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Truncated equine LH beta and asparagine(56)-deglycosylated equine LH alpha combine to produce a potent FSH antagonist

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dc.contributor.author Butnev, Vladimir Y. en_US
dc.contributor.author Singh, V. en_US
dc.contributor.author Nguyen, Van T. en_US
dc.contributor.author Bousfield, George R. en_US
dc.date.accessioned 2012-01-24T17:48:25Z
dc.date.available 2012-01-24T17:48:25Z
dc.date.issued 2002-03 en_US
dc.identifier 11874703 en_US
dc.identifier AG15428/ DK52383 en_US
dc.identifier 0375363 en_US
dc.identifier JOE04323 en_US
dc.identifier.citation The Journal of endocrinology. 2002 Mar; 172(3): 545-55. en_US
dc.identifier.issn 0022-0795 en_US
dc.identifier.uri http://dx.doi.org/10.1677/joe.0.1720545
dc.identifier.uri http://hdl.handle.net/10057/4123
dc.description Click on the DOI link below to access the article (may not be free). en_US
dc.description.abstract Hybrid hormone preparations were prepared by combining intact and Asn(56)-deglycosylated (N(56)dg) equine (e) LH or FSH alpha subunit preparations with truncated, des(121-149)eLH beta (eLH beta t), immunopurified, intact eLH beta or equine chorionic gonadotropin beta (eCG beta) preparations, and eFSH beta. The LH receptor-binding potencies of N(56)dg-eLH alpha:eLH beta t and N(56)dg-eFSH alpha:eLH beta t hybrids were equivalent to that of eLH; however, both N(56)dg-alpha preparations were only 3-4% as active as eLH in the rat testis Leydig cell bioassay. In the granulosa cell FSH bioassay, eLH alpha:eLH beta t stimulated progesterone synthesis and induced aromatase activity, while N(56)dg-eLH alpha:eLH beta t was completely inactive at doses up to 5 microg. N(56)dg-eLH alpha:eLH beta t inhibited progesterone production and aromatase induction elicited by 0.3 ng eFSH or 2 ng human (h) FSH. The inhibitory activities of N(56)dg-eLH alpha:eLH beta and N(56)dg-eCG alpha:eLH beta t were only 10% that of N(56)dg-eLH alpha:eLH beta t. N(56)dg-eLH alpha:eCG beta did not inhibit progesterone synthesis stimulated by eFSH at all and appeared to further stimulate aromatase induction at the highest dose tested. Preincubation of N(56)dg-eLH alpha:eLH beta and N(56)dg-eLH alpha:eLH beta t for 72 h at 37 C resulted in no loss of FSH receptor-binding activity. Preincubation resulted in 50% loss of receptor-binding activity by the eFSH preparation due to subunit dissociation, while 88% of N(56)dg-eLH alpha:eFSH beta activity was lost following 72 h, 37 C preincubation. While alpha Asn(56) oligosaccharide had no effect on eLH beta hybrid stability, it did contribute to the stability of the eFSH heterodimer. en_US
dc.description.sponsorship NIA NIH HHS/ NIDDK NIH HHS en_US
dc.language.iso eng en_US
dc.publisher BioScientifica Ltd. en_US
dc.relation.ispartofseries The Journal of endocrinology en_US
dc.source NLM en_US
dc.subject Research Support, U.S. Gov't, Non-P.H.S. en_US
dc.subject Research Support, U.S. Gov't, P.H.S. en_US
dc.subject.mesh Animals en_US
dc.subject.mesh Dimerization en_US
dc.subject.mesh Dose-Response Relationship, Drug en_US
dc.subject.mesh Female en_US
dc.subject.mesh Follicle Stimulating Hormone/antagonists & inhibitors en_US
dc.subject.mesh Glycoprotein Hormones, alpha Subunit/metabolism en_US
dc.subject.mesh Granulosa Cells/drug effects en_US
dc.subject.mesh Horses en_US
dc.subject.mesh Luteinizing Hormone/chemistry en_US
dc.subject.mesh Radioligand Assay/methods en_US
dc.subject.mesh Rats en_US
dc.subject.mesh Recombinant Proteins/metabolism en_US
dc.subject.mesh Glycoprotein Hormones, alpha Subunit/metabolism en_US
dc.subject.mesh Granulosa Cells/metabolism en_US
dc.subject.mesh Luteinizing Hormone/metabolism* en_US
dc.title Truncated equine LH beta and asparagine(56)-deglycosylated equine LH alpha combine to produce a potent FSH antagonist en_US
dc.type Article en_US
dc.description.version peer reviewed en_US
dc.rights.holder Copyright @ 2002 Society for Endocrinology en_US

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