Disease relevance of GLG1

• Furthermore, we found dysregulated expression of genes not previously associated with pancreatic adenocarcinoma, such as Rac 1, GLG1, NEDD5, RPL-13a, RPS9 and members of the Wnt5A gene family [1].
• Our results suggest that, MG-160 may participate in malignant progression in astrocytomas [2].
• In the present study MG-160 expression was evaluated in human brain tumors exhibiting varying degrees of malignancy [2].
• In contrast to the lower grade tumors, grade IV astrocytomas exhibited variable and weaker expression of MG-160 [2].
• By immunoelectron microscopy the sialoglycoprotein, named MG-160, was localized in medical cisternae of the Golgi apparatus of neurons, glia, adenohypophysis, and cultured rat pheochromocytoma (PC 12) [3].

Psychiatry related information on GLG1

• Microtubules and molecular motor activity are required for determining both the localisation and organisation of the Golgi apparatus [4].
• Presenilins 1 and 2 (PS1/2), causative molecules for familial Alzheimer's disease (FAD), are multipass transmembrane proteins localized predominantly in the endoplasmic reticulum (ER) and Golgi apparatus [5].
• The capacity of lipoprotein production and hyperlipemia development increases during chronic alcohol consumption, probably as a result of the concomitant hypertrophy of the endoplasmic reticulum and Golgi apparatus [6].
• Fragmentation of the Golgi apparatus of the ballooned neurons in patients with corticobasal degeneration and Creutzfeldt-Jakob disease [7].
• The Golgi apparatus (GA) of the large pyramidal motor neurons in the cerebral cortex (Betz cells), was examined in sixteen patients with sporadic amyotrophic lateral sclerosis (ALS), in one patient with familial ALS (FALS), and in ten non-ALS age matched controls including one patient with Huntington's disease and one patient with a brain infarct [8].

High impact information on GLG1

• Genetically encoded fluorescent probes for signaling events such as GTP/GDP exchange on Ras have revealed signaling on a variety of intracellular membranes, including the Golgi apparatus [9].
• Many of these genes encode enzymes termed glycosyltransferases and glycosidases that reside in the Golgi apparatus where they play the major role in constructing the glycan repertoire that is found at the cell surface and among extracellular compartments [10].
• The above nucleotide derivatives and ATP must first be translocated across the membrane of the endoplasmic reticulum and/or Golgi apparatus before they can serve as substrates in the above lumenal reactions [11].
• The lumens of the endoplasmic reticulum and Golgi apparatus are the subcellular sites where glycosylation, sulfation, and phosphorylation of secretory and membrane-bound proteins, proteoglycans, and lipids occur [11].
• Topography of glycosylation in the rough endoplasmic reticulum and Golgi apparatus [12].

Chemical compound and disease context of GLG1

• Electron microscopy of liver tissue obtained from 2 patients before phenobarbital therapy showed hypertrophy and hyperplasia of smooth endoplasmic reticulum with unusual prominence of the Golgi apparatus and focal modification of the cell surface membranes [13].
• The fragmentation of the Golgi apparatus is morphologically different from that seen with brefeldin A and may reflect disequilibration between the anterograde and retrograde Golgi transport caused by the huge influx of viral glycoproteins contained in virions and membranes flowing through the exocytic pathway [14].
• Oncogenic targeting of an activated tyrosine kinase to the Golgi apparatus in a glioblastoma [15].
• Major mutations in calf-1 and calf-2 domains of glycoprotein IIb in patients with Glanzmann thrombasthenia enable GPIIb/IIIa complex formation, but impair its transport from the endoplasmic reticulum to the Golgi apparatus [16].
• Fragmentation of the Golgi apparatus of motor neurons in amyotrophic lateral sclerosis (ALS). Clinical studies in ALS of Guam and experimental studies in deafferented neurons and in beta,beta'-iminodipropionitrile axonopathy [17].

Biological context of GLG1

• Transfection of chimeric constructs into human embryonic kidney epithelial 293 cells revealed that the cytoplasmic domains of GLG1 and GLG2 targeted the expression of each chimeric protein differentially, GLG1 to the cell surface and GLG2 to the Golgi [18].
• These data suggest that alternative splicing of the GLG1 gene transcript might regulate the function of its product [18].
• We report here a novel variant of the human GLG1 gene product that we call GLG2, cloned from a human monocyte cDNA library [18].
• The predicted amino-acid sequence of ESL-1 is 94% identical (over 1,078 amino acids) to the recently identified chicken cysteine-rich fibroblast growth-factor receptor, except for a unique 70-amino-acid aminoterminal domain of mature ESL-1 [19].
• Affinity, kinetics, and thermodynamics of E-selectin binding to E-selectin ligand-1 [20].

Anatomical context of GLG1

• Antibodies against ESL-1 block the binding of mouse myeloid cells to E-selectin [19].
• Using surface plasmon resonance, we measured the kinetics and affinity of binding of monomeric E-selectin to ESL-1 isolated from mouse bone marrow cells [20].
• Expression of sialyl-Lewis X, an E-selectin ligand, in inflammation, immune processes, and lymphoid tissues [21].
• In this study, a less-aggressive variant of MDA-MB-435 cells obtained from the MDA-MB-435 cell line was engineered to express gap junctional intercellular communication (GJIC)-competent Cx26, a GJIC-incompetent cell surface transported GFP-Cx26 chimera, or a Golgi apparatus-localized, disease-linked Cx26 mutant (D66H) [22].
• MG-160 binds fibroblast growth factors (FGFs) and may be involved in the intracellular trafficking of FGFs and the regulation of cellular response to FGFs [2].

Associations of GLG1 with chemical compounds

• It recognizes the glycoprotein E-selectin ligand-1 (ESL-1) as a major binding partner on mouse myeloid cells [20].
• A known E-selectin ligand is the carbohydrate antigen, sialyl Lewis(x) (sLe(x) (Neu5Ac alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc) [23].
• Transporters of nucleotide sugars, ATP, and nucleotide sulfate in the endoplasmic reticulum and Golgi apparatus [11].
• This truncated C8C8 ceramide was soluble in water (but was still able to cross cell membranes) and was utilized by the Golgi apparatus of living cells to produce water-soluble truncated phospholipids and glycolipids that were then secreted into the medium [24].
• The block to secretion is due to the ability of monensin to suppress the export of these secretory proteins from the Golgi apparatus [25].

Physical interactions of GLG1

• We conclude that endogenous polycystin-2 is transported via the Golgi apparatus to the plasma membrane and has a broader membrane localization than polycystin-1 [26].
• Based on our glycosylation variants of presenilin-1 we hypothesize that complex assembly occurs during transport between the endoplasmic reticulum and the Golgi apparatus [27].
• Oxysterol binding protein (OSBP) is a cytosolic protein that undergoes ligand-induced binding to the Golgi apparatus and has been implicated in the regulation of cellular cholesterol metabolism [28].
• It is documented that TG is transported from the endoplasmic reticulum and the Golgi apparatus to the follicular lumen by transport vesicles; most of it being present in the expanded endoplasmic reticulum throughout the cytoplasm [29].
• The maturation of lipoprotein lipase (LPL) into a catalytically active enzyme was believed to occur only after its transport from the endoplasmic reticulum (ER) to the Golgi apparatus [30].

Enzymatic interactions of GLG1

• We previously reported that BACE1 also cleaved alpha2,6-sialyltransferase (ST6Gal I) in the Golgi apparatus and induced its secretion from the cell [31].
• Changes in ER expression were studied in relation to early Alzheimer changes (i.e. hyperphosphorylated tau) and neuronal metabolism in AD as determined by the size of the Golgi apparatus (GA) or cell size [32].

Co-localisations of GLG1

• However, within 10 min following addition of TRAIL, nearly all the cells showed an increased cytoplasm localization of eNOS which appeared co-localized with the Golgi apparatus at a higher extent than in unstimulated cells [33].
• BACE and furin co-localize within the Golgi apparatus, and propeptide cleavage is inhibited by brefeldin A and monensin, drugs that disrupt trafficking through the Golgi [34].
• Via subcellular localization using C19orf24 in vivo and transfected pEYFP-Golgi plasmid in Hela cells, C19orf24 was shown not to co-localize in the Golgi apparatus, which suggested that it secretes via a new and unknown pathway [35].
• We now report that oxidation of caveolar cholesterol with cholesterol oxidase rapidly displaces the caveolin from the plasma membrane to intracellular vesicles that colocalize with Golgi apparatus markers [36].
• In surface epithelium, paranuclear E-cadherin staining colocalized with Griffonia simplicifolia lectin II in the Golgi apparatus [37].

Regulatory relationships of GLG1

• Budding of transport vesicles in the Golgi apparatus requires the recruitment of coat proteins and is regulated by ADP ribosylation factor (ARF) 1 [38].
• Spatial localization of eNOS has been shown to be regulated by different mechanisms that control its targeting from the Golgi apparatus to the plasma membrane, correct compartmentalization within the membrane, and internalization from the plasma membrane to the cytoplasm after activation [39].
• Confocal microscopy revealed TLR4 to be expressed on the plasma membrane and the Golgi apparatus [40].
• HA-GEC1 expressed in CHO cells was localized in the Golgi apparatus and endoplasmic reticulum (ER) [41].
• ApoE epsilon4 genotype is accompanied by lower metabolic activity in nucleus basalis of Meynert neurons in Alzheimer patients and controls as indicated by the size of the Golgi apparatus [42].

Other interactions of GLG1

• We used a monoclonal antibody (10A8), derived from mice immunized with fractions enriched in Golgi apparatus of rat brain neurons, to isolate an intrinsic membrane sialoglycoprotein of 160 KD from rat brain [3].
• Phosphorylation of Nir2 by Cdk1 facilitates its dissociation from the Golgi apparatus, and phospho-Nir2(pS382) is localized in the cleavage furrow and midbody during cytokinesis [43].
• The E-selectin ligand activity of CD44 is conferred by the elaboration of sialylated, fucosylated binding determinants on N-glycans [44].
• ST6Gal I was colocalized with BACE1 in the Golgi apparatus by immunofluorescence microscopy, suggesting that BACE1 acts on ST6Gal I within the same intracellular compartment [45].
• Overexpression of ARNO3 in mammalian cells results in (i) fragmentation of the Golgi apparatus, (ii) redistribution of Golgi resident proteins as well as the coat component beta-COP, and (iii) inhibition of SEAP transport (secreted form of alkaline phosphatase) [38].

Analytical, diagnostic and therapeutic context of GLG1

• Immunoelectron microscopy with rat and human brain and with rat myocardium and pituitary showed prominent and exclusive staining of cis, medial, and occasionally trans cisternae of the Golgi apparatus [3].
• This differential expression of MG-160 mRNA was verified at the protein level using immunohistochemistry [2].
• Therefore, to further investigate the presence and localization of MG-160 or of an antigenically related protein in several species and tissues, we used a polyclonal antiserum raised against MG-160 purified by antibody (10A8) affinity chromatography [3].
• In several human fetal and adult tissues, three mRNA transcripts for MG160 of 10 kb, 5 kb, and 3.8 kb were identified by Northern blot analysis of poly(A)-selected mRNAs [46].
• By electron microscopy, the enterocytes of these mice lacked nascent chylomicrons in the endoplasmic reticulum and Golgi apparatus [47].

References