We have determined the cDNA sequence of preprorelaxin in the pregnant one-h
umped camel by employing reverse transcription- and rapid amplification of
cDNA ends-polymerase chain reaction. Camel preprorelaxin consisted of 600 b
ase pairs (bp) encoding a protein of 199 amino acids (aa) with a signal pep
tide of 25 aa (75 bp), a B domain of 28 aa (84 bp), a C domain of 121 aa (3
66 bp), and an A domain of 24 aa (72 bp). The N terminus of the C domain of
camel prorelaxin contained the unique proline-rich repetitive sequence (-R
PAP)(3)-(-K/RPAL-)(2), and within the B domain the classical -GRELVR- recep
tor binding motif was found. Camel preprorelaxin showed highest homology wi
th porcine (74.6%) and equine (65.4%) relaxin. The ovary and the uteroplace
ntal unit were a dual source of relaxin in the pregnant dromedary. Within t
he ovary, weak expression of relaxin was detected in large luteal cells of
the mature corpus luteum. In the ovarian follicles, immunoreactive relaxin,
but not relaxin mRNA, was detected in the granulosa and theca interna cell
layer. Beginning at around Day 93 of gestation and coinciding with increas
ing interdigitation of the fetal villus with the underlying maternal endome
trium, uterine luminal epithelial cells in the uteroplacental tissue expres
sed relaxin. Weak expression of immunoreactive relaxin, but not relaxin mRN
A, was observed in villous trophoblast cells. Pseudostratified trophoblast
cells at the base of the placental villi and multinucleate giant cells did
not express relaxin.