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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1989-11-9
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pubmed:abstractText |
1. The distribution of the alpha- and beta-subunits of nucleotide-binding G-proteins among rat liver sinusoidal, lateral and canalicular plasma membranes, endosomes, Golgi membranes and lysosomes was investigated. 2. Pertussis-toxin-catalysed ADP-ribosylation identified a 41 kDa inhibitory alpha-subunit in all liver plasma-membrane functional domains as well as in endosomes. An antibody to a synthetic peptide corresponding to a C-terminal sequence of the inhibitory alpha-subunit also identified the 41 kDa polypeptide in all plasma-membrane domains, in 'early' and 'late' endosomes and in Golgi membranes; this polypeptide was not detected in lysosomes. The antibody-binding studies showed that bile-canalicular plasma membranes had the highest content of the inhibitory alpha-subunit. 3. Immunofluorescent microscopy confirmed the presence of the inhibitory alpha-subunit in all regions of the hepatocyte's cell surface. 4. An antibody recognizing the beta-subunit showed that a 36 kDa polypeptide was present in all plasma membranes and in 'early' and 'late' endosomes; it was not detected in lysosomes. The relative distribution among the fractions of this polypeptide was similar to the distribution of the inhibitory alpha-subunit. 5. The presence of high levels of the G-protein inhibitory alpha-subunit in bile-canalicular plasma membranes was confirmed by demonstration of its co-fractionation with marker enzymes in Nycodenz gradients and by free-flow electrophoresis. The significance of this location is discussed.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-125584,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-13511347,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-211139,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-2432660,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-2433590,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-2826014,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-2833223,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-2836065,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-2848502,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-2859513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-2867760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-2906241,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-2982805,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-2983664,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-3083418,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-3103658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-3104090,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-3104112,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-6091623,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/2508624-942051
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
261
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
905-12
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2508624-Animals,
pubmed-meshheading:2508624-Bile Canaliculi,
pubmed-meshheading:2508624-Blotting, Western,
pubmed-meshheading:2508624-Cell Membrane,
pubmed-meshheading:2508624-Endocytosis,
pubmed-meshheading:2508624-GTP-Binding Proteins,
pubmed-meshheading:2508624-Liver,
pubmed-meshheading:2508624-Lysosomes,
pubmed-meshheading:2508624-Male,
pubmed-meshheading:2508624-Organelles,
pubmed-meshheading:2508624-Rats,
pubmed-meshheading:2508624-Rats, Inbred Strains
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pubmed:year |
1989
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pubmed:articleTitle |
Distribution of G-proteins in rat liver plasma-membrane domains and endocytic pathways.
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pubmed:affiliation |
National Institute for Medical Research, Mill Hill, London, U.K.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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