Luteinizing hormone/chorionic gonadotropin bioactivity in the common marmoset (Callithrix jacchus) is due to a chorionic gonadotropin molecule with a structure intermediate between human chorionic gonadotropin and human luteinizing hormone.

Simple item page
dc.contributor.authorSimula, A.
dc.contributor.authorAmato, F.
dc.contributor.authorFaast, R.
dc.contributor.authorLopata, A.
dc.contributor.authorBerka, J.
dc.contributor.authorNorman, R.
dc.date.issued1995
dc.description.abstractChorionic gonadotropin (CG), a pregnancy-specific heterodimeric hormone found in primates, is responsible for CL rescue with pregnancy maintenance. Of the primates, the human and baboon gene sequences are the only structures so far determined. In order to study the structure and function of CG in other primates, we have isolated and sequenced the coding regions for the two subunits of marmoset CG (mCG) by the reverse transcription/polymerase chain reaction method. Study of multiple clones confirmed a high degree of homology with the human sequences (88% and 80% for the alpha and beta nucleotide sequences, respectively). Marmoset CG alpha has an extra four amino acids compared to hCG alpha, whereas the mCG beta sequence has a 3-bp deletion that maintains the reading frame and C-terminal amino acid sequence. Most of the differences between hCG beta and mCG beta peptides occur in the C-terminal region, which includes the loss of two of the O-linked glycosylation consensus sequences and the presence of an N-linked glycosylation consensus sequence. When mCG alpha and beta were co-expressed in CHO cells, assembly of biologically active hormone was confirmed by induced steroid secretion by MA10 cells. Partially purified mCG beta was used to raise anti-mCG antibodies. To date, an antibody has been obtained that is capable of detecting recombinant mCG beta, recombinant mCG dimer, and mCG dimer secreted by cultured marmoset trophoblast. Marmoset CG alpha and beta were also detectable at the transcriptional level in cultured trophoblast by in situ hybridization. This suggests that the LH/CG bioactivity reported from marmoset placentae and embryos is due to a molecule with structural features common to hLH (glycosylation pattern) and hCG (CG beta C-terminal structure).
dc.description.statementofresponsibilityAnthony P. Simula, Fred Amato, Renate Faast, Alexander Lopata, Jennifer Berka, and Robert J. Norman
dc.identifier.citationBiology of Reproduction, 1995; 53(2):380-389
dc.identifier.doi10.1095/biolreprod53.2.380
dc.identifier.issn0006-3363
dc.identifier.issn1529-7268
dc.identifier.orcidNorman, R. [0000-0002-3118-3896]
dc.identifier.urihttp://hdl.handle.net/2440/8027
dc.language.isoen
dc.publisherSociety for the Study of Reproduction
dc.source.urihttp://www.biolreprod.org/content/53/2/380.abstract
dc.subjectCells, Cultured
dc.subjectCHO Cells
dc.subjectTrophoblasts
dc.subjectAnimals
dc.subjectCallithrix
dc.subjectHumans
dc.subjectMacromolecular Substances
dc.subjectChorionic Gonadotropin
dc.subjectLuteinizing Hormone
dc.subjectRNA-Directed DNA Polymerase
dc.subjectTransfection
dc.subjectPolymerase Chain Reaction
dc.subjectSequence Alignment
dc.subjectGene Expression
dc.subjectAmino Acid Sequence
dc.subjectBase Sequence
dc.subjectStructure-Activity Relationship
dc.subjectGlycosylation
dc.subjectPregnancy
dc.subjectMolecular Sequence Data
dc.subjectFemale
dc.subjectCricetinae
dc.titleLuteinizing hormone/chorionic gonadotropin bioactivity in the common marmoset (Callithrix jacchus) is due to a chorionic gonadotropin molecule with a structure intermediate between human chorionic gonadotropin and human luteinizing hormone.
dc.typeJournal article
pubs.publication-statusPublished

Files

Collections

Obstetrics and Gynaecology publications