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Title: Cross-linking of surface Ig receptors on murine B lymphocytes stimulates the expression of nuclear tetradecanoyl phorbol acetate-response element-binding proteins

Abstract

Cross-linking of sIg on primary B lymphocytes leads to increased nuclear DNA-binding activity specific for the tetradecanoyl phorbol acetate-response element (TRE), as judged by gel mobility shift assays. Stimulation of B cells to enter S phase of the cell cycle by treatment with the combination of phorbol ester plus calcium ionophore also stimulated nuclear TRE-binding activity within 2 h, with maximal expression at 4 h; however, phorbol ester and calcium ionophore were not as effective in stimulating binding activity when examined separately. Stimulated nuclear expression of TRE-binding activity appears to require protein synthesis. Fos- and Jun/AP-1-related proteins participate directly in the identified nucleoprotein complex, as shown by the ability of c-fos- and c-jun-specific antisera to either alter or completely abolish electrophoretic migration of the complex in native gels. Further, UV photo-cross-linking studies identified two major TRE-binding protein species, whose sizes correspond to TRE-binding proteins derived from HeLa cell nuclear extracts. The results suggest that in primary B cells nuclear TRE-binding activity represents a downstream signaling event that occurs subsequent to changes in protein kinase C activity and intracellular Ca2+ but that can be triggered physiologically through sIg.

Authors:
; ;  [1]
  1. Boston Univ. Medical Center, MA (USA)
Publication Date:
OSTI Identifier:
5868125
Resource Type:
Journal Article
Journal Name:
Journal of Immunology; (USA)
Additional Journal Information:
Journal Volume: 146:6; Journal ID: ISSN 0022-1767
Country of Publication:
United States
Language:
English
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; IMMUNOGLOBULINS; RECEPTORS; NUCLEOPROTEINS; GENE REGULATION; PHORBOL ESTERS; BIOLOGICAL EFFECTS; CELL CYCLE; CELL NUCLEI; CROSS-LINKING; LYMPHOCYTES; MICE; TRANSCRIPTION FACTORS; ULTRAVIOLET RADIATION; ANIMAL CELLS; ANIMALS; BIOLOGICAL MATERIALS; BLOOD; BLOOD CELLS; BODY FLUIDS; CARCINOGENS; CELL CONSTITUENTS; CHEMICAL REACTIONS; CONNECTIVE TISSUE CELLS; ELECTROMAGNETIC RADIATION; ESTERS; GLOBULINS; LEUKOCYTES; MAMMALS; MATERIALS; MEMBRANE PROTEINS; ORGANIC COMPOUNDS; POLYMERIZATION; PROTEINS; RADIATIONS; RODENTS; SOMATIC CELLS; VERTEBRATES; 560300* - Chemicals Metabolism & Toxicology; 560120 - Radiation Effects on Biochemicals, Cells, & Tissue Culture

Citation Formats

Chiles, T C, Liu, J L, and Rothstein, T L. Cross-linking of surface Ig receptors on murine B lymphocytes stimulates the expression of nuclear tetradecanoyl phorbol acetate-response element-binding proteins. United States: N. p., 1991. Web.
Chiles, T C, Liu, J L, & Rothstein, T L. Cross-linking of surface Ig receptors on murine B lymphocytes stimulates the expression of nuclear tetradecanoyl phorbol acetate-response element-binding proteins. United States.
Chiles, T C, Liu, J L, and Rothstein, T L. 1991. "Cross-linking of surface Ig receptors on murine B lymphocytes stimulates the expression of nuclear tetradecanoyl phorbol acetate-response element-binding proteins". United States.
@article{osti_5868125,
title = {Cross-linking of surface Ig receptors on murine B lymphocytes stimulates the expression of nuclear tetradecanoyl phorbol acetate-response element-binding proteins},
author = {Chiles, T C and Liu, J L and Rothstein, T L},
abstractNote = {Cross-linking of sIg on primary B lymphocytes leads to increased nuclear DNA-binding activity specific for the tetradecanoyl phorbol acetate-response element (TRE), as judged by gel mobility shift assays. Stimulation of B cells to enter S phase of the cell cycle by treatment with the combination of phorbol ester plus calcium ionophore also stimulated nuclear TRE-binding activity within 2 h, with maximal expression at 4 h; however, phorbol ester and calcium ionophore were not as effective in stimulating binding activity when examined separately. Stimulated nuclear expression of TRE-binding activity appears to require protein synthesis. Fos- and Jun/AP-1-related proteins participate directly in the identified nucleoprotein complex, as shown by the ability of c-fos- and c-jun-specific antisera to either alter or completely abolish electrophoretic migration of the complex in native gels. Further, UV photo-cross-linking studies identified two major TRE-binding protein species, whose sizes correspond to TRE-binding proteins derived from HeLa cell nuclear extracts. The results suggest that in primary B cells nuclear TRE-binding activity represents a downstream signaling event that occurs subsequent to changes in protein kinase C activity and intracellular Ca2+ but that can be triggered physiologically through sIg.},
doi = {},
url = {https://www.osti.gov/biblio/5868125}, journal = {Journal of Immunology; (USA)},
issn = {0022-1767},
number = ,
volume = 146:6,
place = {United States},
year = {Fri Mar 15 00:00:00 EST 1991},
month = {Fri Mar 15 00:00:00 EST 1991}
}