1983
DOI: 10.1016/0016-6480(83)90079-5
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Comparative measurement of the lactogenic activity of ovine placental lactogen in rabbit and ewe mammary gland

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Cited by 31 publications
(17 citation statements)
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“…5) when compared with E 2 +P 4 +HC-treated ewes. This confirmed previous reports that oPL stimulated accumulation of -casein mRNA in mammary explants from pregnant ewes, although oPL was considerably less potent than oPRL (Servely et al 1983), and these results are comparable to lactogenic effects of bPL in the heifer with artificially induced lactation (Byatt et al 1994).…”
Section: Figuresupporting
confidence: 91%
See 1 more Smart Citation
“…5) when compared with E 2 +P 4 +HC-treated ewes. This confirmed previous reports that oPL stimulated accumulation of -casein mRNA in mammary explants from pregnant ewes, although oPL was considerably less potent than oPRL (Servely et al 1983), and these results are comparable to lactogenic effects of bPL in the heifer with artificially induced lactation (Byatt et al 1994).…”
Section: Figuresupporting
confidence: 91%
“…It has been purified and characterised by several groups (Martal & Djiane 1975, Chan et al 1976, Hurley et al 1977, Reddy & Watkins 1978, Warren et al 1990, Kappes et al 1992) over the past 20 years, but the physiological role of oPL in ovine physiology remains speculative. Recent results from in vitro binding studies and in vivo studies of biological activities on ovine adult or foetal tissues suggest a role(s) in foetal growth and/or mammogenesis (Chan et al 1978a, Servely et al 1983, Freemark & Handwerger 1986, Freemark & Comer 1989, Byatt et al 1992, Anthony et al 1995. Both the cDNA sequence (Colosi et al 1989) and predicted amino acid sequence indicate that oPL has partial homology with both ovine PRL (oPRL) (49%) and ovine GH (oGH) (25%) and oPL binds to oGH receptors (oGH-R) or oPRL receptors (oPRL-R).…”
Section: Introductionmentioning
confidence: 99%
“…It is produced by binucleate cells of the fetal trophoblast and was first purified by Handwerger et al (1974) and Martal & Djiane (1975). Ovine chorionic somatomammotrophin shares significant structural homology with both ovine prolactin (oPRL -49%) and growth hormone (oGH -28%) and can serve as a bifunctional hormone by binding to GH or PRL receptors (Chan et al 1978a, Servely et al 1983, Colosi et al 1989, Warren et al 1990). Production of oCS was first detected in the ovine trophoblast as early as day 16 (d16) of gestation (Martal & Djiane 1977).…”
Section: Introductionmentioning
confidence: 99%
“…It has been shown that oCS also stimulates the protein synthesis of rabbit mammary gland in organotypic culture, inducing the synthesis of lactose and /3-casein and enhancing j3-casein m-RNA (Servely et al, 1983).…”
Section: Introductionmentioning
confidence: 99%