A group of three fibroblast secreted polypeptides suppressed by cellular ageing and interferon-gamma.
The structural and quantitative characteristics of many fibroblast-secreted proteins are modified during the in vitro cellular ageing. Here we report that three polypeptides (80, 84 and 87 kDa) absent from late passage fibroblast cultures, are constitutively secreted from young (early passage) cultures of various fibroblast strains whereas they are suppressed by the action of interferon-gamma. The three polypeptides were isolated and monoclonal antibodies were produced against the 84 kDa polypeptide. Immunoprecipitation experiments showed that the three polypeptides share common epitopes. The 80 and 84 kDa polypeptides were studied further and proved to be glycosylated polypeptides exhibiting analogous CNBr digestion peptide maps and identity in their sequenced N-terminal segments.
Eleftheriou
C S
CS
Department of Biochemistry, Hellenic Pasteur Institute, Athens, Greece.
Trakas
N
N
Kokla
A
A
Tzartos
S J
SJ
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D002460:Cell Line; D016922:Cellular Senescence; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes; D005347:Fibroblasts / Q000166:cytology / Q000378:metabolism*; D006801:Humans; D007371:Interferon-gamma / Q000494:pharmacology*; D051379:Mice; D008807:Mice, Inbred BALB C; D008969:Molecular Sequence Data; D010455:Peptides / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D011233:Precipitin Tests
D000911:Antibodies, Monoclonal; D000939:Epitopes; D010455:Peptides; D007371:Interferon-gamma