Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1991 Aug 1;88(15):6687–6690. doi: 10.1073/pnas.88.15.6687

Identification of prolactin and growth hormone binding proteins in rabbit milk.

M C Postel-Vinay 1, L Belair 1, C Kayser 1, P A Kelly 1, J Djiane 1
PMCID: PMC52153  PMID: 1862093

Abstract

Two distinct soluble proteins that specifically bind 125I-labeled human growth hormone (GH) are identified in the supernatant of ultracentrifuged rabbit milk, using HPLC gel filtration. The higher molecular weight proteins is GH specific, whereas the other one is specific for prolactin (PRL). The PRL-binding protein has a very high affinity for the hormone, almost 10 times higher than the affinity of the mammary gland membrane receptor. The PRL-binding protein is immunoprecipitated by a monoclonal antibody against the PRL receptor; another monoclonal antibody, which inhibits the PRL binding to mammary gland membranes, is a poor competitor for the PRL binding to the milk protein. These findings suggest that the milk PRL-binding protein corresponds to the binding domain of the receptor, but also that the conformation of the receptor and of the binding protein might differ. The milk and the plasma GH-binding proteins have a similar binding affinity. In cross-linking experiments using 125I-labeled human GH, the Mr of the GH-binding protein and of the PRL-binding protein were estimated to be 51,000 and 33,000, respectively. The binding proteins identified in the present work are probably responsible for the transport of their specific ligands in the milk. It is also conceivable that they have a role in the effects of GH and PRL in the mammary gland and/or the intestine of the young.

Full text

PDF
6687

Images in this article

6689Image
on p.6689

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Baumann G., Stolar M. W., Amburn K., Barsano C. P., DeVries B. C. A specific growth hormone-binding protein in human plasma: initial characterization. J Clin Endocrinol Metab. 1986 Jan;62(1):134–141. doi: 10.1210/jcem-62-1-134. [DOI] [PubMed] [Google Scholar]
  2. Baumbach W. R., Horner D. L., Logan J. S. The growth hormone-binding protein in rat serum is an alternatively spliced form of the rat growth hormone receptor. Genes Dev. 1989 Aug;3(8):1199–1205. doi: 10.1101/gad.3.8.1199. [DOI] [PubMed] [Google Scholar]
  3. Baxter R. C., Martin J. L. Binding proteins for the insulin-like growth factors: structure, regulation and function. Prog Growth Factor Res. 1989;1(1):49–68. doi: 10.1016/0955-2235(89)90041-0. [DOI] [PubMed] [Google Scholar]
  4. Bazan J. F. A novel family of growth factor receptors: a common binding domain in the growth hormone, prolactin, erythropoietin and IL-6 receptors, and the p75 IL-2 receptor beta-chain. Biochem Biophys Res Commun. 1989 Oct 31;164(2):788–795. doi: 10.1016/0006-291x(89)91528-3. [DOI] [PubMed] [Google Scholar]
  5. Clandinin M. T., Chappell J. E., Mager D. Prolactin binding protein in human milk. Endocrinol Exp. 1986 Aug;20(2-3):209–215. [PubMed] [Google Scholar]
  6. Djiane J., Durand P., Kelly P. A. Evolution of prolactin receptors in rabbit mammary gland during pregnancy and lactation. Endocrinology. 1977 May;100(5):1348–1356. doi: 10.1210/endo-100-5-1348. [DOI] [PubMed] [Google Scholar]
  7. Dusanter-Fourt I., Gaye P., Belair L., Pétridou B., Kelly P. A., Djiane J. Prolactin receptor gene expression in the rabbit: identification, characterization and tissue distribution of several prolactin receptor messenger RNAs encoding a unique precursor. Mol Cell Endocrinol. 1991 May;77(1-3):181–192. doi: 10.1016/0303-7207(91)90073-2. [DOI] [PubMed] [Google Scholar]
  8. Dusanter-Fourt I., Kelly P. A., Djiane J. Immunological recognition of the prolactin receptor: identification of a single binding unit of molecular weight approximately 42,000. Biochimie. 1987 Jun-Jul;69(6-7):639–646. doi: 10.1016/0300-9084(87)90183-0. [DOI] [PubMed] [Google Scholar]
  9. Gonnella P. A., Harmatz P., Walker W. A. Prolactin is transported across the epithelium of the jejunum and ileum of the suckling rat. J Cell Physiol. 1989 Jul;140(1):138–149. doi: 10.1002/jcp.1041400117. [DOI] [PubMed] [Google Scholar]
  10. Jammes H., Gaye P., Belair L., Djiane J. Identification and characterization of growth hormone receptor mRNA in the mammary gland. Mol Cell Endocrinol. 1991 Jan;75(1):27–35. doi: 10.1016/0303-7207(91)90242-k. [DOI] [PubMed] [Google Scholar]
  11. Katoh M., Djiane J., Kelly P. A. Monoclonal antibodies against rabbit mammary prolactin receptors. Specific antibodies to the hormone binding domain. J Biol Chem. 1985 Sep 25;260(21):11422–11429. [PubMed] [Google Scholar]
  12. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  13. Leung D. W., Spencer S. A., Cachianes G., Hammonds R. G., Collins C., Henzel W. J., Barnard R., Waters M. J., Wood W. I. Growth hormone receptor and serum binding protein: purification, cloning and expression. Nature. 1987 Dec 10;330(6148):537–543. doi: 10.1038/330537a0. [DOI] [PubMed] [Google Scholar]
  14. Lobie P. E., Breipohl W., Waters M. J. Growth hormone receptor expression in the rat gastrointestinal tract. Endocrinology. 1990 Jan;126(1):299–306. doi: 10.1210/endo-126-1-299. [DOI] [PubMed] [Google Scholar]
  15. Peeters S., Friesen H. G. A growth hormone binding factor in the serum of pregnant mice. Endocrinology. 1977 Oct;101(4):1164–1183. doi: 10.1210/endo-101-4-1164. [DOI] [PubMed] [Google Scholar]
  16. Pope G. S., Swinburne J. K. Reviews of the progress of dairy science: hormones in milk: their physiological significance and value as diagnostic aids. J Dairy Res. 1980 Oct;47(3):427–449. doi: 10.1017/s0022029900021336. [DOI] [PubMed] [Google Scholar]
  17. Ramsey D. H., Bern H. A. Stimulation by ovine prolactin of fluid transfer in everted sacs of rat small intestine. J Endocrinol. 1972 Jun;53(3):453–459. doi: 10.1677/joe.0.0530453. [DOI] [PubMed] [Google Scholar]
  18. Smith W. C., Kuniyoshi J., Talamantes F. Mouse serum growth hormone (GH) binding protein has GH receptor extracellular and substituted transmembrane domains. Mol Endocrinol. 1989 Jun;3(6):984–990. doi: 10.1210/mend-3-6-984. [DOI] [PubMed] [Google Scholar]
  19. Spencer S. A., Hammonds R. G., Henzel W. J., Rodriguez H., Waters M. J., Wood W. I. Rabbit liver growth hormone receptor and serum binding protein. Purification, characterization, and sequence. J Biol Chem. 1988 Jun 5;263(16):7862–7867. [PubMed] [Google Scholar]
  20. Taga T., Hibi M., Hirata Y., Yamasaki K., Yasukawa K., Matsuda T., Hirano T., Kishimoto T. Interleukin-6 triggers the association of its receptor with a possible signal transducer, gp130. Cell. 1989 Aug 11;58(3):573–581. doi: 10.1016/0092-8674(89)90438-8. [DOI] [PubMed] [Google Scholar]
  21. Tar A., Hocquette J. F., Souberbielle J. C., Clot J. P., Brauner R., Postel-Vinay M. C. Evaluation of the growth hormone-binding proteins in human plasma using high pressure liquid chromatography gel filtration. J Clin Endocrinol Metab. 1990 Nov;71(5):1202–1207. doi: 10.1210/jcem-71-5-1202. [DOI] [PubMed] [Google Scholar]
  22. Ymer S. I., Herington A. C. Evidence for the specific binding of growth hormone to a receptor-like protein in rabbit serum. Mol Cell Endocrinol. 1985 Jul;41(2-3):153–161. doi: 10.1016/0303-7207(85)90018-8. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES