Linked Life Data

9364441

Source:http://linkedlifedata.com/resource/pubmed/id/9364441

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1998-1-27
pubmed:databankReference
pubmed:abstractText
Pituitary follitropin (FSH) has pleiotropic actions on gonads, but it is not certain if all these events are mediated by a single receptor. A single gene for the FSH receptor undergoes extensive alternate splicing generating multiple transcripts, and several of these have been cloned and characterized from the sheep testis. In this study we have investigated the expression in HEK (human embryonic kidney) 293 cells of a cloned cDNA encoding the first eight exons of the FSH receptor along with a carboxyterminal extension that contributed a hypothetical single transmembrane domain. This cDNA, which lacked the conventional seven transmembrane motif of the full-length 695 residue wild-type receptor protein, was also efficiently expressed on the cell surface and exhibited high affinity and specificity for FSH binding. LH did not compete for FSH binding indicating that these structures contained all the motifs necessary for specific hormone recognition. Following hormone binding and affinity crosslinking the deduced M(r) of the expressed receptor was compatible with dimer formation. The expression of these altered FSH receptors on the cell surface was confirmed by immunohistochemistry, which revealed punctate labeling in a pattern comparable to that shown by cells transfected by wild-type receptor cDNA. Addition of FSH stimulated 3H-thymidine incorporation in transfected cells in a biphasic manner. By performing RT-PCR we could show that similar altered receptor transcripts were present in both the ovary and testis. Our results reveal for the first time that the seven transmembrane structure of FSH-receptor is not absolutely necessary for cell surface expression and hormone binding provided other compensating motifs are present in the protein structure for membrane insertion. Some of these features are typical of growth factor receptors. Our investigations also demonstrate that alternate splicing of the FSH receptor gene provides a mechanism for creating receptor diversity and suggest that multiple receptors could be involved in regulation of hormone action.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1040-452X
pubmed:author
pubmed:issnType
Print
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
471-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9364441-Alternative Splicing, pubmed-meshheading:9364441-Amino Acid Sequence, pubmed-meshheading:9364441-Animals, pubmed-meshheading:9364441-Base Sequence, pubmed-meshheading:9364441-Cell Line, pubmed-meshheading:9364441-DNA Primers, pubmed-meshheading:9364441-Female, pubmed-meshheading:9364441-Follicle Stimulating Hormone, pubmed-meshheading:9364441-GTP-Binding Proteins, pubmed-meshheading:9364441-Humans, pubmed-meshheading:9364441-Immunohistochemistry, pubmed-meshheading:9364441-Male, pubmed-meshheading:9364441-Molecular Sequence Data, pubmed-meshheading:9364441-Ovary, pubmed-meshheading:9364441-RNA, Messenger, pubmed-meshheading:9364441-Receptors, FSH, pubmed-meshheading:9364441-Receptors, Growth Factor, pubmed-meshheading:9364441-Sheep, pubmed-meshheading:9364441-Testis
pubmed:year
1997
pubmed:articleTitle
Alternative splicing converts the G-protein coupled follitropin receptor gene into a growth factor type I receptor: implications for pleiotropic actions of the hormone.
pubmed:affiliation
Molecular Reproduction Research Laboratory, Clinical Research Institute of Montreal, Quebec, Canada. sairamm@IRCM.UMontreal.CA
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't