Disease relevance of UGCGL1

• To circumvent this, we have used a defective herpes simplex virus vector to overexpress the rat brain glucose transporter (GT) gene under the control of the human cytomegalovirus ie1 promoter [1].
• To assess the contribution of the HepG2/erythrocyte glucose-transporter (HepG2 GT) gene to the inherited susceptibility to non-insulin-dependent diabetes mellitus (NIDDM), cDNA and genomic probes were used to search for restriction-endonuclease polymorphisms at this locus [2].
• Microphthalmia, cataracts, and chronic nongranulomatous inflammation involving the anterior and/or posterior segments of the eye were also found. gamma GT is detectable histochemically as early as 11.5 gestational days in the outer neuroectodermal layer and after birth is more abundant in the ciliary body than in the retinal pigment epithelium [3].
• OBJECTIVE: To examine anxiety levels of women diagnosed with gestational diabetes mellitus (GDM) and to compare these with glucose-tolerant (GT) women at similar stages of pregnancy [4].
• DESIGN: Midthigh AT, muscle composition, and insulin sensitivity were compared in 11 obese patients with type 2 diabetes mellitus (DM); 40 obese, glucose-tolerant (GT) and 15 lean, GT volunteers; and 38 obese subjects who completed a weight-loss program [5].

Psychiatry related information on UGCGL1

• However, an interaction was observed between alcohol consumption and glucose tolerance (GT) status [6].
• In this study, we assessed the GT protein in the frontal cortex, hippocampus, cerebellum, and cerebral microvessels in subjects with Alzheimer's disease (AD) and controls [7].

High impact information on UGCGL1

• Monoglucosylated glycans are then recreated by the UDP-Glc:glycoprotein glucosyltransferase (GT), and thus recognized again by the lectins, only when linked to improperly folded protein moieties, as GT behaves as a sensor of glycoprotein conformations [8].
• RNA transcripts encoding the complete human glucose transporter (GT) or fragments of GT corresponding to the NH2-terminal 340 amino acids (GT-N) or the COOH-terminal 148 amino acids (GT-C) were synthesized in vitro from SP6 plasmids [9].
• Here we demonstrate differential regulation of these two GTs in adipose cells of diabetic and insulin-treated diabetic rats and compare changes in the expression of each GT with marked alterations in insulin-stimulated glucose transport activity [10].
• In contrast, GTs detected with antisera to the carboxyl terminus of the HepG2 GT or to the human erythrocyte GT show no significant change with diabetes or insulin treatment [10].
• UDP-glucose:glycoprotein glucosyltransferase (GT) is a key component of the glycoprotein-specific folding and quality control system in the endoplasmic reticulum [11].

Chemical compound and disease context of UGCGL1

• Virucidal Activity of a GT-Rich Oligonucleotide against Herpes Simplex Virus Mediated by Glycoprotein B [12].
• UDP-galactose:beta-1,4 N-acetyl glucosamine galactosyltransferase (4 beta GT) is a promising tumor marker for ovarian cancer [13].
• Hepatomegaly with liver dysfunction (SGOT, 102 U/L; gamma-glutamyl transferase (GT), 159 U/L) and lactic acidosis (plasma lactate, 7.3 mmol/L) developed simultaneously [14].
• A discriminant function has been devised using sex, CEA, psi, gamma GT, ACT and PHI that can identify 89% of Dukes "D" patients prior to surgery with a misclassification of 7% of other cases of colorectal cancer [15].
• GT was assessed according to the criteria of the Expert Committee on the Diagnosis and Classification of Diabetes Mellitus [16].

Biological context of UGCGL1

• The highest degree of identity resides in the COOH-terminal 20% of these proteins, the putative catalytic domain of HUGT1 [17].
• The HUGT1 and HUGT2 cDNAs were expressed by transient transfection in COS-1 monkey cells to obtain similar levels of protein localized to the ER [18].
• HUGT1 and HUGT2 mRNAs are broadly expressed in multiple tissues and differ slightly in their tissue distribution [18].
• HUGT1 is expressed as multiple mRNA species that are induced to similar extents upon disruption of protein folding in the ER [18].
• Site-directed alanine mutagenesis within a highly conserved region of HUGT1 identified four residues that are essential for catalytic function [18].

Anatomical context of UGCGL1

• The rat brain glucose transporter (GT) gene is rapidly activated coincident with the initiation of growth in response to oncogenic transformation or the addition of growth factors to quiescent fibroblasts [19].
• Microinfusion of GT vectors into the rat hippocampus also reduces kainic acid-induced seizure damage in the CA3 cell field [20].
• GT expressed from vIE1GT was readily immunoprecipitated from membrane fractions of vIE1GT-infected Vero cells [1].
• Comparisons of gamma GT RNA stability were not possible since nontransformed liver cells (228) contain little or no gamma GT RNA [21].
• GT-tSBO activity is catalyzed by GT mu which has polymorphic expression in human lymphocytes [22].

Associations of UGCGL1 with chemical compounds

• Whereas neither catalytic domain displayed detectable activity when expressed alone, co-expression of either catalytic domain with the noncatalytic amino-terminal portion of HUGT1 conferred UDP-Glc binding and transfer of glucose that was specific for unfolded glycoprotein substrates [17].
• The contribution of the NH2-terminal remainder of HUGT1 to glucosyltransferase function is presently unknown [17].
• We present crystal structures of the UDP flavonoid/triterpene GT UGT71G1 from Medicago truncatula bound to UDP or UDP-glucose [23].
• gamma-Glutamyl transpeptidase (EC 2.3.2.2, gamma GT) is a membrane-bound ectoenzyme that plays an important role in the metabolism of glutathione [24].
• Thirteen patients were homozygous for the genetic polymorphism of MDR1 (n = 7 for guanine, n = 6 for thymidine), whereas 17 patients were heterozygous (GT) [25].

Other interactions of UGCGL1

• In this report we demonstrate that HUGT2 is localized to the ER in a manner that overlaps the distribution of HUGT1 [17].
• Lectin (calreticulin [CRT])-N-glycan-mediated quality control of glycoprotein folding is operative in trypanosomatid protozoa but protein-linked monoglucosylated N-glycans are exclusively formed in these microorganisms by UDP-Glc:glycoprotein glucosyltransferase (GT)-dependent glucosylation [26].

Analytical, diagnostic and therapeutic context of UGCGL1

• Northern blotting reveals that the adipose/muscle GT mRNA decreases 50% with diabetes and increases to 6.8-fold control (13-fold diabetic) levels with insulin treatment [10].
• By using indirect double immunofluorescence techniques, vIE1GT was shown to be capable of enhancing GT expression in cultured hippocampal neurons and glia [1].
• When examined 2 days later, GT expression from vIE1GT was demonstrated in hippocampal neurons by in situ hybridization; a small but significant increase in glucose transport was detected in tissue immediately surrounding the injection site by 2-deoxy[14C]glucose uptake and autoradiography [1].
• Using a reverse transcriptase-polymerase chain reaction, we found that type I (but not types II or III) gamma GT RNA is made by the mouse eye; the gamma GT(I)rasT24 transgene transcription product was detected in the eyes of all five transgenic lines [3].
• Examples, based on the literature and our own work, illustrate the increase of A and GT by cortisone acetate premedication as well as long-term oral contraceptive medication [27].

References