Linked Life Data

17186307

Source:http://linkedlifedata.com/resource/pubmed/id/17186307

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2007-3-5
pubmed:abstractText
Increase in mRNA expression and transport activity of the betaine gamma-amino-n-butyric acid cotransporter (BGAT) in response to hyperosmolality has been previously shown in MDCK cells. However, the hyperosmolality-induced response of endogenous BGAT protein expression was not investigated in detail. We show two forms of endogenous BGAT immunoreactivity that are expressed in MDCK II cells. Both are sensitive to Peptide N-Glycosidase F (PNGase F), suggesting that they are N-glycosylated proteins. One band, about 75 kDa, is resistant to Endo H, while the other 55 kDa band is sensitive to it, suggesting that they are fully N-glycosylated mature form in the post-Golgi compartment and core-glycosylated immature form in the endoplasmic reticulum (ER), respectively. When treated with hyperosmolality, they are significantly increased. But the rate of BGAT processing, as assessed by the ratio of mature to immature form, is not increased, suggesting that hyperosmolality does not facilitate the export of BGAT from the ER to the secretory pathway. Surface biotinylation and confocal microscopy show that hyperosmolality significantly increases the amount of the mature form of BGAT on the basolateral membrane with a very small fraction on the apical membrane. We conclude that BGAT is an N-glycosylated protein with two glycoforms and endogenous BGAT synthesis rather than processing is involved in the adaptation to the hyperosmotic stress.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0031-6768
pubmed:author
pubmed:issnType
Print
pubmed:volume
454
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
143-53
pubmed:dateRevised
2007-12-3
pubmed:meshHeading
pubmed-meshheading:17186307-Animals, pubmed-meshheading:17186307-Blotting, Western, pubmed-meshheading:17186307-Cell Line, pubmed-meshheading:17186307-Cell Membrane, pubmed-meshheading:17186307-Dogs, pubmed-meshheading:17186307-GABA Plasma Membrane Transport Proteins, pubmed-meshheading:17186307-Glycosylation, pubmed-meshheading:17186307-Immunohistochemistry, pubmed-meshheading:17186307-Intracellular Membranes, pubmed-meshheading:17186307-Kidney, pubmed-meshheading:17186307-Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase, pubmed-meshheading:17186307-Osmotic Pressure, pubmed-meshheading:17186307-Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, pubmed-meshheading:17186307-Protein Isoforms, pubmed-meshheading:17186307-Protein Processing, Post-Translational, pubmed-meshheading:17186307-Time Factors
pubmed:year
2007
pubmed:articleTitle
Characterization of endogenous betaine gamma-amino-n-butyric acid cotransporter glycoform and its hyperosmotic regulation in MDCK cells.
pubmed:affiliation
Department of Pharmacology, School of Pharmacy, Fudan University, Shanghai, China. xuemzhang@shmu.edu.cn
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural