The purification and characterization of rabbit placental lactogen

Bolander, Franklyn F.; Fellows, Robert E.

doi:10.1042/bj1590775

Cited by 25 publications

(19 citation statements)

References 29 publications

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“…A dissociation between binding and active sites has been established for corticotropin (31). Although the subprimate placental lactogens appear to bind preferentially to the prolactin receptor, there is also some cross-binding to specific growth hormone receptors (13,29). Thus, the biological effects of these hormones may reside in a balance between the activation of the two receptors, much in the same manner as the differential effects of sympathomimetic drugs depend upon their relative potencies at a and , adrenergic receptors (32).…”

Section: Discussionmentioning

confidence: 97%

“…(29). Similarly, the ability of bPL to displace 125I-labeled bGH is only 50% of its ability to displace 125I-labeled bPR in their respective target organs (13). It is of interest that several hormones (oPL, hPL, and bPR) apparently bind to the same receptor but exert different biological activities.…”

Section: Discussionmentioning

confidence: 99%

“…The first two hormones were further purified on a column of Sephadex G-150 as described (12). The preparation of bovine and ovine placental lactogens has been reported elsewhere, (13,14).…”

Section: Materlals and Methodsmentioning

confidence: 99%

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Localization and specificity of binding of subprimate placental lactogen in rabbit tissues.

Bolander¹,

Hurley²,

Handwerger³

et al. 1976

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

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A search for specific placental lactogen binding was undertaken in tissues obtained from late pregnant rabbits using the placental lactogens from sheep, cows, and human beings. 125I-labeled ovine lactogen exhibited highest specific binding to the adrenal gland (57.8%), followed by liver (21.5%), ovary (19.9%), mammary gland (15.9%), uterus (12.2%), kidney (8.8%), brain (8.5%), and adipose tissue (7.9%). In liver and mammary gland, the displacement curves for ovine and human lactogen were identical to that for bovine prolactin, indicating that they share the same receptor site. Although the displacement curve for bovine lactogen was parallel to that of the other lactogens the bovine hormone is less active in the radioreceptor assay.

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

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Localization and specificity of binding of subprimate placental lactogen in rabbit tissues.

Bolander¹,

Hurley²,

Handwerger³

et al. 1976

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

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“…(Endocrine Journal 41: 387-397, 1994) THE PLACENTA produces a PRL-or GH-like hormone known as placental lactogen (PL), which is found in several mammals, including the rat [1], mouse [2], cow [3], sheep [4], monkey [5], and human [6]. In the rat, the PL family shows structural homology with PRL.…”

Section: Glycosylationmentioning

confidence: 99%

A cDNA Encoding a New Member of the Rat Placental Lactogen Family, PL-I mosaic (PL-Im).

et al. 1994

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Abstract. We have isolated a cDNA encoding a novel placental lactogen (PL), PL-I mosaic (PL-Im), by screening the cDNA library in ,ZAP of the mid-pregnant (day 12) rat placenta. The cDNA comprised an open reading frame of 687 by encoding 229 amino acids, in which there were two putative Nglycosylation sites. Northern blot analysis showed that PL-Im mRNA was expressed specifically during mid-pregnancy (days 10 and 12) in the rat placenta. The cDNA was highly homologous with those of other rat PL family members; in particular, the homology among PL-Im, PL-I (mid-pregnancy-specific) and PL-Iv (late-pregnancy-specific) was over 90%. Interestingly, the nucleotide sequence of PL-Im cDNA was a mosaic of PL-I and PL-Iv and it did not possess its own particular sequence. As the genomic pattern determined using Southern blot analysis of PL-Im was distinct from that of PL-I and PLIv, the encoded area of PL-Im appears to be independent of those of PL-I and PL-Iv on the gene. In the dendrogram of the rat PL family constructed on the basis of the nucleotide sequence homologies, PL-Im was located between PL-Iv and PL-I in the process of molecular evolution. Therefore, PL-Im has a unique cDNA structure and may be a principal factor in the molecular evolution of PLs.

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“…Some of these hormones possess another biological activity : for example, hGH also has a lactogenic activity. Some placental hormones have either only a lactogenic activity, such as human (hPL), rat (rPL) and mouse (mPL) placental lactogen (Friesen, 1965; Robertson and Friesen, 1975;Tala-mantes, 1975), or both growth and lactogenic activities, such as bovine (Forsyth, 1973;Bolander and Fellows, 1976;Kelly et al, 1976), caprine (Becka et aL, 1977;Currie et al, 1977), ovine (Handwerger e t al., 1974;Chan et al, 1976;Martal and Djiane, 1976;Martal, 1978), simian (Shome and Friesen, 1971) and guineapig (Talamantes, 1975, Kelly ei al., 1976) chorionic somatomammotropins (CS).…”

Section: Introductionmentioning

confidence: 99%