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Characterization of the muscle-speci...

Zhao, Hao.

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Characterization of the muscle-specific beta(m) protein: A new member of the X,K-ATPase beta-subunit family.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Characterization of the muscle-specific beta(m) protein: A new member of the X,K-ATPase beta-subunit family./
作者:	Zhao, Hao.
面頁冊數:	98 p.
附註:	Source: Dissertation Abstracts International, Volume: 64-01, Section: B, page: 0199.
Contained By:	Dissertation Abstracts International64-01B.
標題:	Chemistry, Biochemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3078915
ISBN:	0493999248

Characterization of the muscle-specific beta(m) protein: A new member of the X,K-ATPase beta-subunit family.
Zhao, Hao.

Characterization of the muscle-specific beta(m) protein: A new member of the X,K-ATPase beta-subunit family. - 98 p.

Source: Dissertation Abstracts International, Volume: 64-01, Section: B, page: 0199.

Thesis (Ph.D.)--Medical College of Ohio at Toledo, 2003.

The fifth member of the X,K-ATPase beta subunit family, beta m, was identified by our lab. The homologous gene transcripts in human, rat and pig exist predominantly in skeletal muscle and at a lower level in hearts of all species tested. In vitro expression analysis using Xenopus oocytes revealed that although sharing most common structures of the beta subunit family, the betam, does not serve as a chaperone for any known X,K-ATPase alpha subunits and Ca-ATPase. In current study, we have shown that the betam protein expression is highly tissue-specific, being detected mainly in skeletal muscles. Moreover, the higher level of protein expression in neonatal than adult animal tissues suggests its involvement in the muscle development. Immunoprecipitation study confirmed that the betam cannot form stable complex with Na pump alpha subunits and Ca-ATPase in vivo. The molecular weight of native beta m purified from neonatal pig skeletal muscle was determined by mass spectrometry to be 47.2 +/- 0.15 KDa. The betam was detected in nucleus by subcellular fractionation and immunohistochemical approaches. Furthermore, we have localized the betam in the inner nuclear membrane of skeletal muscle cells. We also showed that the betam is not a component of nuclear pore complex. Using bacterial two-hybrid system we have identified a putative counterpart of the betam, which is not a constituent of known ATPases. These results demonstrate that despite belonging to the X,K-ATPase beta family, the betam has distinctive properties and may have completely different functions than other beta subunits. Therefore, the physiological roles of X,K-ATPase beta subunit family members are not limited to be just an isoform of ATPases.

ISBN: 0493999248Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Characterization of the muscle-specific beta(m) protein: A new member of the X,K-ATPase beta-subunit family.
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245 1 0 $a Characterization of the muscle-specific beta(m) protein: A new member of the X,K-ATPase beta-subunit family.
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502 $a Thesis (Ph.D.)--Medical College of Ohio at Toledo, 2003.
520 $a The fifth member of the X,K-ATPase beta subunit family, beta m, was identified by our lab. The homologous gene transcripts in human, rat and pig exist predominantly in skeletal muscle and at a lower level in hearts of all species tested. In vitro expression analysis using Xenopus oocytes revealed that although sharing most common structures of the beta subunit family, the betam, does not serve as a chaperone for any known X,K-ATPase alpha subunits and Ca-ATPase. In current study, we have shown that the betam protein expression is highly tissue-specific, being detected mainly in skeletal muscles. Moreover, the higher level of protein expression in neonatal than adult animal tissues suggests its involvement in the muscle development. Immunoprecipitation study confirmed that the betam cannot form stable complex with Na pump alpha subunits and Ca-ATPase in vivo. The molecular weight of native beta m purified from neonatal pig skeletal muscle was determined by mass spectrometry to be 47.2 +/- 0.15 KDa. The betam was detected in nucleus by subcellular fractionation and immunohistochemical approaches. Furthermore, we have localized the betam in the inner nuclear membrane of skeletal muscle cells. We also showed that the betam is not a component of nuclear pore complex. Using bacterial two-hybrid system we have identified a putative counterpart of the betam, which is not a constituent of known ATPases. These results demonstrate that despite belonging to the X,K-ATPase beta family, the betam has distinctive properties and may have completely different functions than other beta subunits. Therefore, the physiological roles of X,K-ATPase beta subunit family members are not limited to be just an isoform of ATPases.
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650 4 $a Biology, Molecular. $3 1017719
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