Disease relevance of GOSR1

• We report immunoelectron microscopy experiments establishing that a Golgi-restricted SNARE, GOS 28, is present in the same population of COPI vesicles as anterograde cargo marked by vesicular stomatitis virus glycoprotein, but is excluded from the COPI vesicles containing retrograde-targeted cargo (marked by KDEL receptor) [1].
• The present studies establish that there are specific, significant decreases in the neuronal calcium-binding protein (28-kDa calbindin-D) gene expression in aging and in neurodegenerative diseases [2].
• Although peripheral blood mononuclear cells from patients with Sézary syndrome have been shown to respond poorly to mitogens, we found that mitogen-activated peripheral blood mononuclear cells from four of five patients with Sézary syndrome produce a 28 kDa protein termed Sézary T-cell activating factor (SAF) [3].
• The zymogen was expressed and isolated from Escherichia coli as inclusion bodies with a molecular mass of 28 kDa [4].
• The gene for a 28-kDa Mycobacterium leprae protein Ag, a major target of antibodies from patients with lepromatous leprosy, was cloned from a lambda-gt11-M. leprae DNA expression library and sequenced [5].

Psychiatry related information on GOSR1

• Sensory neglect and apomorphine-induced rotation were measured at P27 and P28 [6].
• The present experiments explored social consequences of ethanol during adolescence by examining dose-dependent ethanol-induced social facilitation and inhibition in a non-anxiogenic (familiar) environment, and ethanol-related anxiolysis in an anxiogenic (unfamiliar) environment in early (P28) and late (P42) adolescent rats [7].

High impact information on GOSR1

• Both mu- and m-calpain are heterodimers containing an identical 28-kDa subunit and an 80-kDa subunit that shares 55-65% sequence homology between the two proteases [8].
• The transfer may be facilitated by the 28-kDa water channel-forming integral protein (CHIP28), which is expressed in the trophoblast syncytium [9].
• Taspase1 proenzyme is intramolecularly proteolyzed generating an active 28 kDa alpha/22 kDa beta heterodimer [10].
• P0 is a 28 kDa glycoprotein involved in the compaction of the multilamellar myelin sheet and accounts for more than half of the peripheral myelin protein content [11].
• The structure of the 28 kDa complex of the first two RNA binding domains (RBDs) of nucleolin (RBD12) with an RNA stem-loop that includes the nucleolin recognition element UCCCGA in the loop was determined by NMR spectroscopy [12].

Chemical compound and disease context of GOSR1

• Pseudomonas exotoxin (PE) enters cells by receptor-mediated endocytosis and is cleaved by a cellular protease between Arg279 and Gly280 to produce an NH2-terminal fragment of 28 kDa which contains the toxin's binding domain and a COOH-terminal fragment of 37 kDa which has translocating and ADP-ribosylating activity [13].
• We have previously reported the presence of a 28-kDa protein in human mammary adenocarcinoma MCF-7 cells, whose phosphorylation by phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA) and permeant diacylglycerol 1,2-dioctanoyl-sn-glycerol was correlated to growth arrest induced by the protein kinase C (PKC) activators [14].
• In the present study, we have generated a mutant strain of Streptococcus pyogenes, MC25, which lacks M protein on its surface, and we demonstrate that this strain is unable to generate a mature 28 kDa cysteine proteinase [15].
• Herpesviruses encode an essential, maturational serine protease whose catalytic domain, assemblin (28 kDa), is released by self-cleavage from a 74-kDa precursor (pPR, pUL80a) [16].
• This paper reports the crystal structure of the Schistosoma haematobium 28 kDa glutathione S-transferase, a multifunctional enzyme involved in host-parasite interactions and presently considered as a promising vaccine candidate against schistosomiasis [17].

Biological context of GOSR1

• cDNA characterization and chromosomal mapping of human golgi SNARE GS27 and GS28 to chromosome 17 [18].
• The N terminus of the deduced amino acid sequence had properties characteristic for a mitochondrial translocation signal, and cleavage at a putative mitochondrial peptidase cleavage site would give a mature protein size of 28 kDa [19].
• Tumor necrosis factor induces phosphorylation of a 28-kDa mRNA cap-binding protein in human cervical carcinoma cells [20].
• Antibodies 232 and 233, specific for synthetic peptides pep14-24 and pep117-127, corresponding to two nonoverlapping HTLV-related regions in the longer open reading frame of HRES-1, recognize an identical 28-kDa protein in H9 human T cells [21].
• From a flounder pituitary cDNA library, cDNA clones encoding a 28-kDa glycoprotein produced by the pars intermedia of the pituitary were isolated and characterized [22].

Anatomical context of GOSR1

• We report the identification of a putative v-SNARE (GOS-28), localized primarily to transport vesicles at the terminal rims of Golgi stacks [23].
• Antibodies directed against GOS-28 block its ability to bind alpha-SNAP, partially inhibit transport from the cis to the medial cisternae, and do not inhibit budding of COP-coated vesicles, but do accumulate docked uncoated vesicles [23].
• Water-permeable membranes of several plant and mammalian tissues contain specific water channel proteins, the 'aquaporins'. The best characterized aquaporin is CHIP, a 28 kDa red blood cell channel-forming integral protein [24].
• By using human alpha2 laminins as a probe, a major 28-kDa protein in the M. leprae cell wall fraction that binds alpha2 laminins was identified [25].
• CD52 is a 21- to 28-kDa nonmodulating cell surface glycosylphosphatidylinositol-linked glycoprotein expressed on lymphocytes and monocytes, but not in human myeloid cells [26].

Associations of GOSR1 with chemical compounds

• We demonstrate here that the 28 kDa I-TevI binds the extensive 37 bp td homing site as a monomer and significantly distorts its substrate [27].
• BF is a protein with a molecular mass of 28 kDa on reducing sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS/PAGE) [28].
• Phenobarbitone treatment of the animal leads to a significant increase in the phosphorylation of the 26- to 28-kDa and 94-kDa proteins in nuclear labeling experiments followed by isolation on a PE affinity column [29].
• The resultant 28-kDa EBNA fusion polypeptide, comprising 5-10% of the total soluble bacterial protein, was purified to apparent homogeneity by phosphocellulose and hydroxylapatite column chromatography [30].
• The three other proteins, of 100, 32, and 28 kDa, display little sequence or structural binding specificity apart from their preference for uridine-rich sequences [31].

Physical interactions of GOSR1

• The structure of the 28 kDa beta-lactamase inhibitor protein-II (BLIP-II) in complex with the TEM-1 beta-lactamase has been determined to 2.3 A resolution [32].
• Several lines of evidence indicate that the 28-kDa and the 26-kDa cap binding proteins of eIF-4B and eIF-4F are antigenically distinct polypeptides [33].
• Using an anti-clusterin affinity column, we found that an additional protein component with a molecular mass of 28-kDa co-purifies with clusterin from human plasma [34].
• The homology observed suggests, after comparison with the structures of other intracellular CaBPs, that rat 9 kDa CaBP mRNA contains the remains of an untranslated calcium-binding site III-like structure seen in 28 kDa CaBP from kidney and cerebellum of rat [35].
• In the artery extract, serum IgG from 6/18 MPA patients bound to an 85 kDa antigen, whereas purified IgG from all WG patients tested bound to a 28 kDa protein band and IgM from CSS patients bound to 2 main antigens of 38 and 60 kDa [36].

Enzymatic interactions of GOSR1

• RPA32 was cleaved rapidly to a approximately 28-kDa polypeptide containing the C-terminus that was partially resistant to further digestion [37].
• Furthermore, Western blots showed a 118-kDa STAT1 band at the start of the PHA stimulation that was apparently cleaved to STAT1alpha (91 kDa) and a 28 kDa-fragment with further stimulation [38].
• PS1 protein is generated as a 47 kDa protein and is endoproteolytically cleaved into N-terminal 28 kDa and C-terminal 19 kDa fragments in vivo [39].
• MMP-7 cleaves the collagen XVIII NC1 domain to generate a 28-kDa fragment in the cornea [40].

Regulatory relationships of GOSR1

• In human WISH cells, IFN also induces a protein with a molecular mass of 28 kDa (28K) [41].
• The 28-kDa protein whose phosphorylation is induced by protein kinase C activators in MCF-7 cells belongs to the family of low molecular mass heat shock proteins and is the estrogen-regulated 24-kDa protein [14].
• The RAZ1 gene produces two transcripts with variant 5'-untranslated regions containing identical open reading frames that express a 28 kDa protein in vitro [42].
• Localization of distinct functional domains on prekallikrein for interaction with both high molecular weight kininogen and activated factor XII in a 28-kDa fragment (amino acids 141-371) [43].
• Furthermore, only the fractions within the molecular mass ranges of 56 to 44 and 35 to 28 kDa induced IFN-gamma synthesis [44].

Other interactions of GOSR1

• Chromosomal mapping analyses reveal that human GS27 is located on chromosome 17q21 and GS28 on approximately 17q11 [18].
• We also report that GOS 28 and its partnering t-SNARE heavy chain, syntaxin 5, reside together in every cisterna of the stack [1].
• Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) GS28 and syntaxin 5 can be reciprocally coimmunoprecipitated from Golgi extracts, suggesting that they exist in a protein complex [45].
• Two-dimensional polyacrylamide gel electrophoresis (2D-PAGE)/mass-spectrometry analysis identified the 28-kDa protein as human tumor protein D52 (TPD52), whose expression had been previously described only in normal and neoplastic epithelia [46].
• These data suggest that 28-kDa pro-BDNF is not an obligatory intermediate in the formation of the 14-kDa form in the constitutive secretory pathway [47].

Analytical, diagnostic and therapeutic context of GOSR1

• In agreement with this result and also suggesting that the native protein is a monomer, gel-filtration experiments indicated a molecular mass of 28 kDa for TFIID under nondenaturing conditions [48].
• An ELISA with the purified 28-kDa EBNA as antigen was used to quantitate anti-EBNA antibody in human serum samples [30].
• Here we show that the activity of NF-AT in electrophoretic gel mobility-shift assays is greatly enhanced by a distinct protein with an apparent molecular mass of 28 kDa [49].
• These biochemical results appeared entirely consistent with indirect immunofluorescence experiments, demonstrating that the 28-kDa protein resided within the perinuclear region of 37 degrees C cells in close proximity to the Golgi complex [50].
• The affinity purified protein from both peaks was identical in Western blot analysis and had a molecular mass of 28 kDa under reducing conditions [51].

References