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Specific binding of B‐CLL cell‐derived chemokinetic inhibitory factor (CIF) to human polymorphonuclear leukocytes
Author(s) -
Siegbahn Agneta,
Garcia Rodolfo C.,
Kishi Kenji,
Nilsson Kenneth,
Venge Per
Publication year - 1987
Publication title -
european journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.904
H-Index - 84
eISSN - 1600-0609
pISSN - 0902-4441
DOI - 10.1111/j.1600-0609.1987.tb00749.x
Subject(s) - cell culture , granulocyte , chemistry , dimethyl sulfoxide , lymphokine , macrophage , monocyte , blood cell , microbiology and biotechnology , in vitro , biochemistry , immunology , biology , genetics , organic chemistry
The chemokinetic inhibitory factor (CIF) is a recently described B‐cell derived lympho‐kine that mediates a chemokinetic inhibitory effect on human polymorphonuclear leukocyte (PMN) migration. In the present report the interaction of CIF with the neutrophil plasma membrane was studied. Normal human peripheral blood neu‐trophils and purified neutrophil plasma membranes selectively removed biologic activity from CIF‐containing concentrates obtained during the purification procedure from conditioned medium. Removal was obtained at both 4°C and 37°C. Furthermore, HL‐60 cells treated with dimethyl sulfoxide removed CIF activity (granulocyte‐like cells) but HL‐60 cells treated with 12–0‐tetradecanoylphorbol‐13‐acetate (ma‐crophage‐like cells) did not. Purified human blood monocytes, cells from the mac‐rophage‐like U‐937 cell line and cells from the basophilic leukemia cell line KU‐812 did not remove CIF. These studies suggest that neutrophils express specific binding sites for CIF‐activity.