Sequence, tissue distribution, and differential expression of mRNA for a putative insulin-responsive glucose transporter in mouse 3T3-L1 adipocytes.

Kaestner, Klaus H.; Christy, Robert J.; McLenithan, John C.; Braiterman, Lelita T.; Cornelius, Peter; Pekala, Phillip H.; Lane, M. Daniel

doi:10.1073/pnas.86.9.3150

Cited by 296 publications

(150 citation statements)

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“…The nucleotide sequence of GLUT4 cDNA in the NSY mouse was found to be the same as in the C3H/He mouse. The nucleotide sequence in these two strains, however, was different from the previously reported sequence in 129/v strain [19]. This difference in nucleotide sequence led to the substitution of six amino acids in the predicted amino acid sequence compared with the previously reported one ( Table 2).…”

Section: Resultsmentioning

confidence: 43%

“…Total RNA was extracted from the muscle of NSY and C3H/He mice. The DNA sequence of the Glut4 gene of NSY and C3H/He mice was determined by PCR amplification of muscle cDNA as four overlapping segments, using primers based on the sequence of murine GLUT4 cDNA [19]. The resulting PCR products were subcloned into pT7Blue Vector (Novagen, Madison, Wis., USA), subjected to DNA sequencing and analysed on an ABI377 sequencer (Perkin-Elmer, Foster City, Calif., USA).…”

Section: Methodsmentioning

confidence: 99%

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Age-dependent changes in phenotypes and candidate gene analysis in a polygenic animal model of Type II diabetes mellitus; NSY mouse

et al. 2000

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Type II (non-insulin-dependent) diabetes mellitus is a polygenic disease characterised by insulin resistance in muscle, fat and liver, and the failure of pancreatic beta cells to adequately compensate for this resistance [1,2]. Glucose tolerance is reported to be impaired with advancing age [3,4]. Deterioration of glucose tolerance can be due to impaired insulin secretion or impaired insulin action or both. The relative contribution of insulin deficiency and insulin resistance to the pathogenesis of age-related glucose intolerance is still controversial [5] because of the difficulty in doing longitudinal studies in humans. Longitudinal analysis of glucose tolerance in animal models with different degrees of glucose intolerance is one of the best ways to address this question.The Nagoya-Shibata-Yasuda (NSY) mouse strain was established as an inbred animal model with spontaneous development of Type II diabetes, by selective breeding for glucose intolerance from out- Abstract Aims/hypothesis.The Nagoya-Shibata-Yasuda (NSY) mouse closely mimics human Type II (non-insulin-dependent) diabetes mellitus in that the onset is age-dependent, the animals are not severely obese, and both insulin resistance and impaired insulin response to glucose contribute to disease development. The aim of this study was to clarify the influence of age on the pathogenesis of diabetes and to analyse a candidate gene for Type II diabetes in this strain. Methods. Several phenotypic characteristics related to diabetes mellitus were monitored longitudinally in male NSY and control C3H/He mice. The nucleotide sequence of Glut4, a candidate gene for Nidd1nsy (a susceptibility gene for Type II diabetes) on Chromosome 11, encoding insulin-sensitive glucose transporter, was determined in NSY and C3H mice. Results. Glucose intolerance worsened with age, and fasting blood glucose and fasting plasma insulin concentration increased with age in NSY mice. Pancreatic insulin content increased until 24 weeks of age but then decreased at 48 weeks of age in NSY mice. The hypoglycaemic response to insulin was statistically significantly smaller in NSY than in C3H/He mice. The nucleotide sequence of GLUT4 cDNA was identical in NSY and C3H/He mice, but both were different from the sequence reported previously. Conclusion/interpretation. Insulin secretion and insulin resistance, as well as ageing possibly play an important part in the disease development in NSY mice. A decline of pancreatic insulin content in older age might cause the relative insulin deficiency in this strain. Nucleotide sequencing suggests that Glut4 is unlikely to be a candidate gene for Nidd1nsy. [Diabetologia (2000) 43: 932±938]

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Section: Resultsmentioning

confidence: 43%

Section: Methodsmentioning

confidence: 99%

Age-dependent changes in phenotypes and candidate gene analysis in a polygenic animal model of Type II diabetes mellitus; NSY mouse

et al. 2000

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“…The 5Ј primer contained the sequence of the T7 promoter for the preparation of riboprobes for RNA gel shift assays and immunoprecipitation experiments. The GLUT4 3ЈUTR construct is bp 1590 to 2500 of the insulin-responsive glucose transporter contained within pBluescript (20). The plasmid was digested with restriction enzymes to produce templates for T3 transcripts containing the complete 3ЈUTR plus some coding region (XhoI) and progressively shorter sequences which remove potential binding sites for Hel-N1.…”

Section: Methodsmentioning

confidence: 99%

“…The cDNAs used in these studies were as follows: GLUT1, a 2.7-kb EcoRI fragment encoding the murine 3T3-L1 homolog of the HepG2/ brain glucose transporter (20); GLUT4, a 1.8-kb EcoRI fragment encoding the 3T3-L1 homolog of the adipose/muscle (insulin-responsive) glucose transporter (20); and ␤-actin, a 1.9-kb HindIII fragment obtained from D. W. Cleveland, The Johns Hopkins University School of Medicine, Baltimore, Md. (6).…”

Section: Methodsmentioning

confidence: 99%

Ectopic Expression of Hel-N1, an RNA-Binding Protein, Increases Glucose Transporter (GLUT1) Expression in 3T3-L1 Adipocytes

Jain

Andrews

McGowan

et al. 1997

Molecular and Cellular Biology

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186

174

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3T3-L1 preadipocytes ectopically expressing the mammalian RNA-binding protein Hel-N1 expressed up to 10-fold more glucose transporter (GLUT1) protein and exhibited elevated rates of basal glucose uptake. Hel-N1 is a member of the ELAV-like family of proteins associated with the induction and maintenance of differentiation in various species. ELAV proteins are known to bind in vitro to short stretches of uridylates in the 3 untranslated regions (3 UTRs) of unstable mRNAs encoding growth-regulatory proteins involved in transcription and signal transduction. GLUT1 mRNA also contains a large 3 UTR with a U-rich region that binds specifically to Hel-N1 in vitro. Analysis of the altered GLUT1 expression at the translational and posttranscriptional levels suggested a mechanism involving both mRNA stabilization and accelerated formation of translation initiation complexes. These findings are consistent with the hypothesis that the Hel-N1 family of proteins modulate gene expression at the level of mRNA in the cytoplasm.Interaction of RNA-binding proteins with cis elements in mRNAs is believed to be involved in regulation of their stability and translational efficiency (reviewed in reference 32). The regulated stability of transferrin, granulocyte-macrophage colony-stimulating factor, and histone mRNAs has been shown, at least in part, to be controlled by the binding of specific proteins to consensus sequences in the 3Ј untranslated region (3ЈUTR) of these messages (3, 37, 41). Studies of tobacco mosaic virus, the Drosophila melanogaster developmental gene hunchback, human cytokine, and 15-lipoxygenase mRNAs have demonstrated that the 3ЈUTR also contains information capable of regulating translational efficiency which may be mediated by RNA-binding proteins (13,25,35,36). A major class of RNA-binding proteins which possess an 80-amino-acid consensus element, termed the RNA recognition motif (RRM) (39), which forms the core of a functional RNAbinding domain has been identified.Hel-N1 (human embryonic lethal abnormal vision [ELAV]-like neuronal protein 1), a mammalian homolog of Drosophila ELAV, is an mRNA-binding protein of the RRM family (15,16,27). Recent studies on Hel-N1, and the alternative form, Hel-N2 (lacking a 13-amino-acid segment between RRM2 and RRM3), in human medulloblastoma cells and embryonic carcinoma P19 cells have indicated that it plays a role in mRNA metabolism (15). These proteins are bound to poly(A) ϩ mRNA in granular RNP structures, and their expression is upregulated during neuronal cell differentiation of P19 cells (15). Likewise, hNT2 cells when induced to differentiate by retinoic acid exhibited a marked increase in the expression of human ELAV-like proteins which colocalized with mRNPs associated with polysomes (1). Hence, data from both of these studies support an important role for mammalian ELAV-like proteins in the processes of cell growth and differentiation.Interestingly, members of the ELAV family have been shown to bind the AU-rich regions of the 3ЈUTRs in cytokine and proto-oncogene m...

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“…Two transporters are found in skeletal muscle: (a) the major transporter, GLUT4, which occurs exclusively in muscle and adipose tissue, and which is thought to be responsible for insulin-stimulated glucose transport [17][18][19][20][21], and (b) the ubiquitous GLUTI glucose transporter, which is the major brain transporter and is also present in very small amounts in skeletal muscle [22,23]. The aim of the present study was to investigate GLUT4 expression at both the protein and the mRNA levels in the mdx mouse.…”

Section: Introductionmentioning

confidence: 99%

Expression of the glucose transporter GLUT4 in the muscular dystrophic mdx mouse

Olichon-Berthe

Gautier

Obberghen

et al. 1993

Biochemical Journal

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Glucose transporter protein levels have been investigated in mdx and control (C57Bl/1O) mice. Crude membrane fractions (microsomes plus plasma membranes) were prepared from skeletal muscle, heart, diaphragm and brain of 5-6-week-old and 6-7-month-old control and mdx mice. Using Western blot analysis with C-terminal-specific anti-peptide antibodies, we investigated the glucose transporters GLUT4 in the different muscle tissues and GLUTI in brain. In skeletal tissue from the hindlegs, GLUT4 was increased by -55 % in mdx mice compared with control mice at both ages studied. In the diaphragm, the amount of GLUT4 protein was unchanged in young mdx mice, and was decreased by 37.4 + 4.7% in older mice compared with agematched control mice. No difference was observed between mdx and control mice in the amounts of GLUT4 and GLUTI in heart and brain preparations respectively. To determine whether the change in GLUT4 protein observed in the diaphragm and

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Sequence, tissue distribution, and differential expression of mRNA for a putative insulin-responsive glucose transporter in mouse 3T3-L1 adipocytes.

Cited by 296 publications

References 19 publications

Age-dependent changes in phenotypes and candidate gene analysis in a polygenic animal model of Type II diabetes mellitus; NSY mouse

Age-dependent changes in phenotypes and candidate gene analysis in a polygenic animal model of Type II diabetes mellitus; NSY mouse

Ectopic Expression of Hel-N1, an RNA-Binding Protein, Increases Glucose Transporter (GLUT1) Expression in 3T3-L1 Adipocytes

Expression of the glucose transporter GLUT4 in the muscular dystrophic mdx mouse

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