9783844385335 - the effect of mutating the pdz domains within secreted pdzd2: on its insulinotropic action in ins-ie cells de wat (5 resultados)
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Librería: preigu, Osnabrück, Alemaniapreigu
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Taschenbuch. Condición: Neu. The Effect of Mutating the PDZ domains within secreted PDZD2 | on its insulinotropic action in INS-IE cells | Zee man Wat | Taschenbuch | 96 S. | Englisch | 2011 | LAP LAMBERT Academic Publishing | EAN 9783844385335 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 4…9078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu.
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Librería: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, AlemaniaBuchWeltWeit Ludwig Meier e.K.
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Taschenbuch. Condición: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -PDZ domains are one of the most common protein-protein interaction domains in human. PDZ domain containing 2 protein (PDZD2) contains 6 PDZ domains and is highly expressed in pancreatic beta cells. It undergoes cleavage in the endop…lasmic reticulum to produce a secreted form PDZD2 (sPDZD2) which retains the last two PDZ domains of PDZD2. sPDZD2 is a candidate beta cell regulatory factor. In current study, two mutated forms of sPDZD2 were generated with alterations in the amino acid sequence within the carboxylate-binding loop of one of the two PDZ domains, either at the PDZ5 or at the PDZ6 domain. Current study revealed that both the PDZ5-mutated and PDZ6-mutated sPDZD2 proteins failed to exert the insulinotropic effect that the wildtype sPDZD2 had on INS-1E cells when added exogenously in the culture medium. Both mutant proteins also failed to rescue the silencing action of siRNA on the insulinotropic effect of endogenous PDZD2 in INS-1E cells. These results suggest that intact carboxylate-binding loops of both PDZ5 and PDZ6 domain are crucial for the insulinotropic effect of sPDZD2 exerting on INS-1E cells. 96 pp. Englisch.
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Librería: moluna, Greven, Alemaniamoluna
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Condición: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Winnie Wat Zee manDr Winnie Wat was graduated at the medical school of the University of Hong Kong in 1997. She works as an endocrinologist in Hong Kong. In 2009, She pursued her degree in Master of Med…ical Sciences at her alma mater.
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Librería: buchversandmimpf2000, Emtmannsberg, BAYE, Alemaniabuchversandmimpf2000
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Taschenbuch. Condición: Neu. This item is printed on demand - Print on Demand Titel. Neuware -PDZ domains are one of the most common protein-protein interaction domains in human. PDZ domain containing 2 protein (PDZD2) contains 6 PDZ domains and is highly expressed in pancreatic beta cells. It undergoes cleavage in the endoplasm…ic reticulum to produce a secreted form PDZD2 (sPDZD2) which retains the last two PDZ domains of PDZD2. sPDZD2 is a candidate beta cell regulatory factor. In current study, two mutated forms of sPDZD2 were generated with alterations in the amino acid sequence within the carboxylate-binding loop of one of the two PDZ domains, either at the PDZ5 or at the PDZ6 domain. Current study revealed that both the PDZ5-mutated and PDZ6-mutated sPDZD2 proteins failed to exert the insulinotropic effect that the wildtype sPDZD2 had on INS-1E cells when added exogenously in the culture medium. Both mutant proteins also failed to rescue the silencing action of siRNA on the insulinotropic effect of endogenous PDZD2 in INS-1E cells. These results suggest that intact carboxylate-binding loops of both PDZ5 and PDZ6 domain are crucial for the insulinotropic effect of sPDZD2 exerting on INS-1E cells.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 96 pp. Englisch.
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Librería: AHA-BUCH GmbH, Einbeck, AlemaniaAHA-BUCH GmbH
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Taschenbuch. Condición: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - PDZ domains are one of the most common protein-protein interaction domains in human. PDZ domain containing 2 protein (PDZD2) contains 6 PDZ domains and is highly expressed in pancreatic beta cells. It undergoes cleavage in the endoplasmi…c reticulum to produce a secreted form PDZD2 (sPDZD2) which retains the last two PDZ domains of PDZD2. sPDZD2 is a candidate beta cell regulatory factor. In current study, two mutated forms of sPDZD2 were generated with alterations in the amino acid sequence within the carboxylate-binding loop of one of the two PDZ domains, either at the PDZ5 or at the PDZ6 domain. Current study revealed that both the PDZ5-mutated and PDZ6-mutated sPDZD2 proteins failed to exert the insulinotropic effect that the wildtype sPDZD2 had on INS-1E cells when added exogenously in the culture medium. Both mutant proteins also failed to rescue the silencing action of siRNA on the insulinotropic effect of endogenous PDZD2 in INS-1E cells. These results suggest that intact carboxylate-binding loops of both PDZ5 and PDZ6 domain are crucial for the insulinotropic effect of sPDZD2 exerting on INS-1E cells.
