• Metal chaperones (or metallochaperones) are compounds that function to shuttle metal ions to specific intracellular target proteins. (frontiersin.org)
  • Interaction of intracellular beta amyloid peptide with chaperone proteins. (neurotree.org)
  • Fatty Acid Binding Proteins (FABPs) are a family of intracellular proteins that chaperone lipids including endocannabinoids and fatty acids. (tmcnet.com)
  • These proteins usually have 4 - 6 TMSs and function in intracellular protein trafficking in eukaryotes and as protein chaparone proteins in prokaryotes. (tcdb.org)
  • Small copper-binding proteins, denoted copper chaperones, distribute copper to specific intracellular destinations. (vin.com)
  • Misfolded proteins are sticky and tend to form intracellular aggregates underpinning age-related deterioration and diseases including cancer and neurodegeneration. (cam.ac.uk)
  • Small heat shock proteins (sHsp) constitute an evolutionary conserved yet diverse family of chaperones acting as first line of defense against proteotoxic stress. (cam.ac.uk)
  • They promote the storage of misfolded proteins in native-like conformation facilitating disaggregation by ATP dependent chaperone systems. (cam.ac.uk)
  • Glycans, either alone or complexed with glycan-binding proteins, can deliver intracellular signals or control extracellular processes that promote initiation, execution and resolution of cell death programs. (nature.com)
  • Here we used an affinity-purification mass spectrometry-based (AP-MS) approach to identify novel and particularly intracellular sGAG-interacting proteins in human bone marrow stromal cells (hBMSC). (degruyter.com)
  • Enrichment analysis for protein localization showed that mainly intracellular and cell-associated interacting proteins were identified. (degruyter.com)
  • The identification of the intracellular sGAG-interacting proteins could help to unravel these functions. (degruyter.com)
  • Molecular chaperones assist the folding of newly synthesized and denatured proteins in acquiring their native state in the crowded intracellular environment. (uni-muenchen.de)
  • The co-chaperone Hep1 is required to prevent the aggregation of mitochondrial Hsp70 proteins. (cipsm.de)
  • The ability of neurons to manage the burden of misfolded proteins and to resist their accumulation into insoluble protein deposits depends critically on the functioning of molecular chaperones. (biomedcentral.com)
  • This highly complex 'protein biogenesis' process is assisted by a diverse network of folding catalysts and protein-modifying enzymes and is scrutinized by molecular chaperones and other 'quality control' factors which ensure that only correctly folded and assembled proteins exit the ER and proceed to distal compartments of the secretory pathway. (stanford.edu)
  • In the responsive immune system major histocompatibility complex class I (MHC I) proteins plays a key role in the recognition of intracellular pathogens (virus and cancer). (lu.se)
  • One of these proteins, which help to stabilize, facilitate and edit the peptide-loading complex, is Tapasin, a chaperone transmembrane protein. (lu.se)
  • What is the precise role of intracellular and extracellular galectins in the control of cell death programs? (nature.com)
  • Several investigations suggest that, besides their extracellular actions, also intracellular mechanisms of sGAG-derivatives seem possible. (degruyter.com)
  • The comparative fungal proteomics displayed the remarkable inherent intracellular and extracellular mechanism of metal resistance and tolerance potential of A. fumigatus PD-18. (ufz.de)
  • Most chaperones are localised within intracellular compartments, although some are secreted into the extracellular environment. (biomedcentral.com)
  • Prominent amongst such extracellular chaperones is clusterin (CLU), which is present in both plasma and cerebrospinal fluid (CSF). (biomedcentral.com)
  • The primary aim of this work was to elucidate the pathway that leads to the finally assembled trimeric P2X receptors, including the assessment of a possible role of ER chaperones and folding factors in this process. (uni-frankfurt.de)
  • The protein encoded by this gene is also known as p23 which functions as a chaperone which is required for proper functioning of the glucocorticoid and other steroid receptors. (wikipedia.org)
  • and intracellular trafficking, secretion, and vesicular transport (18). (ufz.de)
  • Clearance of small intestinal crypts involves goblet cell mucus secretion by intracellular granule rupture and enterocyte ion transport. (gu.se)
  • HSP70, together with the DNAJA2 member of HSP40 co-chaperones, is the main chaperone involved in IRES-mediated translation of the viral genome, while HSP90 may play some role as well. (wjgnet.com)
  • In plants, fungi and bacteria the central disaggregation machinery is a powerful bi-chaperone system comprised by the AAA + disaggregase Hsp100 (Hsp104, ClpB) and the cooperating Hsp70 chaperone system. (cam.ac.uk)
  • Metazoan cells lack Hsp100 disaggregases, but have evolved a potent Hsp70-based disaggregation machinery which relies on synergistic action of Hsp70 and its co-chaperones. (cam.ac.uk)
  • This unfolding is a local phenomena and can also be observed when the substrate is transferred from DnaK/J system (bacterial Hsp70) to GroEL, indicating the possibility of the existence of this conformational heterogeneity in vivo as the protein follows the cellular chaperone pathway. (uni-muenchen.de)
  • Respecting the preferentially intracellular localization of sGAG in vesicle-like structures, also the interaction data indicate sGAG-specific modulation of vesicle-based transport processes. (degruyter.com)
  • These results demonstrate that Caspr regulates the intracellular processing and transport of contactin to the cell surface, thereby affecting its ability to interact with other cell adhesion molecules. (rupress.org)
  • Calreticulin plays a central role in intracellular Ca homeostasis. (bio.net)
  • Cumulatively, however, these processes serve to maintain tight regulatory control over cellular metal ion homeostasis such that the intracellular concentration of freely available metal ions (such as copper and zinc) is close to zero. (frontiersin.org)
  • Biochemically, inherited mutations most frequently reduce enzyme's stability, altering its homeostasis to ultimately decrease the intracellular haem production. (irbbarcelona.org)
  • Subsequent research suggested that DJ-1 has various potential functions, including transcriptional regulation, oxidative stress inhibition, acting as a chaperone or protease and mitochondrial regulation ( 12 ). (spandidos-publications.com)
  • It not only inhibits tyrosine phosphorylation but also enhances ubiquitinylation and accelerates endocytosis and subsequent intracellular destruction of ErbB-2 molecules. (lclabs.com)
  • We therefore conclude that increased expression of clusterin can provide an important defense against intracellular proteotoxicity under conditions that mimic specific features of neurodegenerative disease. (biomedcentral.com)
  • The Molecular Chaperone CCT Sequesters Gelsolin and Protects it from Cleavage by Caspase-3. (gu.se)
  • Suppression of in vivo beta-amyloid peptide toxicity by overexpression of the HSP-16.2 small chaperone protein. (neurotree.org)
  • The protease not only releases small peptides, such as the amyloid-β peptide, which drives Alzheimer's disease pathogenesis, but also intracellular domains, which can have critical functions in nuclear signaling. (cipsm.de)
  • Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. (wikipedia.org)
  • 1997). "Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. (wikipedia.org)
  • The sigma-1 receptor (Sig-1R), a well-known ER-chaperone localizes in the MAM. (eurekaselect.com)
  • RME-2 contains a typical NPXY internalization motif in its intracellular domain that is known to direct other members of the LDL-receptor family into clathrin-coated pits. (wormbook.org)
  • The degradative pathway of ErbB receptor tyrosine kinases stimulated by tyrosine kinase inhibitors appears to be chaperone mediated, and thus is similar to the pathways activated by the heat shock protein 90 (Hsp90) antagonist geldanamycin and by stress-induced mechanisms. (lclabs.com)
  • have begun to reveal new components and new mechanisms associated with intracellular membrane traffic in a variety of cell types. (wormbook.org)
  • This is particularly evident in disorders such as Alzheimer's disease (AD), where the use of metal chaperones (that transport metals), as opposed to chelators (which exclude metals from biological interactions), may prove to be the first truly disease modifying approach for this condition. (frontiersin.org)
  • Taken together, these data suggest an important role for ORP150 in the setting of impaired wound repair and identify a key, inducible chaperone-like molecule in the ER. (jci.org)
  • DJ‑1 protein, as a multifunctional intracellular protein, has been demonstrated to serve a critical role in regulating cell survival and oxidative stress. (spandidos-publications.com)
  • α-synuclein's physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. (biolegend.com)
  • Such vesicles are then uncoated by the chaperone hsc70 and the DNA-J domain co-chaperone auxillin. (wormbook.org)
  • The antigen processing and loading onto MHC-I molecules takes place in the intracellular environment, when the antigen-MHC-I complex is transferred to the cell surface for detection by circulating CD8 + T cells. (lu.se)
  • Subsequently it was demonstrated that the ER-resident chaperone BiP (GRP78) facilitates the translocation of CLU to the cytosol during ER stress in human prostate cancer LNCaP cells [ 16 ]. (biomedcentral.com)
  • Intracellular lectins and glycan-modifying enzymes mediate autophagy and control host immunity and inflammation. (nature.com)
  • Although sulfated GAGs (sGAGs) appear intracellularly, the knowledge about intracellular effects and putative interaction partners is scarce. (degruyter.com)
  • This includes gene, protein and metabolic networks, cellular architecture and intracellular dynamics, cell communication and motility, cell division and differentiation, tissue formation and organogenesis, tissue and organ functions, changes in population characteristics as a consequence of interaction of organisms with their physical environment, with individuals of their own species, and with organisms of other species. (nih.gov)
  • Compensatory regulation among ER chaperones in C. elegans. (neurotree.org)
  • Furthermore, calreticulin modulates gene expression, is a chaperone and affects cell adhesion. (bio.net)
  • Metallothionein 1A (MT1A) is a small intracellular protein capable of chelating several metal ions, including copper. (vin.com)
  • We have examined in this study whether or not increased expression of clusterin is able to protect neuronal cells against intracellular protein aggregation and cytotoxicity, characteristics that are strongly implicated in a range of neurodegenerative diseases. (biomedcentral.com)
  • The purpose of this mini-review is to highlight the emerging notion that metal chaperones, such as PBT2 (Prana Biotechnology), modulate a variety of critical pathways affecting key aspects of the AD cascade to provide a more "holistic" approach to the treatment of this disease. (frontiersin.org)
  • Lactate dehydrogenase (LDH) and creatine kinase‑MB (CK‑MB) release, infarct size, cardiac function, superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx) activities, malondialdehyde (MDA), intracellular reactive oxygen species (ROS), and DJ‑1 protein expression levels were assessed. (spandidos-publications.com)
  • GroEL-GroES, the Hsp-60 of E.coli, is one of the best studied chaperone systems. (uni-muenchen.de)
  • At CMCB it was used to study kinetics of binding, unbinding and rebinding of chaperones to OMPs. (tu-dresden.de)
  • David B. Williams Department of Biochemistry, University of Toronto, Toronto, Ontario, CANADA Lectin and chaperone properties of calreticulin and calnexin. (bio.net)