Induction of expression of protein disulphide-isomerase during lymphocyte maturation stimulated by bacterial lipopolysaccharide.
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.
Biological Laboratory, University of Kent, Canterbury, England.
J L
JL
Paver
R B
RB
Freedman
R M
RM
Parkhouse
D000818:Animals; D001402:B-Lymphocytes / Q000166:cytology / Q000201:enzymology*; D002454:Cell Differentiation; D004790:Enzyme Induction; D066298:In Vitro Techniques; D007535:Isomerases / Q000096:biosynthesis*; D008070:Lipopolysaccharides / Q000494:pharmacology; D008213:Lymphocyte Activation; D051379:Mice; D010950:Plasma Cells / Q000166:cytology / Q000201:enzymology; D019704:Protein Disulfide-Isomerases; D013997:Time Factors
D008070:Lipopolysaccharides; D007535:Isomerases; D019704:Protein Disulfide-Isomerases