title: Cell cycle-associated change in the expression of the proliferation-sensitive and heat-shock protein hs x 70 (IEF14): increased synthesis during mitosis.
abstract: The major heat-inducible protein of transformed human amnion cells (AMA) has been identified as the proliferation-sensitive polypeptide IEF14 (Mr 66 kDa; HeLa protein catalogue). From its mobility in two-dimensional gels (Mr and pI) as well as from the fact that this protein is immunoprecipitated by mAb C92 F3-5 (W. J. Welch, and J. P. Suhan, (1986) J. Cell Biol. 103, 2035-2052), we concluded that this polypeptide is either closely related or identical to the 72 kDa inducible stress human protein hs X 70 (H. R. B. Pelham (1986) Cell 46, 959-961). It is further shown that in AMA cells the rate of synthesis of this protein increases preferentially during mitosis. These results provide further evidence suggesting that the levels of hs X 70 can be modulated by mechanisms independent of heat shock.
authors.affiliation: Department of Medical Biochemistry, Aarhus University, Denmark.
authors.forename: J E
authors.initials: JE
authors.lastname: Celis
authors.forename: J B
authors.initials: JB
authors.lastname: Lauridsen
authors.forename: B
authors.initials: B
authors.lastname: Basse
mesh_terms: D000650:Amnion; D002453:Cell Cycle; D002455:Cell Division; D002461:Cell Line, Transformed; D005455:Fluorescent Antibody Technique; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D006358:Hot Temperature; D006801:Humans; D007163:Immunosorbent Techniques; D007399:Interphase; D008938:Mitosis; D017830:Octoxynol; D011092:Polyethylene Glycols
chemical_list: D006360:Heat-Shock Proteins; D011092:Polyethylene Glycols; D017830:Octoxynol