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| _ < | __/ | |_ | | | |_) | | __/ | (_| | | | | (_| |
|_| \_\ \___| \__| |_| | .__/ \___| \__,_| |_| \__,_|
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GLUT-3
ββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββ
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GLUT-3 (Glucosetransporter Typ 3) (Gen: SLC2A3) heiΓt das Protein, das besonders in der Zellmembran der Neuronen von Tieren lokalisiert ist und die Ein- bzw. Ausschleusung von Glucose sowie von Dehydroascorbat erleichtert. Es handelt sich um ein Membran-Transportprotein. Beim Menschen ist GLUT-3 in geringem MaΓ auch in vielen anderen Gewebetypen vorhanden. Bei der Hausmaus (Mus musculus) ist es eines der hΓ€ufigsten Proteine in den Spermien.cite-ref-u-2-0[2]cite-ref-3[3]cite-ref-4[4]
Das entwicklungsgeschichtlich Γ€lteste Exemplar wurde in Nematostella vectensis, einer Seeanemone gefunden.
Contents
β’ Funktion
β’ Weblinks
β’ Einzelnachweise
ββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββ
Funktion
In Neuronen wird die Expression von GLUT-3 durch AktivitΓ€t der AMP-Kinase reguliert. Dieser Prozess ist ein wichtiger Teil der Unempfindlichkeit von Neuronen gegenΓΌber ExcitotoxizitΓ€t (Γberaktivierung von Glutamatrezeptoren). Auch in der frΓΌhen Entwicklungsphase des Embryos ist GLUT-3 unentbehrlich.cite-ref-5[5]cite-ref-6[6]
WeiterfΓΌhrende Literatur
β’ MaulΓ©n NP, HenrΓquez EA, Kempe S, et al.: Up-regulation and polarized expression of the sodium-ascorbic acid transporter SVCT1 in post-confluent differentiated CaCo-2 cells. In: J. Biol. Chem. 278. Jahrgang, Nr. 11, MΓ€rz 2003, S. 9035β41, doi:10.1074/jbc.M205119200, PMID 12381735 (jbc.org).
β’ Rumsey SC, Kwon O, Xu GW, Burant CF, Simpson I, Levine M: Glucose transporter isoforms GLUT1 and GLUT3 transport dehydroascorbic acid. In: J. Biol. Chem. 272. Jahrgang, Nr. 30, Juli 1997, S. 18982β9, PMID 9228080 (jbc.org).
β’ Liang WJ, Johnson D, Jarvis SM: Vitamin C transport systems of mammalian cells. In: Mol. Membr. Biol. 18. Jahrgang, Nr. 1, 2001, S. 87β95, PMID 11396616.
β’ Rivas CI, ZΓΊΓ±iga FA, Salas-Burgos A, Mardones L, Ormazabal V, Vera JC: Vitamin C transporters. In: J. Physiol. Biochem. 64. Jahrgang, Nr. 4, Dezember 2008, S. 357β75, PMID 19391462.
Weblinks
β’ DβEustachio / reactome: Dehydroascorbate transport across the plasma membrane
Einzelnachweise
cite-note-11. InterPro: Glucose transporter, type 3 (GLUT3)
cite-note-33. β InterPro: IPR002945 Glucose transporter, type 3 (GLUT3)
cite-note-44. β Simpson IA, Dwyer D, Malide D, Moley KH, Travis A, Vannucci SJ: The facilitative glucose transporter GLUT3: 20 years of distinction. In: Am. J. Physiol. Endocrinol. Metab. 295. Jahrgang, Nr. 2, August 2008, S. E242β53, doi:10.1152/ajpendo.90388.2008, PMID 18577699, PMC 2519757 (freier Volltext) β (physiology.org).
cite-note-55. β WeisovΓ‘ P, Concannon CG, Devocelle M, Prehn JH, Ward MW: Regulation of glucose transporter 3 surface expression by the AMP-activated protein kinase mediates tolerance to glutamate excitation in neurons. In: J. Neurosci. 29. Jahrgang, Nr. 9, MΓ€rz 2009, S. 2997β3008, doi:10.1523/JNEUROSCI.0354-09.2009, PMID 19261894 (jneurosci.org).