Prolactin Synthesis by Human Chorion-Decidual Tissue: a Possible Source of Prolactin in the Amniotic Fluid

Golander, Avraham; Hurley, Thomas W.; Barrett, Janet R; Hizi, Amnon; Handwerger, Stuart

doi:10.1126/science.694535

Cited by 220 publications

(60 citation statements)

References 15 publications

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Section: Discussionmentioning

confidence: 99%

“…The level of PRL is apparently much higher in the blood and amniotic fluid during pregnancy (Golander et al 1978, Daly et al 1983. After conception, a continuous increase in PRL production in the decidual cells leads to an accumulation of PRL in the amniotic fluid up to 2-3 mg/ml (Golander et al 1978, Daly et al 1983. Concomitantly, the PRL receptor expression and its mRNA are up-regulated toward the secretory phase of the menstrual cycle , Jones et al 1998) and maintained throughout pregnancy (Maaskant et al 1996).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Regulation of electrolyte transport across cultured endometrial epithelial cells by prolactin

Deachapunya

Poonyachoti²,

Krishnamra³

2008

Journal of Endocrinology

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The effect of prolactin (PRL) on ion transport across the porcine glandular endometrial epithelial cells was studied in primary cell culture using the short-circuit current technique. Addition of 1 mg/ml PRL either to the apical solution or to the basolateral solution produced a peak followed by a sustained increase in Isc, but with a lesser response when PRL was added apically. Basolateral addition of PRL increased the Isc in a concentrationdependent manner with a maximum effect at 1 mg/ml and an effective concentration value of 120 ng/ml. The PRLstimulated Isc was significantly reduced by pretreatment with an apical addition of 5-nitro-2-(3-phenylpropylamino) benzoic acid (200 mM), diphenylamine-2-carboxylic acid (1 mM) or 4,4 0 -diisothiocyanatostilbene-2,2 0 -disulfonic acid (200 mM), Cl K channel blockers, but not by amiloride (10 mM), a Na C channel blocker. In addition, pretreatment with bumetanideK cotransporter inhibitor, in the basolateral solution significantly reduced the PRL-stimulated Isc. Replacement of Cl K or HCO K 3 in the bathing solutions also decreased the Isc response to PRL. Pretreatment of the monolayer with AG490 (50 mM), an inhibitor of JAK2 activity significantly inhibited the PRL-induced increase in Isc. Western blot analysis of the porcine endometrial epithelial cells revealed the presence of short isoform of PRL receptor (PRLR-S) that could be regulated by 17b-estradiol. The results of this investigation showed that PRL acutely stimulated anion secretion across the porcine endometrial epithelial cells possibly through PRLR-S present in both apical and basolateral membranes. The PRL response appeared to be mediated by the JAK2-dependent pathway.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Regulation of electrolyte transport across cultured endometrial epithelial cells by prolactin

Deachapunya

Poonyachoti²,

Krishnamra³

2008

Journal of Endocrinology

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“…A variety of mammalian cells have receptors for prolactin, including those of the mammary gland, liver, kidney, brain, prostate, testis, and ovary (41). Although prolactin is a pituitary hormone, proteins that react with anti-prolactin sera appear to be synthesized in nonpituitary tissues as well (42,43). Arguing by analogy to prolactin, we hypothesize that proliferin is secreted by certain types of proliferating cells, binds to cell surface receptors of like or different cells, and stimulates their growth or differentiation.…”

Section: Methodsmentioning

confidence: 99%

Nucleotide sequence of a growth-related mRNA encoding a member of the prolactin-growth hormone family.

Linzer¹,

Nathans²

1984

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

166

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As part of the proliferative response to serum, mouse 3T3 cells produce a set of growth-related mRNAs identified by hybridization to cloned cDNAs. One of these mRNAs, which is about 1 kilobase long, appears within a few hours after stimulation of resting cells with serum or plateletderived growth factor and reaches a high level during the transition from the GI to the S phase of growth. This mRNA is translated in vitro into a protein of approximately 25 kilodaltons. The corresponding cloned cDNA of 791 base pairs has been sequenced; it contains a single open reading frame that encodes a protein of 224 amino acids with extensive sequence homology to mammalian prolactins. The initial 29-amino acid segment of the encoded protein resembles the signal sequences of prehormones. That the growth-related protein is not mouse prolactin is indicated by comparison of its predicted amino acid composition with that of mouse prolactin and by the distinct fragment patterns seen when restricted mouse DNA is probed with the cloned cDNA or rat prolactin cDNA. Therefore, the growth-related protein appears to be a new member of the prolactin-growth hormone family. Because of its relationship to prolactin and growth hormone and its association with cell proliferation, the protein has been called "proliferin."Activation of specific genes occurs during the transition of mammalian cells from the resting to the growing state (1). What these genes are and what roles the products of these genes play in the progression of the cell cycle remain, for the most part, to be elucidated. Recently, several groups of workers have reported the molecular cloning of cDNAs corresponding to growth-related mRNAs from cultured mouse cells stimulated with serum or purified growth factors (2-4). One of the growth-related mRNAs that we found in a number of proliferating murine cell lines is a 1-kilobase RNA (referred to as 28H6) that is virtually undetectable in nongrowing cells (2, 5). Following serum stimulation of BALB/c 3T3 fibroblastic cells, 28H6 RNA appears within 3 hr and reaches a maximal level at the time of transition between the G1 and S phases of growth. Because 28H6 RNA is not always found in proliferating murine cell lines (2, 5), its expression is not essential for growth. However, our interest in this RNA was reinforced when nucleotide sequence analysis of an incomplete cDNA clone suggested that 28H6 RNA encoded a protein related to prolactin (2,5). We now report the sequence of a cDNA clone that appears to contain the complete coding and 3'-untranslated regions of the mRNA. This cDNA encodes a protein of 224 amino acids with extensive homology to mammalian prolactins. By several criteria the encoded protein is likely to be a new member of the prolactin-growth hormone family. Because of its relationship to prolactin and growth hormone and its association with cell proliferation, the protein will be referred to as "proliferin" or "PLF." MATERIALS AND METHODSDNA Sequence Analysis. The cDNA clones were end labeled by filling in 5' overha...

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“…The amino acid sequence of hePRL is identical to that of pPRL, whereas hePRL mRNA is 150 nucleotides larger because of the difference in the 5' untranslated region of each mRNA [6]. hePRL is synthesized in the decidualized endometrium and secreted into the amniotic fluid during pregnancy [7,8]. The physiological role of hePRL has not been fully clarified yet.…”

Section: Introductionmentioning

confidence: 99%

Expression of Prolactin Gene in Human Decidua During Pregnancy Studied by In Situ Hybridization Histochemistry.

et al. 1995

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Prolactin Synthesis by Human Chorion-Decidual Tissue: a Possible Source of Prolactin in the Amniotic Fluid

Cited by 220 publications

References 15 publications

Regulation of electrolyte transport across cultured endometrial epithelial cells by prolactin

Regulation of electrolyte transport across cultured endometrial epithelial cells by prolactin

Nucleotide sequence of a growth-related mRNA encoding a member of the prolactin-growth hormone family.

Expression of Prolactin Gene in Human Decidua During Pregnancy Studied by In Situ Hybridization Histochemistry.

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