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Persistent growth of BALB/C mouse plasmacytoma and human myeloma cell lines in the presence of phorbol myristate acetate is associated with continued expression of Lap18 (stathmin)
Author(s) -
Jones N. A.,
Rowlands D. C.,
Johnson W. E. B.,
Maclennan I. C. M.,
Brown G.
Publication year - 1995
Publication title -
hematological oncology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.918
H-Index - 44
eISSN - 1099-1069
pISSN - 0278-0232
DOI - 10.1002/hon.2900130105
Subject(s) - stathmin , plasmacytoma , cell culture , plasma cell leukemia , hl60 , biology , plasma cell , cell growth , microbiology and biotechnology , tetradecanoylphorbol acetate , cancer research , protein kinase c , multiple myeloma , phosphorylation , immunology , biochemistry , genetics
Lap 18 is a highly conserved cytosolic protein that is expressed in dividing cells. Data from a number of studies show that a range of cell lines and mitogen‐stimulated normal cells cultured in PMA phosphorylate and subsequently down‐regulate Lap 18. This has been found to be associated with growth arrest, although it is not clear that these events are causally related. In the present study we confirm that the HL60 promyelocytic leukemia and K562 erythroleukemia cell lines, when cultured with PMA, behave in this manner. This was not the case for any of five mouse plasmacytoma cell lines and six lines derived from patients with multiple myeloma or plasma cell leukemia. All of these lines contain Lap18, although the level of this protein in the mouse but not the human plasmacytoma cell‐line cells is relatively low. All the neoplastic plasma cell‐line cells phosphorylate Lap18 on culture with PMA, but this does not induce growth arrest nor result in down‐regulation of Lap18 expression. Further experiments are required to test whether there is a mechanistic relationship between the continued growth of plasmacytoma cell lines and their failure to down‐regulate Lap18 on culture in PMA.