Document Detail


Molecular cloning of pituitary glycoprotein alpha-subunit and follicle stimulating hormone and chorionic gonadotropin beta-subunits from New World squirrel monkey and owl monkey.
MedLine Citation:
PMID:  17897645     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The goal of this study was to characterize the gonadotropins expressed in pituitary glands of the New World squirrel monkey (Saimiri sp.) and owl monkey (Aotus sp.). The various subunits were amplified from total RNA from squirrel monkey and owl monkey pituitary glands by reverse transcription-polymerase chain reaction and the deduced amino acid sequences compared to those of other species. Mature squirrel monkey and owl monkey glycoprotein hormone alpha-polypeptides (96 amino acids in length) were determined to be 80% homologous to the human sequence. The sequences of mature beta subunits of follicle stimulating hormone (FSHbeta) from squirrel monkey and owl monkey (111 amino acids in length) are 92% homologous to human FSHbeta. New World primate glycoprotein hormone alpha-polypeptides and FSHbeta subunits showed conservation of all cysteine residues and consensus N-linked glycosylation sites. Attempts to amplify the beta-subunit of luteinizing hormone from squirrel monkey and owl monkey pituitary glands were unsuccessful. Rather, the beta-subunit of chorionic gonadotropin (CG) was amplified from pituitaries of both New World primates. Squirrel monkey and owl monkey CGbeta are 143 and 144 amino acids in length and 77% homologous with human CGbeta. The greatest divergence is in the C terminus, where all four sites for O-linked glycosylation in human CGbeta, responsible for delayed metabolic clearance, are predicted to be absent in New World primate CGbetas. It is likely that CG secreted from pituitary of New World primates exhibits a relatively short half-life compared to human CG.
Authors:
Jonathan G Scammell; Jane D Funkhouser; Felricia S Moyer; Susan V Gibson; Donna L Willis
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2007-08-24
Journal Detail:
Title:  General and comparative endocrinology     Volume:  155     ISSN:  0016-6480     ISO Abbreviation:  Gen. Comp. Endocrinol.     Publication Date:  2008 Feb 
Date Detail:
Created Date:  2008-02-11     Completed Date:  2008-05-01     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0370735     Medline TA:  Gen Comp Endocrinol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  534-41     Citation Subset:  IM    
Affiliation:
Department of Comparative Medicine, University of South Alabama, College of Medicine, Mobile, AL 36688, USA. jscammel@jaguar1.usouthal.edu
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Aotidae / genetics*
Chorionic Gonadotropin / genetics*
Cloning, Molecular
Female
Follicle Stimulating Hormone / genetics*
Glycoprotein Hormones, alpha Subunit / genetics*
Male
Molecular Sequence Data
Phylogeny
Protein Subunits / genetics
Saimiri / genetics*
Sequence Homology, Amino Acid
Grant Support
ID/Acronym/Agency:
13200//PHS HHS; R24 RR013200-09/RR/NCRR NIH HHS
Chemical
Reg. No./Substance:
0/Chorionic Gonadotropin; 0/Glycoprotein Hormones, alpha Subunit; 0/Protein Subunits; 9002-68-0/Follicle Stimulating Hormone
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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