Binding and bioactivity of ovine and porcine prolactins in porcine mammary tissue

D. J. Jerry, Lester C. Griel, Jr., J. F. Kavanaugh, R. S. Kensinger

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Differential binding of homologous and heterologous prolactin was investigated in porcine mammary tissue. Specific binding of ovine prolactin to porcine mammary membranes or tissue slices was significantly greater than specific binding of the homologous porfine prolactin. Ovine prolactin was also more potent than porcine prolactin in stimulating proliferation of Nb2 cells. In contrast, stimulation of glucose metabolism in porcine mammary explants by porcine prolactin was greater than that by ovine prolactin. Differences in specific binding were probably not due to damage during iodination, as low concentrations of iodinated prolactins were similar to unlabelled prolactins in their abilities to stimulate proliferation of Nb2 cells. Furthermore, electrophoretic analysis of medium from binding reactions suggested that differences in specific binding were not due to proteolytic cleavage of the homologous prolactin into large (>10 kDa) fragments. These studies suggest that ovine prolactin either binds to sites in addition to the authentic lactogenic receptor in porcine mammary tissue or that a significantly higher affinity of ovine prolactin for the porcine lactogenic receptor has little effect on its biological activity.

Original languageEnglish (US)
Pages (from-to)43-51
Number of pages9
JournalJournal of Endocrinology
Volume130
Issue number1
DOIs
StatePublished - Jan 1 1991

Fingerprint

Prolactin
Sheep
Breast
Swine
Cell Proliferation
Halogenation
Glucose
Membranes

All Science Journal Classification (ASJC) codes

  • Endocrinology, Diabetes and Metabolism
  • Endocrinology

Cite this

Jerry, D. J., Griel, Jr., L. C., Kavanaugh, J. F., & Kensinger, R. S. (1991). Binding and bioactivity of ovine and porcine prolactins in porcine mammary tissue. Journal of Endocrinology, 130(1), 43-51. https://doi.org/10.1677/joe.0.1300043
Jerry, D. J. ; Griel, Jr., Lester C. ; Kavanaugh, J. F. ; Kensinger, R. S. / Binding and bioactivity of ovine and porcine prolactins in porcine mammary tissue. In: Journal of Endocrinology. 1991 ; Vol. 130, No. 1. pp. 43-51.
@article{e1714b3db1da4b439430b23e70ef5c3a,
title = "Binding and bioactivity of ovine and porcine prolactins in porcine mammary tissue",
abstract = "Differential binding of homologous and heterologous prolactin was investigated in porcine mammary tissue. Specific binding of ovine prolactin to porcine mammary membranes or tissue slices was significantly greater than specific binding of the homologous porfine prolactin. Ovine prolactin was also more potent than porcine prolactin in stimulating proliferation of Nb2 cells. In contrast, stimulation of glucose metabolism in porcine mammary explants by porcine prolactin was greater than that by ovine prolactin. Differences in specific binding were probably not due to damage during iodination, as low concentrations of iodinated prolactins were similar to unlabelled prolactins in their abilities to stimulate proliferation of Nb2 cells. Furthermore, electrophoretic analysis of medium from binding reactions suggested that differences in specific binding were not due to proteolytic cleavage of the homologous prolactin into large (>10 kDa) fragments. These studies suggest that ovine prolactin either binds to sites in addition to the authentic lactogenic receptor in porcine mammary tissue or that a significantly higher affinity of ovine prolactin for the porcine lactogenic receptor has little effect on its biological activity.",
author = "Jerry, {D. J.} and {Griel, Jr.}, {Lester C.} and Kavanaugh, {J. F.} and Kensinger, {R. S.}",
year = "1991",
month = "1",
day = "1",
doi = "10.1677/joe.0.1300043",
language = "English (US)",
volume = "130",
pages = "43--51",
journal = "Journal of Endocrinology",
issn = "0022-0795",
publisher = "Society for Endocrinology",
number = "1",

}

Jerry, DJ, Griel, Jr., LC, Kavanaugh, JF & Kensinger, RS 1991, 'Binding and bioactivity of ovine and porcine prolactins in porcine mammary tissue', Journal of Endocrinology, vol. 130, no. 1, pp. 43-51. https://doi.org/10.1677/joe.0.1300043

Binding and bioactivity of ovine and porcine prolactins in porcine mammary tissue. / Jerry, D. J.; Griel, Jr., Lester C.; Kavanaugh, J. F.; Kensinger, R. S.

In: Journal of Endocrinology, Vol. 130, No. 1, 01.01.1991, p. 43-51.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Binding and bioactivity of ovine and porcine prolactins in porcine mammary tissue

AU - Jerry, D. J.

AU - Griel, Jr., Lester C.

AU - Kavanaugh, J. F.

AU - Kensinger, R. S.

PY - 1991/1/1

Y1 - 1991/1/1

N2 - Differential binding of homologous and heterologous prolactin was investigated in porcine mammary tissue. Specific binding of ovine prolactin to porcine mammary membranes or tissue slices was significantly greater than specific binding of the homologous porfine prolactin. Ovine prolactin was also more potent than porcine prolactin in stimulating proliferation of Nb2 cells. In contrast, stimulation of glucose metabolism in porcine mammary explants by porcine prolactin was greater than that by ovine prolactin. Differences in specific binding were probably not due to damage during iodination, as low concentrations of iodinated prolactins were similar to unlabelled prolactins in their abilities to stimulate proliferation of Nb2 cells. Furthermore, electrophoretic analysis of medium from binding reactions suggested that differences in specific binding were not due to proteolytic cleavage of the homologous prolactin into large (>10 kDa) fragments. These studies suggest that ovine prolactin either binds to sites in addition to the authentic lactogenic receptor in porcine mammary tissue or that a significantly higher affinity of ovine prolactin for the porcine lactogenic receptor has little effect on its biological activity.

AB - Differential binding of homologous and heterologous prolactin was investigated in porcine mammary tissue. Specific binding of ovine prolactin to porcine mammary membranes or tissue slices was significantly greater than specific binding of the homologous porfine prolactin. Ovine prolactin was also more potent than porcine prolactin in stimulating proliferation of Nb2 cells. In contrast, stimulation of glucose metabolism in porcine mammary explants by porcine prolactin was greater than that by ovine prolactin. Differences in specific binding were probably not due to damage during iodination, as low concentrations of iodinated prolactins were similar to unlabelled prolactins in their abilities to stimulate proliferation of Nb2 cells. Furthermore, electrophoretic analysis of medium from binding reactions suggested that differences in specific binding were not due to proteolytic cleavage of the homologous prolactin into large (>10 kDa) fragments. These studies suggest that ovine prolactin either binds to sites in addition to the authentic lactogenic receptor in porcine mammary tissue or that a significantly higher affinity of ovine prolactin for the porcine lactogenic receptor has little effect on its biological activity.

UR - http://www.scopus.com/inward/record.url?scp=0025768254&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025768254&partnerID=8YFLogxK

U2 - 10.1677/joe.0.1300043

DO - 10.1677/joe.0.1300043

M3 - Article

C2 - 1880477

AN - SCOPUS:0025768254

VL - 130

SP - 43

EP - 51

JO - Journal of Endocrinology

JF - Journal of Endocrinology

SN - 0022-0795

IS - 1

ER -