The primary structure of bovine prolactin

Wallis, Michael

doi:10.1016/0014-5793(74)80726-x

Cited by 43 publications

(13 citation statements)

References 11 publications

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“…4C) 3. Alignment of the partial amino acid sequences (represented by standard single-letter abbreviations) of the 20-kDa and the PRLs from tilapia with the corresponding NH2 termini of PRLs from chum salmon (22), human (23), whale (24); pig (25), cow (26), sheep (25), rat (27), and mouse (28). Identical residues among the teleost PRLs are boxed with a broken line.…”

Section: Resultsmentioning

confidence: 99%

Isolation and partial characterization of a pair of prolactins released in vitro by the pituitary of a cichlid fish, Oreochromis mossambicus.

Specker¹,

King²,

Nishioka³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

110

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The pituitary of the cichlid fish tilapia secretes two prolactins (PRLs) of molecular masses 20 kDa and 24 kDa. The 20-kDa PRL has an isoelectric point in the range of those of mammalian PRLs (pI 6.7), but the 24-kDa PRL is unusually basic (pI 8.7). Partial sequence information indicates that the PRLs are homologous but distinct proteins, differing by five amino acids within the first 29 NH2-terminal residues. Homology in the known region is higher with chum salmon PRL than with known mammalian PRLs. Reversed-phase HPLC permits isolation of these two PRLs and a single tilapia growth hormone from culture medium or from the pituitary in a single step. HPLC and radio-HPLC analysis of [3H]leucine pulse-chase experiments reveal that each PRL is secreted in vitro at remarkably high rates (21 pmol per gland per hr) and that the two PRLs are released in approximately equimolar amounts, suggesting the coordinate regulation of the secretion. Both PRLs exert characteristic PRL activity in that they prevent the loss of Na' from the plasma of hypophysectomized tilapia in fresh water.In teleost fishes, pituitary prolactin (PRL) production is confined to the rostral pars distalis (RPD). The RPD of the cichlid fish tilapia (Oreochromis mossambicus) consists almost entirely of PRL-secreting cells and accounts for almost one-third of the entire pituitary (1, 2). This regionalization of PRL cells differs from the scattered distribution of PRL cells in the pituitaries ofother vertebrates and has made the teleost pituitary a useful model for the study of PRL cell function.The aim of the investigations reported here was to make use of this organizational simplicity in order to isolate and characterize both stored and secreted PRL from the tilapia pituitary. This research direction was taken following reports that mammalian PRL might be modified during release (3-6) and because we thought that such modification might explain why tilapia PRL isolated previously exhibited anomalous electrophoretic behavior (7-9), even though its immunological and biological characteristics were similar to those of other vertebrate PRLs (10, 11).Our approach has been to culture the PRL-producing lobes and to isolate secreted proteins from the culture medium using reversed-phase HPLC.

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Section: Resultsmentioning

confidence: 99%

Isolation and partial characterization of a pair of prolactins released in vitro by the pituitary of a cichlid fish, Oreochromis mossambicus.

Specker¹,

King²,

Nishioka³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

110

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“…1. The sequence of bovine prolactin is from Wallis (1974) and Yudaev et al (1975). The sequence of ovine prolactin is from Li et al (1970) and Li (1976), and that of pig prolactin is from Li (1976).…”

Section: Evolutionary Tree For the Growth Hormones Andmentioning

confidence: 97%

The molecular evolution of pituitary growth hormone prolactin and placental lactogen: A protein family showing variable rates of evolution

Wallis

1981

J Mol Evol

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Summary. Pituitary growth hormone and prolactin, together with the homologous placental hormones, comprise a family of related protein hormones. Complete or partial amino acid sequences of seven mammalian growth hormones, six mammalian prolactins and one placental lactogen are available, and have been compared. A phylogenetic tree has been constructed which describes the relationships within the family. At least two gene duplications have occurred during the evolution of these proteins. Rates of evolution in the family have been quite variable, the overall rate of evolution having been apparently fairly slow, but having increased markedly on several occasions, most notably in the evolution of human (and, on the basis of immunological relationships, probably other primate) growth hormones and rat (and possibly other rodent) prolactins.

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“…In most mammalian species, the hormone consists of 197-199 amino acids (SINHA, 1995). Bovine PRL consists 199 amino acids (WALLIS, 1974). Prolactin is essential for the initiation and maintenance of lactation.…”

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confidence: 99%

Association of genetic variants of bovine <i>prolactin</i> with milk production traits of Black-and-White and Jersey cattle

et al. 2005

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Associations between polymorphism localised in the third exon of the prolactin gene (PRL-RsaI) and milk production traits of Black-and-White and Jersey cattle were analysed. A total of 427 cows were included in the study. PCR-RFLP method was used. The frequencies of genotypes and alleles were as follows: 0.7107 -AA, 0.2851 -AB, 0.0042 -BB; 0.8533 -PRL A and 0.1467 -PRL B for Black-and-White cattle and 0.0919 -AA, 0.4324 -AB, 0.4757 -BB; 0.3081 -PRL A and 0.6919 -PRL B for Jersey cattle. Statistically significant differences between the breeds were observed in the frequencies of genotypes and alleles. Associations between PRL-RsaI polymorphism and milk production traits of Jersey cows and lack of associations with these traits in Black-andWhite cows were observed.

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The primary structure of bovine prolactin

Cited by 43 publications

References 11 publications

Isolation and partial characterization of a pair of prolactins released in vitro by the pituitary of a cichlid fish, Oreochromis mossambicus.

Isolation and partial characterization of a pair of prolactins released in vitro by the pituitary of a cichlid fish, Oreochromis mossambicus.

The molecular evolution of pituitary growth hormone prolactin and placental lactogen: A protein family showing variable rates of evolution

Association of genetic variants of bovine <i>prolactin</i> with milk production traits of Black-and-White and Jersey cattle

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The primary structure of bovine prolactin

Cited by 43 publications

References 11 publications

Isolation and partial characterization of a pair of prolactins released in vitro by the pituitary of a cichlid fish, Oreochromis mossambicus.

Isolation and partial characterization of a pair of prolactins released in vitro by the pituitary of a cichlid fish, Oreochromis mossambicus.

The molecular evolution of pituitary growth hormone prolactin and placental lactogen: A protein family showing variable rates of evolution

Association of genetic variants of bovine &lt;i&gt;prolactin&lt;/i&gt; with milk production traits of Black-and-White and Jersey cattle

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Association of genetic variants of bovine <i>prolactin</i> with milk production traits of Black-and-White and Jersey cattle