Ask about this productRelated genes to: S100A6 antibody
- Gene:
- CACYBP NIH gene
- Name:
- calcyclin binding protein
- Previous symbol:
- -
- Synonyms:
- SIP, S100A6BP
- Chromosome:
- 1q25.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-11-03
- Date modifiied:
- 2016-10-05
- Gene:
- S100A6 NIH gene
- Name:
- S100 calcium binding protein A6
- Previous symbol:
- CACY
- Synonyms:
- 2A9, PRA, CABP
- Chromosome:
- 1q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2018-05-02
Related products to: S100A6 antibody
Related articles to: S100A6 antibody
- Neuronal morphogenesis relies on intercellular signaling. Astrocytes release metabolites, trophic, and guidance factors to promote neuronal maturation. In contrast, the mechanisms by which astrocytes could limit and stabilize neuronal connectivity remain less explored. Here, we find cortical astrocytes to express and release S100A6, a Ca-binding protein ('calcyclin'). Simultaneously, the majority of cortical neurons expressed calcyclin-binding protein (CaCyBp), a bona fide binding partner for S100A6. In neurons, CaCyBp maintains the unfolded protein response pathway, thereby controlling proteostasis. When released, S100A6 inhibits CaCyBp-mediated signaling, thus slowing protein turnover, and, consequently, neuritogenesis. In the cerebral cortex of male mice, S100A6-CaCyBp signaling during gestation is sensitive to the mother's nutritional status, particularly eicosapentaenoic acid intake. Thus, a member of the S100 protein family acts as an astroglia-derived morphogen, whose action on neurons is modulated by environmental factors. - Source: PubMed
Publication date: 2025/10/13
Cinquina ValentinaTretiakov Evgenii OKalaba PredragAlpár AlánCalvigioni DanielaPiscitelli FabianaKeimpema ErikDi Marzo VincenzoVerkhratsky AlexejHarkany Tibor - The S100A6 protein is present in different mammalian cells and tissues including the brain. It binds Ca and Zn and interacts with many target proteins/ligands. The best characterized ligands of S100A6, expressed at high level in the brain, include CacyBP/SIP and Sgt1. Research concerning the functional role of S100A6 and these two ligands indicates that they are involved in various signaling pathways that regulate cell proliferation, differentiation, cytoskeletal organization, and others. In this review, we focused on the expression/localization of these proteins in the brain and on their possible role in neurodegenerative diseases. Published results demonstrate that S100A6, CacyBP/SIP, and Sgt1 are expressed in various brain structures and in the spinal cord and can be found in different cell types including neurons and astrocytes. When it comes to their possible involvement in nervous system pathology, it is evident that their expression/level and/or subcellular localization is changed when compared to normal conditions. Among diseases in which such changes have been observed are Alzheimer's disease (AD), amyotrophic lateral sclerosis (ALS), epileptogenesis, Parkinson's disease (PD), Huntington's disease (HD), and others. - Source: PubMed
Publication date: 2020/06/01
Filipek AnnaLeśniak Wiesława - S100A6, a calcium binding protein, whose gene was first identified as growth inducible one, has been linked to the process of cell proliferation and growth related phenomena ever since. While the structure and Ca2+ binding kinetics of S100A6 are rather well established the mechanism of its action has only recently begun to be elucidated. It is nonetheless evident that S100A6 exerts its biological role by interacting with a wide range of proteins ligands, many of which have been identified in our laboratory. Our research concentrates on two S100A6 ligands, CacyBP/SIP and Sgt1, which in turn possess their own interactomes. The imposing list of S100A6-interacting proteins indicates that together with its ligands it is a component of an extended network of cellular interactions and may be involved not only in cell proliferation but also in many other processes, of which cell differentiation and response to stress seem to be best documented. - Source: PubMed
Filipek AnnaLeśniak Wiesława - (1) Background: Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are neurodegenerative disorders with an overlap in clinical presentation and neuropathology. Common and differential mechanisms leading to protein expression changes and neurodegeneration in ALS and FTD were studied trough a deep neuroproteome mapping of the spinal cord. (2) Methods: A liquid chromatography tandem mass spectrometry (LC-MS/MS) analysis of the spinal cord from ALS-TAR DNA-binding protein 43 () subjects, ubiquitin-positive frontotemporal lobar degeneration (FTLD-U) subjects and controls without neurodegenerative disease was performed. (3) Results: 281 differentially expressed proteins were detected among ALS versus controls, while 52 proteins were dysregulated among FTLD-U versus controls. Thirty-three differential proteins were shared between both syndromes. The resulting data was subjected to network-driven proteomics analysis, revealing mitochondrial dysfunction and metabolic impairment, both for ALS and FTLD-U that could be validated through the confirmation of expression levels changes of the Prohibitin () complex. (4) Conclusions: ALS-TDP-43 and FTLD-U share molecular and functional alterations, although part of the proteostatic impairment is region- and disease-specific. We have confirmed the involvement of specific proteins previously associated with ALS (Galectin 2 (), Transthyretin (), Protein S100-A6 (), and Protein S100-A11 ()) and have shown the involvement of proteins not previously described in the ALS context (Methanethiol oxidase (), Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (), Calcyclin-binding protein () and Rho-associated protein kinase 2 ()). - Source: PubMed
Publication date: 2018/12/20
Iridoy Marina OaiaZubiri IreneZelaya María VictoriaMartinez LeyreAusín KarinaLachen-Montes MercedesSantamaría EnriqueFernandez-Irigoyen JoaquínJericó Ivonne - Women live about 4 years longer due to lower prevalence of cardiovascular complication with ageing. However, the mechanisms involved in the preservation of heart functionality in women have not been fully elucidated. The endocannabinoid system fulfils a significant role in the regulation of cardiovascular system functioning. Cannabinoids, acting through specific receptors (CB1 and CB2), influence on blood pressure, heart rate and myocardial contractility. The function of cardiac muscle cells is strictly dependent on calcium ions. Calcium homeostasis in cardiomyocytes is subjected to complex regulation via calcium-binding proteins. Among them, increasing attention has been paid to the recently discovered S100A6 and CacyBP/SIP. In order to better understand sex differences in the regulation of cardiomyocyte function during ageing, we undertook the present research aimed at immunohistochemical identification and comparative evaluation of cannabinoid receptors, S100A6 and CacyBP/SIP, in the myocardium of ageing men and women. - Source: PubMed
Publication date: 2018/11/27
Piotrowska ŻanetaNiezgoda MichałŁebkowski WojciechFilipek AnnaDomian NataliaKasacka Irena