Open AccessIncrease in proliferative markers after inhibition of transglutaminase.
Author(s) -
Paul J. Birckbichler,
Gerald R. Orr,
M. K. Patterson,
Eugene Conway,
H A Carter
Publication year - 1981
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.78.8.5005
Subject(s) - cystamine , tissue transglutaminase , lysine , biochemistry , chemistry , dna synthesis , fetal bovine serum , peptide , mitosis , amine gas treating , cell growth , microbiology and biotechnology , in vitro , enzyme , biology , amino acid , organic chemistry
Cystamine inhibited transglutaminase activity (R-glutaminyl-peptide:amine gamma-glutamyltransferase, EC 2.3.2.13) of proliferating WI-38 cells in a dose-dependent manner over the concentration range 0.005-0.25 mM when added to the culture medium. The epsilon-(gamma-glutamyl)lysine content in the cells was decreased and several proliferation markers were enhanced. "Non-mitotic" cells were stimulated by cystamine (about 25% of that observed with 10% fetal bovine serum) to undergo DNA synthesis with subsequent increases in nuclei number. Numerous other disulfides, thiols, and amines were ineffective when added to culture medium. The findings are supportive of the concept that growth control involves a relationship between isopeptide crosslinks and proliferation.