rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1981-7-23
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pubmed:abstractText |
The carboxylic ionophore, monensin, blocks the migration of glycoprotein-containing vesicles from the Golgi region to the plasma membrane in fibroblasts resulting in an accumulation of secretory products in the Golgi cisternae. Treatment of cultured I-cell fibroblasts with monensin (0.5 muM) decreased the abnormal excretion of beta-hexosaminidase to 40% of untreated cultures within 15 min. A corresponding intracellular accumulation of the enzyme to greater than 200% of untreated cultured by 24 h was also observed. A small intracellular accumulation and slightly enhanced excretion of beta-hexosaminidase occurred in treated normal fibroblasts cultures. The intra- and extra-cellular distribution of newly synthesized beta-hexosaminidase in both monensin-treated normal and I-cell fibroblasts were electrophoretically indistinguishable from the four bands characteristic of I-cell intracellular beta-hexosaminidase. The excreted enzyme from both cultures was found to be a low- or no-uptake form. This form of beta-hexosaminidase may have been excreted from a secondary route preceding the site of the monensin effect. The similar findings in monensin-treated normal and I-cell cultures suggest that the subcellular site of the biochemical defect in I-cell disease is at a location after the site of the monensin effect i.e. late in the Golgi region or at a post-Golgi-region location.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-103883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-1119807,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-1201084,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-13273400,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-377287,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-4249768,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-4345092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-4364008,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-438323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-481112,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-526296,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-597304,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-623792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-6244586,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-646806,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-656062,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-6989822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-7190150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-747663,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-786156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-880235,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-908752,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-922886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-925606,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7236240-942051
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Dec
|
pubmed:issn |
0264-6021
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
192
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
813-20
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7236240-Acetylglucosaminidase,
pubmed-meshheading:7236240-Biological Transport,
pubmed-meshheading:7236240-Cells, Cultured,
pubmed-meshheading:7236240-Extracellular Space,
pubmed-meshheading:7236240-Fibroblasts,
pubmed-meshheading:7236240-Furans,
pubmed-meshheading:7236240-Hexosaminidases,
pubmed-meshheading:7236240-Humans,
pubmed-meshheading:7236240-Mannosephosphates,
pubmed-meshheading:7236240-Monensin,
pubmed-meshheading:7236240-Mucolipidoses,
pubmed-meshheading:7236240-Subcellular Fractions
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pubmed:year |
1980
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pubmed:articleTitle |
The effect of monensin on beta-hexosaminidase transport in normal and I-cell fibroblasts.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|