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Characterization of the human organe...

Jones, Ewen St.Clair.

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Characterization of the human organellar sodium/proton exchanger isoforms NHE8 and NHE9.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Characterization of the human organellar sodium/proton exchanger isoforms NHE8 and NHE9./
Author:	Jones, Ewen St.Clair.
Description:	105 p.
Notes:	Source: Masters Abstracts International, Volume: 46-03, page: 1369.
Contained By:	Masters Abstracts International46-03.
Subject:	Biology, Animal Physiology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=MR32726
ISBN:	9780494327265

Characterization of the human organellar sodium/proton exchanger isoforms NHE8 and NHE9.
Jones, Ewen St.Clair.

Characterization of the human organellar sodium/proton exchanger isoforms NHE8 and NHE9. - 105 p.

Source: Masters Abstracts International, Volume: 46-03, page: 1369.

Thesis (M.Sc.)--McGill University (Canada), 2007.

Sodium/proton exchangers (NHEs) are secondary active transporters that catalyze the electroneutral exchange of Na+ and H+ down their respective concentration gradients using the inward electrochemical Na+ gradient established by the plasma membrane Na+/K+-ATPase. NHEs play a fundamental role in maintaining the intracellular pH (pHi) homeostasis and cell volume which are required for stable protein activity, and ultimately cell survival. To date, nine NHE isoforms (NHE 1-9) have been identified, and are expressed in a tissue/cell specific manner, which indicates a degree of specialization in their respective cellular functions. NHE1 through 5 are plasmalemmal-type exchangers, whereas NHE6 and 7 accumulate predominantly in organellar compartments. Substantially less information is known about NHE8 and NHE9. Initial reports have shown that both NHE8 and NHE9 mRNA are ubiquitously expressed, and that NHE8 protein can be detected in the proximal tubules of kidney nephrons (Goyal et al., 2003; de Silva et al., 2003).

ISBN: 9780494327265Subjects--Topical Terms:

1017835
Biology, Animal Physiology.

Characterization of the human organellar sodium/proton exchanger isoforms NHE8 and NHE9.
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020 $a 9780494327265
035 $a (UMI)AAIMR32726
035 $a AAIMR32726
040 $a UMI $c UMI
100 1 $a Jones, Ewen St.Clair. $3 1267771
245 1 0 $a Characterization of the human organellar sodium/proton exchanger isoforms NHE8 and NHE9.
300 $a 105 p.
500 $a Source: Masters Abstracts International, Volume: 46-03, page: 1369.
502 $a Thesis (M.Sc.)--McGill University (Canada), 2007.
520 $a Sodium/proton exchangers (NHEs) are secondary active transporters that catalyze the electroneutral exchange of Na+ and H+ down their respective concentration gradients using the inward electrochemical Na+ gradient established by the plasma membrane Na+/K+-ATPase. NHEs play a fundamental role in maintaining the intracellular pH (pHi) homeostasis and cell volume which are required for stable protein activity, and ultimately cell survival. To date, nine NHE isoforms (NHE 1-9) have been identified, and are expressed in a tissue/cell specific manner, which indicates a degree of specialization in their respective cellular functions. NHE1 through 5 are plasmalemmal-type exchangers, whereas NHE6 and 7 accumulate predominantly in organellar compartments. Substantially less information is known about NHE8 and NHE9. Initial reports have shown that both NHE8 and NHE9 mRNA are ubiquitously expressed, and that NHE8 protein can be detected in the proximal tubules of kidney nephrons (Goyal et al., 2003; de Silva et al., 2003).
520 $a To gain further insight into the subcellular distribution and function of these latter isoforms, full length cDNAs of NHE8 and NHE9 were cloned, epitope tagged and transfected into cultured cell lines. Examination of their subcellular localization by confocal microscopy showed that NHE8 and NHE9 are targeted to lysosomes and endosomes respectively. Furthermore, co-immunoprecipitation experiments indicated that NHE9 can form homodimeric complexes. Co-immunoprecipitation studies and confocal microscopy also indicated that NHE9 may form heterocomplexes with NHE8. In order to further characterize NHE9 under native conditions, a native polyclonal antibody was raised against a distinct region of its C-terminal cytoplasmic tail.
590 $a School code: 0781.
650 4 $a Biology, Animal Physiology. $3 1017835
690 $a 0433
710 2 $a McGill University (Canada). $3 1018122
773 0 $t Masters Abstracts International $g 46-03.
790 $a 0781
791 $a M.Sc.
792 $a 2007
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=MR32726