Hydrodynamic properties of rat hepatic prolactin receptors

Rae-Venter, Barbara; Dao, Thomas L.

doi:10.1016/0003-9861(83)90497-6

Cited by 13 publications

(2 citation statements)

References 24 publications

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“…The Mr of this small subunit is almost identical in value with those reported by others (Borst & Sayare, 1982;Haeuptle et al, 1983;Hughes et al, 1983;Yamada & Donner, 1984;Borst et al, 1985;Katoh et al, 1985;Kelly et al, 1985). The hormone-receptor complex has an Mr of 97000-99 800 as revealed by hydrodynamic analysis of hepatic Prl receptors (Jaffe, 1982;Rae-Venter & Dao, 1983), which estimated the Mr of the receptor alone to be 73000-77800. This agrees with our estimated Mr of the aggregated Prl receptor (74000).…”

Section: Discussionsupporting

confidence: 82%

Separation of rabbit mammary-gland prolactin receptors by ion-exchange chromatography, h.p.l.c.-gel filtration and ultracentrifugation

Sakai¹,

Ike²,

Kohmoto³

et al. 1986

Biochemical Journal

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Rabbit mammary-gland prolactin (Prl) receptors in the microsomal fraction were solubilized in 7.5 mM-Chaps) or 1% Triton X-100 and analysed by ion-exchange chromatography using DEAE-Bio-Gel A. Prl receptors in the presence of 7.5 mM-Chaps were separated into two different fractions (Fr. A and B), both of which showed identical specificity of binding to peptide hormones as those in the Chaps or Triton extract. oPrl and human growth hormone (hGH) bound to the same site, but other non-lactogenic hormones (follicle-stimulating hormone, oGH, luteinizing hormone and insulin) failed to bind to the Prl receptors. The dissociation constant (Kd) for Prl binding to the receptors in Fr. A was about 50% of those in Fr. B, suggesting that the rabbit mammary gland contains two types of Prl receptors, one with a high, and one with a low, Kd for Prl binding. A decrease in the concentration of Chaps in the column buffer to 4 mM caused aggregation of the receptors in Fr. A. H.p.l.c.-gel filtration, using Shim pack 150 and 300 columns connected in series, separated the receptor as a protein with an Mr of 74,000 +/- 4,900 (mean +/- S.D.) in the presence of 5 mM-Chaps, or of 36,800 +/- 2,100 in the presence of 7.5 mM-Chaps. Sucrose-gradient-centrifugation analysis showed that the Prl-receptor complexes in the presence of 5 mM-Chaps were sedimented between gamma-globulin and bovine serum albumin (5.56 +/- 0.22 S). As the Chaps concentration was increased to 7.5 mM, a further peak of the Prl-receptor complexes (4.01 +/- 0.23 S) appeared below ovalbumin. The present data suggest that the binding subunit causes the monomeric subunit to aggregate with itself or with another specific associated protein of similar Mr.

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Section: Discussionsupporting

confidence: 82%

Separation of rabbit mammary-gland prolactin receptors by ion-exchange chromatography, h.p.l.c.-gel filtration and ultracentrifugation

Sakai¹,

Ike²,

Kohmoto³

et al. 1986

Biochemical Journal

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“…This value is identical with that reported by Emtner and Roos [26] for female rat liver lac togenic receptors studied with the same technique. Other Mr values reported for solubilized hepatic PRL or lac togenic receptors range from 40,000 to 90,000 [27,28]. Recently, the cDNA of a rat liver prolactin receptor has been cloned.…”

Section: Discussionmentioning

confidence: 99%

Characterization of Prolactin Receptors in Human Choroid Plexus

Lai

Roos²,

Olsson³

et al. 1992

Neuroendocrinology

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The specific binding of ¹²⁵I-human prolactin (hPRL) was studied in different areas of the human brain. Particularly high binding affinity of the hormone was found in the choroid plexus and this tissue was therefore selected for further studies. The hippocampus, the hypothalamus and the pituitary were among other regions containing prolactin-binding sites. In the choroid plexus the amount of PRL receptors was significantly higher in females than in males and was also found in both sexes to decrease with age. The binding affinity of ¹²⁵I-hPRL to choroid plexus was 3.0 × 10⁹M-^↑and the binding capacity was 10.3 pmol per mg protein. Following solubilization with Triton X-100 the PRL receptor fraction retained its hormone-binding properties and upon molecular sieve chromatography it behaved as a protein with a molecular mass of approximately 250,000. Cross-linking of ^I25I-hPRL to receptors from choroid plexus and subsequent sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis indicated a major hormone-binding unit of M_r 44,000. This value is about 7,000 smaller than that reported earlier by us for the growth hormone receptors from the same tissue, following cross-linking to ¹²⁵I-human growth hormone (hGH). By affinity column chromatography a complete separation of the hPRL and hGH binding units was achieved. It was thus shown that in choroid plexus the binding sites for GH and PRL occur as discrete entities.

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Prolactin

Vonderhaar¹

1987

The Mammary Gland

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Hydrodynamic properties of rat hepatic prolactin receptors

Cited by 13 publications

References 24 publications

Separation of rabbit mammary-gland prolactin receptors by ion-exchange chromatography, h.p.l.c.-gel filtration and ultracentrifugation

Separation of rabbit mammary-gland prolactin receptors by ion-exchange chromatography, h.p.l.c.-gel filtration and ultracentrifugation

Characterization of Prolactin Receptors in Human Choroid Plexus

Prolactin

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