2002 Fiscal Year Final Research Report Summary
Splice variant Human LH receptor modulates the function of wild type Human LH receptor
Project/Area Number |
13671695
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Obstetrics and gynecology
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Research Institution | Gunma University |
Principal Investigator |
NAKAMURA Kazuto Medicine, Assistant Professor, 医学部, 講師 (60332558)
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Project Period (FY) |
2001 – 2002
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Keywords | LH receptor / dimerization |
Research Abstract |
We previously reported a splice variant form of human LH receptor [hLHR(Dexon 9)] that lacks exon 9 coding the N-terminal extracellular loop close to the first transmembrane domain. Several recent studies suggest G protein-coupled receptors (GPCRs) are able to form dimerization or oligomerization of receptor, which raises the possibility of an intermolecular interaction between hLHR(Dexon 9) and the wild-type LH receptor (hLHR). The aim of this study is to test whether hLHR could form the association with hLHR(Dexon 9), by a co-immunoprecipitation study. An interaction between hLHR(Dexon 9) with the immature band (68 kDa) of hLHR and not with the mature band (85 kDa) was seen. When hLHR and hLHR(Dexon 9) were co-expressed, the density of hLHR expression was significantly reduced as compared to hLHR expressed alone. The hCG-stimulated cAMP accumulation in cells expressing hLHR(Dexon 9) was also impaired, compared to cells expressing hLHR. A small decrease in the internalization index was observed in cells co-expressing both hLHR and hLHR(Dexon 9). In this study, we demonstrated human LH receptor is capable of forming receptor complexes. Our findings may expand the possibility that a splice variant of human LH receptor specifically modulates the functional property of the wild-type human LH receptor.
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Research Products
(4 results)