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Nuclear origin of progesterone receptor of the chick oviduct cytosol. An immunoelectron microscopic study.

Authors
  • Isola, J
  • Ylikomi, T
  • Tuohimaa, P
Type
Published Article
Journal
Histochemistry
Publisher
Springer Nature
Publication Date
Jan 01, 1986
Volume
86
Issue
1
Pages
53–58
Identifiers
PMID: 3539892
Source
Medline
License
Unknown

Abstract

Progesterone receptor (PR) was studied immunoelectron microscopically from fixed vibratome sections of the chick oviduct and biochemically from the fractionated oviduct homogenate. Immunoelectron microscopically both unoccupied and occupied PR were localized inside the nuclei. Only a few cells showed PR immunoreactivity in the endoplasmic reticulum which probably represents newly synthetized PR. Biochemically unoccupied PR was in the cytosol fraction. The cytosol and nuclear PR as well as the non-transformed 8S-form and the transformed 4S-forms of cytosol PR were recognized by the anti-PR antibody (IgG-RB). The lack of PR immunostaining in the cytoplasm is therefore not due to lack of recognition by IgG-RB. We propose that in the chick oviduct progesterone receptor is a nuclear protein but synthetized in the endoplasmic reticulum.

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