouse genes. We next analyzed different expression levels of mRNAs. Considering 4 mouse and 7 human high-quality proteome data sets, we identified then those major mRNA expression differences (81%) which were supported by proteome data. CC is conserved regarding genetic completeness, but we observed major differences in mRNA and protein levels between both species. Looking at central interactors, human PLCB2, MMP9, BDNF, ITPR3 and SLC25A6 (always Entrez notation) show absence in all murine datasets. CC interactors GNG12, PRKCE and ADCY9 occur only in mice. Looking at the common proteins, TLN1, CALM3, PRKCB, APP, SOD2 and TIMP1 are higher abundant in human, whereas RASGRP2, ITGB2, MYL9, EIF4EBP1, ADAM17, ARRB2, CD9 and ZYX are higher abundant in mouse. Pivotal kinase SRC shows different regulation on mRNA and protein level as well as ADP receptor P2RY12. Our results highlight species-specific differences in platelet signaling and points of specific fine-tuning in human platelets as well as murine-specific signaling differences.

/pdf/comparison-of-the-central-human-and-mouse-platelet-signaling-cc6qism0vq.pdf

Comparison of the central human and mouse platelet signaling cascade by systems biological analysis

Thrombozyten sind als anukleare Zellen ideale Forschungsobjekte fur moderne Proteomanalysen. Trotz ihrer Bedeutung in Hamostase und Thrombose ist das Proteinrepertoire von Plattchen zu grosen Teilen bislang nicht detailliert charakterisiert worden. In Vorbereitung auf bioinformatische und funktionelle Studien wurde eine Reihe von Proteomanalysen auf Thrombozytensubproteome angewendet, die ein Plasmamembranproteom sowie die Analyse von posttranslationalen Modifikationen einschliesen. Auf dieser Basis konnten 489 Proteine dargestellt werden, die nicht in bisherigen Proteomansatzen charakterisiert wurden sowie uber 550 Phosphorylierungs- und 326 N-Glykosylierungsstellen. Diese Ergebnisse stellen neue Ansatzpunkte fur funktionelle Forschungen durch die Identifikation neuer Plattchenproteine bzw. derer Modifikationen dar.

Funktionelle Proteomanalyse humaner Thrombozyten

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Funktionelle Proteomanalyse humaner Thrombozyten