Two-dimensional gel electrophoresis was used to study the expression of intracellular proteins in adherent cells of human T lymphoblastic cell line, CCRF-CEM. The adherent cells grown in monolayer on a culture plate decreased the amount of proteins of M(r) 37,000 and pI 4.7-4.9, and of 17,000 and pI 5.7. The proteins were identified to be nucleophosmin for the 37,000 protein and stathmin for the 17,000 protein by microsequencing their CNBr fragments. The amount of proteins was increased in CCRF-CEM cells grown in floating mass to a comparable level of JURKAT cells which grew in floating mass throughout the culture. The adherent cells decreased their growth rate as compared with the cells in the floating mass. These results suggest that the adhesion of human T lymphoblastic cells modulates their morphology and proliferation via a concomitant decrease in the amount of nucleophosmin and stathmin.
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Nakamura et al. (1995) studied this question.
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