Relaxin 2000 pp 349-356 | Cite as
The Relaxin-Like Factor (Insulin 3) is highly expressed in the ruminant ovary: A putative ruminant relaxin?
Abstract
The relaxin-like factor (RLF, Ins13) was initially characterized as the leydig insulin like peptide (Ley-I-L)[1] as it was highly expressed in porcine Leydig cells. More recently however, the RLF gene has also been shown to be expressed in the human ovary and trophoblasts as well as the mouse ovary [Ivell et al., this volume]. This data, together with the similarity in structure of the derived protein sequence of RLF to relaxin, including a conserved, although shifted, relaxin-like receptor binding site (Fig. 1), led to the name relaxin-like factor [2]. The function of this new member of the relaxin/insulin family of peptides is discussed in detail in Ivell et al. (this volume).
Keywords
Thecal Cell Oestrous Cycle Bovine Corpus Luteum Relaxin Receptor Porcine RelaxinPreview
Unable to display preview. Download preview PDF.
References
- 1.Adham, I.M., Burkhardt, E., Benahmed, M. and Engel, W., J. Biol. Chem., 268 (1993) 26668.PubMedGoogle Scholar
- 2.Büllesbach, E. and Schwabe C., J. Biol. Chem., 270, (1995) 16011.PubMedCrossRefGoogle Scholar
- 3.Hartung, S., Kondo, S., Abend, N., Hunt, N., Rust, W., Balvers, M., Bryant-Greenwood, G. and Ivell R., In McLennan, A.H., Tregear, G. and Bryant-Greenwood, G.D. (eds.) Progress in Relaxin Research, World scientific Publishing, Singapore, 1995, p. 439Google Scholar
- 4.Musah, A.I., Schwabe, C. and Willham, R.L., Biol. Reprod., 34 (1986) 363.PubMedCrossRefGoogle Scholar
- 5.Musah, A.I., Schwabe, C. and Willham, R.L., Endocrinology, 118 (1986) 1476.PubMedCrossRefGoogle Scholar
- 6.Smith, D.E., Hixon, D.L., Moore, D.W., van Kirk, E.A., Alexander, B.M., Anthony, R.V. and Moss, G.E., Dom. Anim. Endo., 13 (1996) 469.CrossRefGoogle Scholar
- 7.Fields, M.J., Fields, P.A., Castro-Hernandez, A. and Larkin, L.H., Endocrinology, 869 (1980) 869.CrossRefGoogle Scholar
- 8.Wathes, D.C., Rees, J.M. and Porter, D.G., J. Reprod. Fertil., 84 (1988) 247.PubMedCrossRefGoogle Scholar
- 9.Roche, P.J., Crawford, R.J. and Tregear, G.W., Mol. Cell. Endocrinol., 91 (1993) 21.PubMedCrossRefGoogle Scholar
- 10.Bathgate, R., Moniac, N., Bartlick, B., Schumacher, M., Fields, M. and Ivell, R., Biol. Reprod., 61 (1999) 1090.Google Scholar
- 11.Roche, P.J., Butkus, E., Wintour, E.M. and Tregear, G., Mol. Cell. Endocrinol., 121 (1996) 171.PubMedCrossRefGoogle Scholar
- 12.Bathgate, R.A.D., Balvers, M., Hunt, N. and Ive11, R., Biol. Reprod., 55 (1996) 1452.Google Scholar
- 13.Sherwood O.D., In Knobil, E. and Neill, J.D. (eds), The Physiology of Reproduction 2nd ed., Raven Press, New York, USA, 1994, p. 861.Google Scholar
- 14.Dawson, N.F., Tan, Y.Y., Macris, M., Otvos Jr, L., Summers, R.J., Tregear, G.W. and Wade, J.D., J. Peptide Res., 53 (1999), 542.CrossRefGoogle Scholar
- 15.Büllesbach, E. and Schwabe C., Biochemistry, 38 (1999) 3073.PubMedCrossRefGoogle Scholar
- 16.Porter, D.G., Lye, S.J., Bradshaw, J.M. and Kendall, J.Z., J. Reprod. Fertil., 61 (1981) 409.PubMedCrossRefGoogle Scholar
- 17.Schramm, W., Einer-Jensen, N., Brown, M.B. and McCracken, J.A., Biol. Reprod., 30 (1984) 523.PubMedCrossRefGoogle Scholar
- 18.Maclennan, A.H., Grant, P. and Bryant-Greenwood, G., J. Reprod. Med., 40 (1995) 703.PubMedGoogle Scholar
- 19.Castro, J.M., Eddie, L.W. and Summers, R.J., Clin. Exp. Pharmacol. Physiol. Suppl., 21 (1992) 12.Google Scholar