Synaptic vesicle proteins under conditions of rest and activation: Analysis by 2-D difference gel electrophoresis

Burré, Jacqueline; Beckhaus, Tobias; Corvey, Carsten; Karas, Michael; Zimmermann, Herbert; Volknandt, Walter

doi:10.1002/elps.200500864

Cited by 38 publications

(31 citation statements)

References 43 publications

(48 reference statements)

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“…Although proteomic techniques have existed for several years and have already been successfully used in numerous neurological diseases [125][126][127][128][129] , most proteomic studies described in stroke are based on animal models [130][131][132] . Therefore, its application and development in the study of human biological samples is a major challenge for understanding the disease.…”

Section: Expert Commentary and Fi Ve-year Viewmentioning

confidence: 99%

Potential blood biomarkers for stroke

Laborde

Mouriño-Álvarez

Åkerström³

et al. 2012

Expert Review of Proteomics

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Stroke is one of the most common causes of death worldwide and a major cause of acquired disability in adults. Despite advances in research during the last decade, prevention and treatment strategies still suffer from significant limitations, and therefore new theoretical and technical approaches are required. Technological advances in the proteomic and metabolomic areas, during recent years, have permitted a more effective search for novel biomarkers and therapeutic targets that may allow for effective risk stratification and early diagnosis with subsequent rapid treatment. This review provides a comprehensive overview of the latest candidate proteins and metabolites proposed as new potential biomarkers in stroke.

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Section: Expert Commentary and Fi Ve-year Viewmentioning

confidence: 99%

Potential blood biomarkers for stroke

Laborde

Mouriño-Álvarez

Åkerström³

et al. 2012

Expert Review of Proteomics

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“…Among the 185 identified proteins, only 19% were identified by all three techniques. The authors further demonstrated that synaptic depolarization induced synaptic vesicle protein changes, which were partly caused by post-translational modifications such as phosphorylation [36]. Takamori et al identified a larger number of synaptic vesicle proteins (410 proteins) [10].…”

Section: Review LI and Jimenezmentioning

confidence: 97%

Synapse proteomics: current status and quantitative applications

Jiménez²

2008

Expert Review of Proteomics

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Chemical synapses are key organelles for neurotransmission. The coordinated actions of protein networks in diverse synaptic subdomains drive the sequential molecular events of transmitter release from the presynaptic bouton, activation of transmitter receptors located in the postsynaptic density and the changes of postsynaptic potential. Plastic change of synaptic efficacy is thought to be caused by the alteration of protein constituents and their interaction in the synapse. As a first step toward the understanding of the organization of synapse, several proteomics studies have been carried out to profile the protein constituents and the post-translational modifications in various rodent excitatory chemical synaptic subdomains, including postsynaptic density, synaptic vesicle and the synaptic phosphoproteome. Quantitative proteomics have been applied to examine the changes of synaptic proteins during brain development, in knockout mice model developed for studies of synapse physiology and in rodent models of brain disorders. These analyses generate testable hypotheses of synapse function and regulation both in health and disease.

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“…In particular, diVerential quantitative proteomics, the comparison of an experiment and its control, is very discriminating for proteins involved in the process studied (Wilm 2009). The development of diVerential gel electrophoresis (DIGE) allows the evaluation of diVerences in protein pattern and post-translational modiWcations in the synaptic vesicle proteome of diVerent functional origin (Burré et al 2006a). A proteomic strategy to compare, for example, the proteome of mutant mice to that of controls can involve either gel-based diVerence gel electrophoresis (DIGE, Marouga et al 2005;Tannu and Hemby 2006b) or tandem mass tag (for review, see Elliott et al 2009).…”

Section: Quantitative Mass Spectrometrymentioning

confidence: 99%

Proteomic analysis of the presynaptic active zone

Volknandt

Karas

2012

Exp Brain Res

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Synaptic vesicles are key organelles in chemical signaling, allowing neurons to communicate with each other and with neighboring cells. Vesicle integral or membrane-associated proteins mediate the various tasks the organelle fulfills during its life cycle. These include organelle transport, interaction with the nerve terminal cytoskeleton, uptake and storage of low molecular weight constituents, and the regulated interaction with the presynaptic plasma membrane, the active zone, during exo- and endocytosis. Converging work from several laboratories within the last 30 years resulted in the molecular and functional characterization of the protein inventory of the synaptic vesicle compartment. Nowadays advances in membrane protein separation and mass spectrometry have dramatically promoted this field resulting in a detailed description of the synaptic vesicle proteome and making synaptic vesicles the best characterized organelles. Recently, the proteome of the active zone was identified using the docked synaptic vesicles as target for immunoisolation. Combining gel-based protein separation techniques, mass spectrometry, and immunodetection, a considerable variety of proteins has been detected in the active zone. This includes synaptic vesicle proteins, components of the presynaptic fusion and retrieval machinery, proteins involved in intracellular signal transduction, a large variety of adhesion molecules and proteins potentially involved in regulating the functional and structural dynamics of the presynapse. Here, we discuss recent information concerning the proteome of the presynaptic active zone, focusing on proteins that are potentially involved in the short- and long-term structural modulation of the mature presynaptic compartment. In addition, we discuss the functional relevance of amyloid precursor protein in these membrane fractions and the putative interplay with direct or indirect interaction partners in the active zone.

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Synaptic vesicle proteins under conditions of rest and activation: Analysis by 2-D difference gel electrophoresis

Cited by 38 publications

References 43 publications

Potential blood biomarkers for stroke

Potential blood biomarkers for stroke

Synapse proteomics: current status and quantitative applications

Proteomic analysis of the presynaptic active zone

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