Expression of human relaxin genes: characterization of a novel alternatively-spliced human relaxin mRNA species.

Bibliographic Collection: 
MOCA Reference, APE
Publication Type: Journal Article
Authors: Gunnersen, J M; Fu, P; Roche, P J; Tregear, G W
Year of Publication: 1996
Journal: Mol Cell Endocrinol
Volume: 118
Issue: 1-2
Pagination: 85-94
Date Published: 04/1996
Publication Language: eng
ISSN: 0303-7207
Keywords: Alternative Splicing, Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, Decidua, DNA, Female, Gene Expression, Humans, Male, Molecular Sequence Data, Ovary, Pan troglodytes, Placenta, Polymerase Chain Reaction, Prostate, Relaxin, RNA, Messenger, Sequence Homology, Nucleic Acid

Relaxin is a two-chain peptide hormone encoded by two non-allelic genes in humans and great apes, and by a single gene in all other species studied. We have characterized the expression of the human relaxin genes (H1 and H2) in placenta, decidua, prostate and ovary by reverse-transcription/polymerase chain reaction (RT/PCR). H2 relaxin mRNA was detected in the ovary, term placenta, decidua, and prostate gland. In contrast, H1 gene expression was detected only in the prostate gland. In addition to the relaxin PCR product of the predicted size (486 bp), a larger relaxin-specific product (587 bp) was detected in both H1 and H2 amplifications and in amplifications of chimpanzee relaxin from placenta and corpus luteum. Sequencing of human and chimpanzee PCR products, and human relaxin genomic clones, revealed that the larger product arises from an alternatively-spliced relaxin mRNA species incorporating an extra exon. This is the first evidence that the structure of the human and chimpanzee relaxin genes differ from that of other characterized relaxin genes, such as pig and rat. The novel peptide arising from this alternate message would be identical to prorelaxin in the B-chain and part of the C-peptide (extending to the position of the intron) but would differ from prorelaxin in the carboxy-terminal domain. Observation of a similar mRNA species in the chimpanzee suggests that this conserved relaxin-like peptide may have a significant biological role.

Alternate Journal: Mol. Cell. Endocrinol.
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