Induction of expression of protein disulphide‐isomerase during lymphocyte maturation stimulated by bacterial lipopolysaccharide
- 2 January 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 242 (2), 357-362
- https://doi.org/10.1016/0014-5793(89)80501-0
Abstract
Protein disulphide-isomerase (PDI) activity, and the level of immunodetectable PDI protein, were monitored in splenic lymphocytes and in BCL1 cells during culture in the presence of various activating factors. Bacterial lipopolysaccharide stimulated induction of PDI in splenic B cells and BCL1 cells. The time-course and specificity of induction indicated that the increase in expression of PDI is closely coupled to the final stages of B cell differentiation into antibody-producing plasma cells. The system will prove valuable in studies on the control of expression of PDI.Keywords
This publication has 28 references indexed in Scilit:
- ‘B-cell factors’ are pleiotropicImmunology Today, 1988
- In vivo cross-linking of protein disulfide isomerase to immunoglobulinsBiochemistry, 1987
- The role of immunoglobulin heavy chain binding proteinImmunology Today, 1987
- Characterization of secretory protein translocation: ribosome-membrane interaction in endoplasmic reticulum.The Journal of cell biology, 1986
- Native disulphide bond formation in protein biosynthesis: evidence for the role of protein disulphide isomeraseTrends in Biochemical Sciences, 1984
- B cell activation: Three steps and their variationsCell, 1984
- Protein Disulphide‐Isomerase Activity in Various Cells Synthesizing CollagenEuropean Journal of Biochemistry, 1983
- FUNCTIONAL ASPECTS OF IMMUNOGLOBULIN D (IgD)Annals of the New York Academy of Sciences, 1982
- Role of disulfide interchange enzyme in immunoglobulin synthesisBiochemistry, 1981
- Induction of immunoglobulin and antibody synthesis in vitro by lipopolysaccharidesEuropean Journal of Immunology, 1972