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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
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pubmed:dateCreated |
1996-7-1
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pubmed:abstractText |
The gonadotropin/thyrotropin hormone family is characterized by a heterodimeric structure composed of a common alpha subunit noncovalently linked to a hormone-specific beta subunit. The conformation of the heterodimer is essential for controlling secretion, hormone-specific post-translational modifications, and signal transduction. Structure-function studies of follicle-stimulating hormone (FSH) and the other glycoprotein hormones are often hampered by mutagenesis-induced defects in subunit combination. Thus, the ability to overcome the limitation of subunit assembly would expand the range of structure-activity relationships that can be performed on these hormones. Here we converted the FSH heterodimer to a single chain by genetically fusing the carboxyl end of the FSH beta subunit to the amino end of the alpha subunit in the presence or absence of a linker sequence. In the absence of the CTP linker, the secretion rate was decreased over 3-fold. Unexpectedly, however, receptor binding/signal transduction was unaffected by the absence of the linker. These data show that the single-chain FSH was secreted efficiently and is biologically active and that the conformation determinants required for secretion and biologic activity are not the same.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Follicle Stimulating Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Follicle Stimulating Hormone, beta...,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoprotein Hormones, alpha Subunit,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10445-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8631838-Amino Acid Sequence,
pubmed-meshheading:8631838-Animals,
pubmed-meshheading:8631838-Base Sequence,
pubmed-meshheading:8631838-CHO Cells,
pubmed-meshheading:8631838-Cells, Cultured,
pubmed-meshheading:8631838-Cloning, Molecular,
pubmed-meshheading:8631838-Cricetinae,
pubmed-meshheading:8631838-DNA Primers,
pubmed-meshheading:8631838-Follicle Stimulating Hormone,
pubmed-meshheading:8631838-Follicle Stimulating Hormone, beta Subunit,
pubmed-meshheading:8631838-Glycoprotein Hormones, alpha Subunit,
pubmed-meshheading:8631838-Humans,
pubmed-meshheading:8631838-Molecular Sequence Data,
pubmed-meshheading:8631838-Recombinant Fusion Proteins
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pubmed:year |
1996
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pubmed:articleTitle |
Expression of biologically active fusion genes encoding the common alpha subunit and the follicle-stimulating hormone beta subunit. Role of a linker sequence.
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pubmed:affiliation |
Department of Molecular Biology & Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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