Source:http://linkedlifedata.com/resource/pubmed/id/15226594
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
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| pubmed:dateCreated |
2004-6-30
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| pubmed:abstractText |
Equine chorionic gonadotropin (eCG), which consists of highly glycosylated alpha- and beta-subunits, is a unique member of the gonadotropin family because it elicits response characteristics of both follicle-stimulating hormone (FSH) and luteinizing hormone (LH) in species other than the horse. In this study, recombinant tethered-eCG as well as its deglycosylated mutants were produced to determine if alpha- and beta- subunits can be synthesized as a single polypeptide chain (tethered-eCG) and display biological activity. We found that tethered-eCG (T- betaalpha) had both LH- and FSH-like activities comparable to dimeric eCG. Luteinizing hormone-like activity of tethered-eCGs deglycosylated at Asn(56) (T-betaalpha56) was decreased. In contrast, LH-like activity of eCG without O-glycosylated carboxyl-terminal peptide (CTP) (T-betacalpha) was slightly decreased but still similar to T-betaalpha. Double mutation at Asn(56) and CTP (T-betacalpha56) caused marked decrease in the activity, indicating that both glycosylations at Asn(56) and CTP are involved in LH-like activity in the tethered form. Interestingly, FSH-like activity remained in all deglycosylated eCG mutants (T-betaalpha56, T-betacalpha and T-betacalpha56) as well as T-betaalpha. The biological roles of oligosaccharides at Asn(56) of eCG alpha-subunit and O-linked peptide of beta-subunit appear to be different in LH- and FSH-like activities in tethered-eCG.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Asparagine,
http://linkedlifedata.com/resource/pubmed/chemical/Chorionic Gonadotropin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Follicle Stimulating Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/Luteinizing Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jun
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| pubmed:issn |
0916-8818
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
50
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
297-304
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:15226594-Animals,
pubmed-meshheading:15226594-Asparagine,
pubmed-meshheading:15226594-Biological Assay,
pubmed-meshheading:15226594-CHO Cells,
pubmed-meshheading:15226594-Chorionic Gonadotropin,
pubmed-meshheading:15226594-Cricetinae,
pubmed-meshheading:15226594-DNA,
pubmed-meshheading:15226594-Dose-Response Relationship, Drug,
pubmed-meshheading:15226594-Follicle Stimulating Hormone,
pubmed-meshheading:15226594-Genetic Vectors,
pubmed-meshheading:15226594-Glycosylation,
pubmed-meshheading:15226594-Hormones,
pubmed-meshheading:15226594-Horses,
pubmed-meshheading:15226594-Luteinizing Hormone,
pubmed-meshheading:15226594-Models, Genetic,
pubmed-meshheading:15226594-Mutation,
pubmed-meshheading:15226594-Oligosaccharides,
pubmed-meshheading:15226594-Peptides,
pubmed-meshheading:15226594-Recombinant Proteins,
pubmed-meshheading:15226594-Transfection
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| pubmed:year |
2004
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| pubmed:articleTitle |
Biological activities of tethered equine chorionic gonadotropin (eCG) and its deglycosylated mutants.
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| pubmed:affiliation |
Laboratory of Cellular Biochemistry, Animal Resource Sciences /Veterinary Medical Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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