scholarly journals Complexin 2 regulates secretion of immunoglobulin in antibody‐secreting cells

2019 ◽  
Vol 7 (4) ◽  
pp. 318-325
Author(s):  
Emi Tsuru ◽  
Kohei Oryu ◽  
Ken Sawada ◽  
Makoto Nishihara ◽  
Masayuki Tsuda
Keyword(s):  
Complexin 2 ◽  
Antibody Secreting Cells

scholarly journals The Proteome of the Dentate Terminal Zone of the Perforant Path Indicates Presynaptic Impairment in Alzheimer Disease

2019 ◽  
Vol 19 (1) ◽  
pp. 128-141 ◽  
Author(s):  
Hazal Haytural ◽  
Georgios Mermelekas ◽  
Ceren Emre ◽  
Saket Milind Nigam ◽  
Steven L. Carroll ◽  
...  
Keyword(s):  
Alzheimer Disease ◽  
Dentate Gyrus ◽  
Molecular Mechanisms ◽  
Molecular Layer ◽  
Synaptic Proteins ◽  
Perforant Path ◽  
Synaptic Dysfunction ◽  
Complexin 2 ◽  
Terminal Zone ◽  
Vesicle Cycle

Synaptic dysfunction is an early pathogenic event in Alzheimer disease (AD) that contributes to network disturbances and cognitive decline. Some synapses are more vulnerable than others, including the synapses of the perforant path, which provides the main excitatory input to the hippocampus. To elucidate the molecular mechanisms underlying the dysfunction of these synapses, we performed an explorative proteomic study of the dentate terminal zone of the perforant path. The outer two-thirds of the molecular layer of the dentate gyrus, where the perforant path synapses are located, was microdissected from five subjects with AD and five controls. The microdissected tissues were dissolved and digested by trypsin. Peptides from each sample were labeled with different isobaric tags, pooled together and pre-fractionated into 72 fractions by high-resolution isoelectric focusing. Each fraction was then analyzed by liquid chromatography-mass spectrometry. We quantified the relative expression levels of 7322 proteins, whereof 724 showed significantly altered levels in AD. Our comprehensive data analysis using enrichment and pathway analyses strongly indicated that presynaptic signaling, such as exocytosis and synaptic vesicle cycle processes, is severely disturbed in this area in AD, whereas postsynaptic proteins remained unchanged. Among the significantly altered proteins, we selected three of the most downregulated synaptic proteins; complexin-1, complexin-2 and synaptogyrin-1, for further validation, using a new cohort consisting of six AD and eight control cases. Semi-quantitative analysis of immunohistochemical staining confirmed decreased levels of complexin-1, complexin-2 and synaptogyrin-1 in the outer two-thirds of the molecular layer of the dentate gyrus in AD. Our in-depth proteomic analysis provides extensive knowledge on the potential molecular mechanism underlying synaptic dysfunction related to AD and supports that presynaptic alterations are more important than postsynaptic changes in early stages of the disease. The specific synaptic proteins identified could potentially be targeted to halt synaptic dysfunction in AD.

scholarly journals Complexin-2 redistributes to the membrane of muscle cells in response to insulin and contributes to GLUT4 translocation

2021 ◽  
Author(s):  
Martin Alejandro Pavarotti ◽  
Victoria Tokarz ◽  
Scott Frendo-Cumbo ◽  
Philip Bilan ◽  
Zhi Liu ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Insulin Signalling ◽  
Muscle Cells ◽  
Secretory Vesicle ◽  
Vesicle Fusion ◽  
Glut4 Translocation ◽  
Vesicle Membrane ◽  
Actin Fiber ◽  
Complexin 2 ◽  
Intracellular Compartments

Insulin stimulates glucose uptake in muscle cells by rapidly redistributing vesicles containing GLUT4 glucose transporters from intracellular compartments to the plasma membrane. GLUT4 vesicle fusion requires formation of SNARE complexes between vesicular VAMP and plasma membrane syntaxin4 and SNAP23. SNARE accessory proteins usually regulate vesicle fusion processes. Complexins aide in neuro-secretory vesicle-membrane fusion by stabilizing trans-SNARE complexes but their participation in GLUT4 vesicle fusion is unknown. We report that complexin-2 is expressed and homogeneously distributed in L6 rat skeletal muscle cells. Upon insulin stimulation, a cohort of complexin-2 redistributes to the plasma membrane. Complexin-2 knockdown markedly inhibited GLUT4 translocation without affecting proximal insulin signalling of Akt/PKB phosphorylation and actin fiber remodelling. Similarly, complexin-2 overexpression decreased maximal GLUT4 translocation suggesting that the concentration of complexin-2 is finely tuned to vesicle fusion.  These findings reveal an insulin-dependent regulation of GLUT4 insertion into the plasma membrane involving complexin-2.

scholarly journals Involvement of Complexin 2 in Docking, Locking and Unlocking of Different SNARE Complexes during Sperm Capacitation and Induced Acrosomal Exocytosis

PLoS ONE ◽  
2012 ◽  
Vol 7 (3) ◽  
pp. e32603 ◽  
Author(s):  
Pei-Shiue J. Tsai ◽  
Ian A. Brewis ◽  
Jillis van Maaren ◽  
Bart M. Gadella
Keyword(s):  
Sperm Capacitation ◽  
Acrosomal Exocytosis ◽  
Complexin 2

Regulation of complexin 1 and complexin 2 in the developing human prefrontal cortex

Synapse ◽  
2008 ◽  
Vol 62 (4) ◽  
pp. 273-282 ◽  
Author(s):  
Kayvon Salimi ◽  
Leisa A. Glantz ◽  
Robert M. Hamer ◽  
Thomas T. German ◽  
John H. Gilmore ◽  
...  
Keyword(s):  
Prefrontal Cortex ◽  
Complexin 2

scholarly journals Clorgyline-mediated reversal of neurological deficits in a Complexin 2 knockout mouse

2010 ◽  
Vol 19 (17) ◽  
pp. 3402-3412 ◽  
Author(s):  
D. Glynn ◽  
H. E. Gibson ◽  
M. K. Harte ◽  
K. Reim ◽  
S. Jones ◽  
...  
Keyword(s):  
Knockout Mouse ◽  
Neurological Deficits ◽  
Complexin 2

Complexin-2 (CPLX2) as a potential prognostic biomarker in human lung high grade neuroendocrine tumors

2013 ◽  
Vol 13 (3) ◽  
pp. 171-180 ◽  
Author(s):  
Hiroaki Komatsu ◽  
Anna Kakehashi ◽  
Noritoshi Nishiyama ◽  
Nobuhiro Izumi ◽  
Shinjiro Mizuguchi ◽  
...  
Keyword(s):  
Neuroendocrine Tumors ◽  
Human Lung ◽  
Prognostic Biomarker ◽  
High Grade ◽  
Complexin 2

Structural organization of the human complexin 2 gene (CPLX2) and aspects of its functional activity

Gene ◽  
2005 ◽  
Vol 359 ◽  
pp. 127-137 ◽  
Author(s):  
Natalja M. Raevskaya ◽  
Lyudmila V. Dergunova ◽  
Irina P. Vladychenskaya ◽  
Vasily V. Stavchansky ◽  
Maria V. Oborina ◽  
...  
Keyword(s):  
Functional Activity ◽  
Structural Organization ◽  
Complexin 2
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