Synthesis and glycosylation of the common alpha subunit of human glycoprotein hormones in mouse cells.

The synthesis and the post-translational modification of the alpha subunit of human glycoprotein hormones have been studied in a mouse cell. A full-length cDNA coding for the human alpha subunit has been expressed in mouse C127 cells under the control of mouse metallothionein regulatory sequences, u...

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Huvudupphovsmän: Ramabhadran, T V, Reitz, B A, Tiemeier, D C
Materialtyp: Artikel
Språk:en
Publicerad: 1984
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Research Article
Länkar:https://ncbi.nlm.nih.gov/pmc/articles/PMC391998/
https://ncbi.nlm.nih.gov/pubmed/6208554
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spelling pubmed-3919982004-04-23 Synthesis and glycosylation of the common alpha subunit of human glycoprotein hormones in mouse cells. Ramabhadran, T V Reitz, B A Tiemeier, D C Proc Natl Acad Sci U S A Research Article The synthesis and the post-translational modification of the alpha subunit of human glycoprotein hormones have been studied in a mouse cell. A full-length cDNA coding for the human alpha subunit has been expressed in mouse C127 cells under the control of mouse metallothionein regulatory sequences, using a bovine papilloma virus vector. Stable clones secreting the alpha subunit into the medium have been obtained. Two intracellular forms of 22,000 Da and 21,000 Da have been detected. Pulse-chase experiments suggest that the 22,000-Da form is exported, while the 21,000-Da form appears to remain intracellular. The secreted form of the alpha subunit migrates as a broad peak between 22,000 and 30,000 Da, suggesting further modification of the intracellular form prior to secretion. Both the secreted and the intracellular forms incorporate glucosamine label, indicating that at least a portion of the modification observed here is in the form of glycosylation. 1984-11 /pmc/articles/PMC391998/ /pubmed/6208554 Text en
institution US National Library of Medicine
collection PubMed Central
language en
format Article
topic Research Article
spellingShingle Research Article
Ramabhadran, T V
Reitz, B A
Tiemeier, D C
Synthesis and glycosylation of the common alpha subunit of human glycoprotein hormones in mouse cells.
description The synthesis and the post-translational modification of the alpha subunit of human glycoprotein hormones have been studied in a mouse cell. A full-length cDNA coding for the human alpha subunit has been expressed in mouse C127 cells under the control of mouse metallothionein regulatory sequences, using a bovine papilloma virus vector. Stable clones secreting the alpha subunit into the medium have been obtained. Two intracellular forms of 22,000 Da and 21,000 Da have been detected. Pulse-chase experiments suggest that the 22,000-Da form is exported, while the 21,000-Da form appears to remain intracellular. The secreted form of the alpha subunit migrates as a broad peak between 22,000 and 30,000 Da, suggesting further modification of the intracellular form prior to secretion. Both the secreted and the intracellular forms incorporate glucosamine label, indicating that at least a portion of the modification observed here is in the form of glycosylation.
author Ramabhadran, T V
Reitz, B A
Tiemeier, D C
author_facet Ramabhadran, T V
Reitz, B A
Tiemeier, D C
author_sort Ramabhadran, T V
title Synthesis and glycosylation of the common alpha subunit of human glycoprotein hormones in mouse cells.
title_short Synthesis and glycosylation of the common alpha subunit of human glycoprotein hormones in mouse cells.
title_full Synthesis and glycosylation of the common alpha subunit of human glycoprotein hormones in mouse cells.
title_fullStr Synthesis and glycosylation of the common alpha subunit of human glycoprotein hormones in mouse cells.
title_full_unstemmed Synthesis and glycosylation of the common alpha subunit of human glycoprotein hormones in mouse cells.
title_sort synthesis and glycosylation of the common alpha subunit of human glycoprotein hormones in mouse cells.
publishDate 1984
url https://ncbi.nlm.nih.gov/pmc/articles/PMC391998/
https://ncbi.nlm.nih.gov/pubmed/6208554
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