Relaxin pp 179-187 | Cite as

Messenger RNA Dependent Synthesis of a Protein Containing Relaxin Related Sequences

  • Michael J. Gast
  • Hugh D. Niall
  • Irving Boime
Part of the Advances in Experimental Medicine and Biology book series (AEMB)

Abstract

Serum relaxin levels in pregnant rats, sows, and guinea pigs are very low during most of gestation (Sherwood et al. 1975); mean relaxin concentrations in the sow range between 0.1 and 2.0 ng/ml throughout the first 100 days of pregnancy. During this period small electron dense cytoplasmic granules begin to appear in luteal cells. This granule population continued to increase in late gestation, reaching a maximum several days before parturition. About 24–48 hours before delivery a rapid disintegration of the cytoplasmic granules occurs. Serum levels of relaxin rise rapidly and then drop precipitously during parturition and lactation (Belt et al.3 1971). Studies in rat ovarian homogenates also suggest a steady, gradual rise in relaxin production throughout pregnancy (Sherwood and Crnekovic, 1979). The stimuli for the initial production of the hormone, the factors controlling its secretion and storage during pregnancy, and the reasons for its explosive release at term remain obscure. Relaxin has traditionally been assigned to the class of pregnancy-related hormones, but at least one study suggests that in humans the protein is also present in non-pregnant sera (Bryant-Greenwood et al.3 1977).

Keywords

Sucrose Albumin EDTA Cysteine Fractionation 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Belt, W. D., Anderson, L. L., Cavazos, L. F. and Melampy, R. M. (1971). Cytoplasmic granules and relaxin levels in porcine corpora lutea. Endocrinology. 89: 1.PubMedCrossRefGoogle Scholar
  2. Bryant-Greenwood, G.D., Greenwood, F.C., Hale, R.W. and Morislige, W. K. (1977). Hormonal evaluation of the intrauterine pro-gesterone contraceptive system. J. Clin. Endocrinol. Metab. 44:721.CrossRefGoogle Scholar
  3. Chan, S. J., Keim, P. and Steiner, D. F. (1976). Cell-free synthesis of rat preproinsulins: characterization and partial amino acid sequence determination. Proc. Natl. Acad. Sci. 73: 1964.Google Scholar
  4. Daniels-McQueen, S., McWilliams, D., Birken, S., Canfield,R., Landefeld, T. and Boime, I. (1978). Identification of mRNAs encoding the a and (3 subunits of human choriogondotropin. J. Biol. Chem. 253: 7109.Google Scholar
  5. James, R., Niall, H., Kwok, S., and Bryant-Greenwood, G. (1977). Primary structure of porcine relaxin: homology with insulin and related growth factors. Nature 267: 544.PubMedCrossRefGoogle Scholar
  6. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the heat of bacteriophate T4. Nature 227: 680.PubMedCrossRefGoogle Scholar
  7. Laskey, R. A. and Mills, A. D. (1975). Quantitative film detection of 3h and 14C in polyacrylamide gels by fluorography. Eur. J. Biochem. 56:335.PubMedCrossRefGoogle Scholar
  8. Mains, R. E. and Eipper, B. A. (1978). Coordinate synthesis of corticotropins and endorphins by mouse pituitary tumor cells. J. Biol. Chem. 253: 651.Google Scholar
  9. O’Byrne, E. M., Carriere, B. T., Sorenson, L., Segaloff, A., Schwabe, C. and Steinetz, B. G. (1978). Plasma immunoreactive relaxin levels in pregnant and non-pregnant women. J. Clin. Endocrinol. Metab. 47: 1106.Google Scholar
  10. Roberts, J. L., Phillips, M., Rosa, P. A. and Herbert, E. (1978). Steps involved in the processing of common precursor forms of adrenocorticotropin and endorphin in cultures of mouse pituitary cells. Biochemistry. 17: 3609.PubMedCrossRefGoogle Scholar
  11. Sherwood, O. D., Chang, C. C., Bevier, G. W. and Dziuk, P. J. (1975). Radioimmunoassay of plasma relaxin levels throughout pregnancy and at parturition in the pig. Endocrinology 97: 834.PubMedCrossRefGoogle Scholar
  12. Sherwood, O. D. and Crnekovic, V. E. (1979). Development of a homo-logous radioimmunoassay for rat relaxin. Endocrinology 104: 893.PubMedCrossRefGoogle Scholar
  13. Sherwood, O. D. and O’Bryne, E. M. (1974). Purification and characterization of porcine relaxin. Arch. Biochem. Biophys. 160:185.PubMedCrossRefGoogle Scholar
  14. Szczesna, E and Boime, I. (1976). mRNA-dependent synthesis of authentic precursor to human placental lactogen: conversion to its mature hormone form in ascites cell-free extracts. Proc. Nat. Acad. Sci. 73: 1179.Google Scholar

Copyright information

© Plenum Press, New York 1982

Authors and Affiliations

  • Michael J. Gast
    • 1
  • Hugh D. Niall
    • 1
  • Irving Boime
    • 1
  1. 1.Department of Pharmacology School of MedicineWashington UniversitySt. LouisUSA

Personalised recommendations