Neutrophil migration inhibition factor from T lymphocytes (NIF-T) : selective removal of biologic activity by human peripheral blood neutrophils, myelocytic leukemia cells, and differentiated HL-60 cells
Weisbart, R.H.; Lusis, A.J.; Chan, G.; Billing, R.; Ashman, R.F.; Golde, D.W.
Journal of Immunology 128(1): 457-462
1982
ISSN/ISBN: 0022-1767 PMID: 6976379 Document Number: 189848
Neutrophil migration inhibition factor from T lymphocytes (NIF-T) is a newly recognized mediator that may regulate neutrophil function. Normal and leukemic human peripheral blood neutrophils selectively removed NIF-T activity from conditioned medium. Removal of NIF-T activity was similar at 37.degree. C and 4.degree. C, neutrophil supernatants did not destroy NIF-T activity and purified neutrophil plasma membranes removed NIF-T activity at 0.degree. C in contrast to the microsomal fraction of neutrophils, suggesting that membrane binding was responsible for neutrophil removal of NIF-T activity. The specificity of the removal of NIF-T activity by human neutrophils was indicated by the absence of detectable removal by human peripheral blood monocytes and alveolar macrophages and by neutrophils from other species. Cells from patients with acute and chronic myelocytic leukemia removed measurable NIF-T activity; cells from a patient with acute myelomonocytic leukemia did not. In contrast to other human lymphoid and myeloid cell lines, only the human promyeloblast cell line, HL-60, removed NIF-T activity. Uninduced HL-60 cells removed only .apprx. 7% of the NIF-T activity removed by neutrophils. Differentiation of HL-60 cells by exposure to dimethyl sulfoxide enhanced the removal capacity for NIF-T to that of peripheral blood neutrophils and differentiated HL-60 cells responded to NIF-T in the migration assay. The responsiveness of differentiated HL-60 cells to NIF-T was markedly impaired. Monocytes differentiated from HL-60 by 12-O-tetradecanoylphorbol-13-acetate did not remove measurable NIF-T activity. Human neutrophils and neutrophil precursors may express specific binding sites for NIF-T.