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Role of Serum and Glucocoritcoid [sic] inducible Kinase SGK1 in the regulation of glucose transport

von Dr. Sankarganesh Jeyaraj

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[1.] Sj/Fragment 007 01 - Diskussion
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Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop, Sj, Uldry and Thorens 2004

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Hindemith
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Yes
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Quelle: Uldry and Thorens 2004
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[Signature sequences conserved between the] different members of the SLC2 family are present at distinct locations in the primary structure. The presence of these sequences, however, does not predict the substrate specificity of these transporters.

Glucose transporters are expressed in every cell of the body, as might be anticipated from the key role of glucose in providing metabolic energy and building blocks for the synthesis of biomolecules. The specific physiological role of the isoforms expressed in tissues involved in the control of glucose homeostasis, i.e. muscle, adipose tissue, liver, pancreatic beta-cells and brain, has been studied in greatest detail. Indeed, in these tissues glucose transporters play important roles in the control of glucose utilization, glucose production and glucose sensing and their dysregulated expression may underlie pathogenetic mechanisms leading to development of diabetes mellitus, but also other specific monogenic diseases (17).

Facilitated diffusion of glucose across plasma membranes has been studied for several decades (18). The recognition that human erythrocytes have a high density of glucose transporters allowed the initial biochemical purification of this transporter and the preparation of specific antibodies. These were then used for initial cloning of a human glucose transporter by screening an expression library prepared from a human hepatoma cell line (HepG2) (4).This glucose transporter, named GLUT1 (SLC2A1) , was then used for subsequent cloning, by low-stringency screening, of GLUT2–5 (SLC2A2, SLC2A3, SLC2A4, SLC2A5)


4. Kloppel,G, Lohr,M, Habich,K, Oberholzer,M, Heitz,PU: Islet pathology and the pathogenesis of type 1 and type 2 diabetes mellitus revisited. Surv.Synth.Pathol.Res. 4:110-125, 1985

17. Fernandez,EB: [Monogenic forms of diabetes mellitus]. An.R.Acad.Nac.Med.(Madr.) 123:211-217, 2006

18. Gylfe,E, Grapengiesser,E, Hellman,B: Propagation of cytoplasmic Ca2+ oscillations in clusters of pancreatic beta-cells exposed to glucose. Cell Calcium 12:229-240, 1991

Signature sequences conserved between the different members of the SLC2 family are present at distinct locations in the primary structure (Fig. 2). The presence of these sequences, however, does not predict the substrate specificity of these transporters.

Glucose transporters are expressed in every cell of the body, as might be anticipated from the key role of glucose in providing metabolic energy and building blocks for the synthesis of biomolecules. The specific physiological role of the isoforms expressed in tissues involved in the control of glucose homeostasis, i.e. muscle, adipose tissue, liver, pancreatic beta- cells and brain, has been studied in greatest detail. Indeed, in these tissues glucose transporters play important roles in the control of glucose utilization, glucose production and glucose sensing and their dysregulated expression may underlie pathogenetic mechanisms leading to development of diabetes mellitus, but also other specific monogenic diseases (see below).

Facilitated diffusion of glucose across plasma membranes has been studied for several decades [43]. The recognition that human erythrocytes have a high density of glucose transporters allowed the initial biochemical purification of this transporter and the preparation of specific antibodies. These were then used for initial cloning of a human glucose transporter by screening an expression library prepared from a human hepatoma cell line (HepG2) [53]. This glucose transporter, GLUT1, was then used for subsequent cloning, by low-stringency screening, of GLUT2–5.


43. Lieb WR, Stein WD (1971) New theory for glucose transport across membranes. Nat New Biol 230:108–109

53. Mueckler M, Caruso C, Baldwin SA, Panico M, Blench I, Morris HR, Allard WJ, Lienhard GE, Lodish HF (1985) Sequence and structure of a human glucose transporter. Science 229:941–945

Anmerkungen

The source is not mentioned anywhere.

Sichter
(Hindemith) LieschenMueller

[2.] Sj/Fragment 007 19 - Diskussion
Zuletzt bearbeitet: 2016-11-23 22:44:00 WiseWoman
Fragment, Gesichtet, Joost et al 2002, KomplettPlagiat, SMWFragment, Schutzlevel sysop, Sj

Typus
KomplettPlagiat
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Hindemith
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Yes
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Quelle: Joost et al 2002
Seite(n): E975, E976, Zeilen: E975: r.col: 18ff; E976: l.col: 1ff
Class I is comprised of the extensively characterized glucose transporters GLUT1 to GLUT4, which can be distinguished on the basis of their distinct tissue distributions (GLUT1, erythrocytes, brain micro vessels; GLUT2 , liver, pancreatic islets; GLUT3, neuronal cells; GLUT4, muscle, adipose tissue) and their hormonal regulation (e.g., insulin sensitivity of GLUT4) (19). Class II is comprised of the fructose-specific transporter GLUT5 (20) and three related proteins, GLUT7 (SLC1A7), GLUT9 (SLC1A9), and GLUT11 (SLC1A11) (21) For GLUT11, fructose-inhibitable glucose transport activity has been demonstrated in a system of reconstituted vesicles. Class III is characterized by the lack of a glycosylation site in the first extra cellular linker domain and by the presence of such a site in loop 9. HMIT1 (SLC1A13), can be included in the class III GLUTs . Glucose transport activity has been demonstrated for GLUT6 and GLUT8. It should be emphasized, however, that the designation of the family does not necessarily reflect the substrate specificity of its members, which may transport sugars or polyols other than glucose (e.g. GLUT5-fructose, MIT1-myoinositol) (20).

19. Davey,KA, Garlick,PB, Warley,A, Southworth,R: Immunogold labeling study of the distribution of GLUT-1 and GLUT-4 in cardiac tissue following stimulation by insulin or ischemia. Am.J.Physiol Heart Circ.Physiol 292:H2009-H2019, 2007

20. Drozdowski,LA, Woudstra,TD, Wild,GE, Clandinin,MT, Thomson,AB: Ageassociated changes in intestinal fructose uptake are not explained by alterations in the abundance of GLUT5 or GLUT2. J.Nutr.Biochem. 15:630-637, 2004

21. Stuart,CA, Yin,D, Howell,ME, Dykes,RJ, Laffan,JJ, Ferrando,AA: Hexose transporter mRNAs for GLUT4, GLUT5, and GLUT12 predominate in human muscle. Am.J.Physiol Endocrinol.Metab 291:E1067-E1073, 2006

Class I is comprised of the extensively characterized glucose transporters GLUT1 to GLUT4, which can be distinguished on the basis of their distinct tissue distributions (GLUT1, erythrocytes, brain microvessels; GLUT2, liver, pancreatic islets; GLUT3, neuronal cells; GLUT4, muscle, adipose tissue) and their hormonal regulation (e.g., insulin sensitivity of GLUT4). Class II is comprised of the fructose-specific transporter GLUT5 and three related proteins, GLUT7, GLUT9, and GLUT11. For GLUT11, fructose-inhibitable glucose transport activity has been demonstrated in a system of reconstituted vesicles (4). Class III is characterized by the lack of a glycosylation site in the first extracellular linker domain and by the presence of such a site in loop 9.

[page E976]

[...] (HMIT1, Ref. 18) can be included in the class III GLUTs (10). Glucose transport activity has been demonstrated for GLUT6 and GLUT8. It should be emphasized, however, that the designation of the family does not necessarily reflect the substrate specificity of its members, which may transport sugars or polyols other than glucose (e.g., GLUT5, fructose; HMIT1, myoinositol).


4. Doege H, Bocianski A, Scheepers A, Axer H, Eckel J, Joost HG, and Schürmann A. Characterization of the human glucose transporter GLUT11, a novel sugar transport facilitator specifically expressed in heart and skeletal muscle. Biochem J 359: 443–449, 2001.

10. Joost HG and Thorens B. The extended GLUT-family of sugar/polyol transport facilitators—nomenclature, sequence characteristics, and potential function of its novel members. Molec Membr Biol 18: 247–256, 2001.

18. Uldry M, Ibberson M, Riederer B, Chatton JY, Horisberger JD, and Thorens B. Identification of a novel H+-myoinositol symporter expressed predominantly in the brain. EMBO J 20: 4467–4477, 2001.

Anmerkungen

The source is not given.

Sichter
(Hindemith) LieschenMueller


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