Endothelial cell chemotaxic activity expressed in rat placenta is not associated with prolactin-like proteins B and C

Grantley D. Charles, Maria B. Grant, Theresa A. Medrano, Paul Saunders, Marc Edery, Paul A. Kelly, Kathleen T. Shiverick

Research output: Contribution to journalArticle

Abstract

Conditioned medium from gestation day 18 rat placental cultures showed potent stimulation of the directional migration of human retinal endothelial cells. To examine the role of major secreted placental proteins in this chemotaxic activity, prolactin-like proteins (PLPs)-B and C were purified from rat placenta using immuno-affinity chromatography. In contrast to conditioned medium, native PLP-B and PLP-C preparations failed to show any significant stimulation of endothelial cell migration. This study further examined the ability of PLP-B to bind to rat receptors for growth hormone (GH-R) and prolactin (PRL-R). In competitive binding assays with [125I]- hGH, neither native nor recombinant PLPB preparations showed significant high affinity binding to the transfected rat GHR or PRL-R. In summary, neither PLP-B nor PLP-C exhibit the potent chemotaxis stimulatory activity of placental conditioned media, nor does PLP-B show evidence of ability to act via rat GH or PRL receptors.

Original languageEnglish (US)
Pages (from-to)795-804
Number of pages10
JournalLife Sciences
Volume65
Issue number8
DOIs
StatePublished - Jul 16 1999
Externally publishedYes

Fingerprint

Endothelial cells
Protein C
Placenta
Rats
Endothelial Cells
Conditioned Culture Medium
Prolactin
Aptitude
Pregnancy Proteins
Prolactin Receptors
Somatotropin Receptors
Affinity chromatography
Competitive Binding
Chemotaxis
Affinity Chromatography
Cell Movement
Assays
prolactin-like protein B
Pregnancy

Keywords

  • Angiogenesis
  • Growth hormone
  • Placenta
  • Prolactin receptor
  • Prolactin-like proteins

ASJC Scopus subject areas

  • Pharmacology

Cite this

Charles, G. D., Grant, M. B., Medrano, T. A., Saunders, P., Edery, M., Kelly, P. A., & Shiverick, K. T. (1999). Endothelial cell chemotaxic activity expressed in rat placenta is not associated with prolactin-like proteins B and C. Life Sciences, 65(8), 795-804. https://doi.org/10.1016/S0024-3205(99)00306-9

Endothelial cell chemotaxic activity expressed in rat placenta is not associated with prolactin-like proteins B and C. / Charles, Grantley D.; Grant, Maria B.; Medrano, Theresa A.; Saunders, Paul; Edery, Marc; Kelly, Paul A.; Shiverick, Kathleen T.

In: Life Sciences, Vol. 65, No. 8, 16.07.1999, p. 795-804.

Research output: Contribution to journalArticle

Charles, GD, Grant, MB, Medrano, TA, Saunders, P, Edery, M, Kelly, PA & Shiverick, KT 1999, 'Endothelial cell chemotaxic activity expressed in rat placenta is not associated with prolactin-like proteins B and C', Life Sciences, vol. 65, no. 8, pp. 795-804. https://doi.org/10.1016/S0024-3205(99)00306-9
Charles, Grantley D. ; Grant, Maria B. ; Medrano, Theresa A. ; Saunders, Paul ; Edery, Marc ; Kelly, Paul A. ; Shiverick, Kathleen T. / Endothelial cell chemotaxic activity expressed in rat placenta is not associated with prolactin-like proteins B and C. In: Life Sciences. 1999 ; Vol. 65, No. 8. pp. 795-804.
@article{08bd718b616545cebba0df83d1cbae86,
title = "Endothelial cell chemotaxic activity expressed in rat placenta is not associated with prolactin-like proteins B and C",
abstract = "Conditioned medium from gestation day 18 rat placental cultures showed potent stimulation of the directional migration of human retinal endothelial cells. To examine the role of major secreted placental proteins in this chemotaxic activity, prolactin-like proteins (PLPs)-B and C were purified from rat placenta using immuno-affinity chromatography. In contrast to conditioned medium, native PLP-B and PLP-C preparations failed to show any significant stimulation of endothelial cell migration. This study further examined the ability of PLP-B to bind to rat receptors for growth hormone (GH-R) and prolactin (PRL-R). In competitive binding assays with [125I]- hGH, neither native nor recombinant PLPB preparations showed significant high affinity binding to the transfected rat GHR or PRL-R. In summary, neither PLP-B nor PLP-C exhibit the potent chemotaxis stimulatory activity of placental conditioned media, nor does PLP-B show evidence of ability to act via rat GH or PRL receptors.",
keywords = "Angiogenesis, Growth hormone, Placenta, Prolactin receptor, Prolactin-like proteins",
author = "Charles, {Grantley D.} and Grant, {Maria B.} and Medrano, {Theresa A.} and Paul Saunders and Marc Edery and Kelly, {Paul A.} and Shiverick, {Kathleen T.}",
year = "1999",
month = "7",
day = "16",
doi = "10.1016/S0024-3205(99)00306-9",
language = "English (US)",
volume = "65",
pages = "795--804",
journal = "Life Sciences",
issn = "0024-3205",
publisher = "Elsevier Inc.",
number = "8",

}

TY - JOUR

T1 - Endothelial cell chemotaxic activity expressed in rat placenta is not associated with prolactin-like proteins B and C

AU - Charles, Grantley D.

AU - Grant, Maria B.

AU - Medrano, Theresa A.

AU - Saunders, Paul

AU - Edery, Marc

AU - Kelly, Paul A.

AU - Shiverick, Kathleen T.

PY - 1999/7/16

Y1 - 1999/7/16

N2 - Conditioned medium from gestation day 18 rat placental cultures showed potent stimulation of the directional migration of human retinal endothelial cells. To examine the role of major secreted placental proteins in this chemotaxic activity, prolactin-like proteins (PLPs)-B and C were purified from rat placenta using immuno-affinity chromatography. In contrast to conditioned medium, native PLP-B and PLP-C preparations failed to show any significant stimulation of endothelial cell migration. This study further examined the ability of PLP-B to bind to rat receptors for growth hormone (GH-R) and prolactin (PRL-R). In competitive binding assays with [125I]- hGH, neither native nor recombinant PLPB preparations showed significant high affinity binding to the transfected rat GHR or PRL-R. In summary, neither PLP-B nor PLP-C exhibit the potent chemotaxis stimulatory activity of placental conditioned media, nor does PLP-B show evidence of ability to act via rat GH or PRL receptors.

AB - Conditioned medium from gestation day 18 rat placental cultures showed potent stimulation of the directional migration of human retinal endothelial cells. To examine the role of major secreted placental proteins in this chemotaxic activity, prolactin-like proteins (PLPs)-B and C were purified from rat placenta using immuno-affinity chromatography. In contrast to conditioned medium, native PLP-B and PLP-C preparations failed to show any significant stimulation of endothelial cell migration. This study further examined the ability of PLP-B to bind to rat receptors for growth hormone (GH-R) and prolactin (PRL-R). In competitive binding assays with [125I]- hGH, neither native nor recombinant PLPB preparations showed significant high affinity binding to the transfected rat GHR or PRL-R. In summary, neither PLP-B nor PLP-C exhibit the potent chemotaxis stimulatory activity of placental conditioned media, nor does PLP-B show evidence of ability to act via rat GH or PRL receptors.

KW - Angiogenesis

KW - Growth hormone

KW - Placenta

KW - Prolactin receptor

KW - Prolactin-like proteins

UR - http://www.scopus.com/inward/record.url?scp=0033575201&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033575201&partnerID=8YFLogxK

U2 - 10.1016/S0024-3205(99)00306-9

DO - 10.1016/S0024-3205(99)00306-9

M3 - Article

C2 - 10466745

AN - SCOPUS:0033575201

VL - 65

SP - 795

EP - 804

JO - Life Sciences

JF - Life Sciences

SN - 0024-3205

IS - 8

ER -