Regulation of transglutaminase activity in Chinese hamster ovary cells.

abstract

• We have investigated the regulation of transglutaminase activity (epsilon-(gamma-glutamyl)lysine crosslinking enzyme) in Chinese hamster ovary cells in culture. We report that transglutaminase activity increases several-fold in CHO cells at maximum density in suspension culture. This increase cannot be explained by the presence of soluble regulators of the enzyme activity or the appearance of a new enzyme activity with a different affinity for substrate, but appears to be due to an increase in total enzyme activity. Treatment of CHO cells at low cell density with 8-bromo cyclic AMP results in a small increase (20--70%) in transglutaminase activity. By studying CHO mutants which have altered or absent cyclic-AMP-dependent protein kinases, we have demonstrated that the effect of cyclic AMP on transglutaminase activity at low cell density is mediated by cyclic-AMP-dependent protein kinase. However, the protein kinase mutants show normal increases in transglutaminase activity at high cell density, indicating that cyclic AMP-dependent protein kinase does not mediate density-dependent changes in transglutaminase activity.

authors

• Davies, Peter

published proceedings

• Biochim Biophys Acta

author list (cited authors)

• Milhaud, P. G., Davies, P. J., Pastan, I., & Gottesman, M. M.

citation count

• 22

complete list of authors

• Milhaud, PG||Davies, PJ||Pastan, I||Gottesman, MM

publication date

• January 1980

publisher

• Elsevier  Publisher

published in

• Biochimica et Biophysica Acta: international journal of biochemistry and biophysics  Journal

keywords

• Animals
• Cell Compartmentation
• Cell Count
• Clone Cells
• Cricetinae
• Cricetulus
• Cyclic AMP
• Female
• Gamma-Glutamyltransferase
• Mutation
• Ovary

Digital Object Identifier (DOI)

• 10.1016/0304-4165(80)90002-1

start page

• 476

end page

• 484

volume

• 630

issue

• 4

URL

• http://dx.doi.org/10.1016/0304-4165(80)90002-1