Cloning and expression of a unique short form of the porcine prolactin receptor

Josephine F. Trott, Anke Schennink, Russell C. Hovey

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Prolactin (PRL) is required not only for maintenance of gestation in pigs but also for mammary gland development and subsequent lactogenesis. The actions of PRL are modulated by both long and short isoforms of the PRL receptor (PRLR), where short isoforms can interfere with the essential signaling function of the long isoform. Using 3′ RACE we have isolated a unique splice variant of the porcine PRLR (pPRLR) that contains a short intracellular domain of 38 aa that is encoded by splicing from exon 9 to a novel exon 11 located 17.5 kb downstream of exon 10 on chromosome 16. The short pPRLR was detected as a 42 kDa protein in membranes from porcine mammary glands. Functional analyses indicated that the short pPRLR functions as a dominant negative against the differentiative function of the long pPRLR and does not transduce a signal to the rat β-casein promoter. Differential abundance of long pPRLR and short pPRLR mRNA was established in a range of porcine tissues. The binding affinity of the short pPRLR for pPRL was lower (Kd=3.7 nM) than the affinity of the long pPRLR (Kd=1.6 nM) despite a fourfold higher level of binding sites for the short pPRLR. Our data raise the possibility that the short pPRLR in pigs may function independently from the long pPRLR, where the splicing strategy used to generate the short pPRLR likely evolved under different selection pressures to those acting on the long pPRLR.

Original languageEnglish (US)
Pages (from-to)51-62
Number of pages12
JournalJournal of Molecular Endocrinology
Volume46
Issue number1
DOIs
StatePublished - Feb 2011

Fingerprint

Prolactin Receptors
Organism Cloning
Swine
Exons
Protein Isoforms
Human Mammary Glands
Prolactin
Chromosomes, Human, Pair 16

ASJC Scopus subject areas

  • Endocrinology
  • Molecular Biology

Cite this

Cloning and expression of a unique short form of the porcine prolactin receptor. / Trott, Josephine F.; Schennink, Anke; Hovey, Russell C.

In: Journal of Molecular Endocrinology, Vol. 46, No. 1, 02.2011, p. 51-62.

Research output: Contribution to journalArticle

Trott, Josephine F. ; Schennink, Anke ; Hovey, Russell C. / Cloning and expression of a unique short form of the porcine prolactin receptor. In: Journal of Molecular Endocrinology. 2011 ; Vol. 46, No. 1. pp. 51-62.
@article{f983687749f94c7290ee412001d175a7,
title = "Cloning and expression of a unique short form of the porcine prolactin receptor",
abstract = "Prolactin (PRL) is required not only for maintenance of gestation in pigs but also for mammary gland development and subsequent lactogenesis. The actions of PRL are modulated by both long and short isoforms of the PRL receptor (PRLR), where short isoforms can interfere with the essential signaling function of the long isoform. Using 3′ RACE we have isolated a unique splice variant of the porcine PRLR (pPRLR) that contains a short intracellular domain of 38 aa that is encoded by splicing from exon 9 to a novel exon 11 located 17.5 kb downstream of exon 10 on chromosome 16. The short pPRLR was detected as a 42 kDa protein in membranes from porcine mammary glands. Functional analyses indicated that the short pPRLR functions as a dominant negative against the differentiative function of the long pPRLR and does not transduce a signal to the rat β-casein promoter. Differential abundance of long pPRLR and short pPRLR mRNA was established in a range of porcine tissues. The binding affinity of the short pPRLR for pPRL was lower (Kd=3.7 nM) than the affinity of the long pPRLR (Kd=1.6 nM) despite a fourfold higher level of binding sites for the short pPRLR. Our data raise the possibility that the short pPRLR in pigs may function independently from the long pPRLR, where the splicing strategy used to generate the short pPRLR likely evolved under different selection pressures to those acting on the long pPRLR.",
author = "Trott, {Josephine F.} and Anke Schennink and Hovey, {Russell C.}",
year = "2011",
month = "2",
doi = "10.1677/JME-10-0101",
language = "English (US)",
volume = "46",
pages = "51--62",
journal = "Journal of Molecular Endocrinology",
issn = "0952-5041",
publisher = "Society for Endocrinology",
number = "1",

}

TY - JOUR

T1 - Cloning and expression of a unique short form of the porcine prolactin receptor

AU - Trott, Josephine F.

AU - Schennink, Anke

AU - Hovey, Russell C.

PY - 2011/2

Y1 - 2011/2

N2 - Prolactin (PRL) is required not only for maintenance of gestation in pigs but also for mammary gland development and subsequent lactogenesis. The actions of PRL are modulated by both long and short isoforms of the PRL receptor (PRLR), where short isoforms can interfere with the essential signaling function of the long isoform. Using 3′ RACE we have isolated a unique splice variant of the porcine PRLR (pPRLR) that contains a short intracellular domain of 38 aa that is encoded by splicing from exon 9 to a novel exon 11 located 17.5 kb downstream of exon 10 on chromosome 16. The short pPRLR was detected as a 42 kDa protein in membranes from porcine mammary glands. Functional analyses indicated that the short pPRLR functions as a dominant negative against the differentiative function of the long pPRLR and does not transduce a signal to the rat β-casein promoter. Differential abundance of long pPRLR and short pPRLR mRNA was established in a range of porcine tissues. The binding affinity of the short pPRLR for pPRL was lower (Kd=3.7 nM) than the affinity of the long pPRLR (Kd=1.6 nM) despite a fourfold higher level of binding sites for the short pPRLR. Our data raise the possibility that the short pPRLR in pigs may function independently from the long pPRLR, where the splicing strategy used to generate the short pPRLR likely evolved under different selection pressures to those acting on the long pPRLR.

AB - Prolactin (PRL) is required not only for maintenance of gestation in pigs but also for mammary gland development and subsequent lactogenesis. The actions of PRL are modulated by both long and short isoforms of the PRL receptor (PRLR), where short isoforms can interfere with the essential signaling function of the long isoform. Using 3′ RACE we have isolated a unique splice variant of the porcine PRLR (pPRLR) that contains a short intracellular domain of 38 aa that is encoded by splicing from exon 9 to a novel exon 11 located 17.5 kb downstream of exon 10 on chromosome 16. The short pPRLR was detected as a 42 kDa protein in membranes from porcine mammary glands. Functional analyses indicated that the short pPRLR functions as a dominant negative against the differentiative function of the long pPRLR and does not transduce a signal to the rat β-casein promoter. Differential abundance of long pPRLR and short pPRLR mRNA was established in a range of porcine tissues. The binding affinity of the short pPRLR for pPRL was lower (Kd=3.7 nM) than the affinity of the long pPRLR (Kd=1.6 nM) despite a fourfold higher level of binding sites for the short pPRLR. Our data raise the possibility that the short pPRLR in pigs may function independently from the long pPRLR, where the splicing strategy used to generate the short pPRLR likely evolved under different selection pressures to those acting on the long pPRLR.

UR - http://www.scopus.com/inward/record.url?scp=79551718973&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79551718973&partnerID=8YFLogxK

U2 - 10.1677/JME-10-0101

DO - 10.1677/JME-10-0101

M3 - Article

C2 - 21147947

AN - SCOPUS:79551718973

VL - 46

SP - 51

EP - 62

JO - Journal of Molecular Endocrinology

JF - Journal of Molecular Endocrinology

SN - 0952-5041

IS - 1

ER -