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Investigations on the cellular uptake of hexadecylphosphocholine
Author(s) -
Fleer Eduard A. M.,
Berkovic Dinko,
Eibl Hansjoerg,
Unger Clemens
Publication year - 1993
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02535995
Subject(s) - monensin , endocytosis , colchicine , cytochalasin b , chemistry , cell culture , receptor , cytochalasin , clinical chemistry , cell , biochemistry , microbiology and biotechnology , biology , medicine , cytoskeleton , genetics
The uptake of [(9,10)‐ 3 H]hexadecylphosphocholine (HePC) in six tumor cell lines was studied. All cell lines incorporated HePC in similar amounts, with the exception of the epidermoid cancer cell line KB, which took up higher amounts of HePC. The uptake of HePC at 37°C was shown to be time and concentration dependent. At 20°C, uptake was drastically reduced and at 4°C it was blocked completely. Binding of HePC, at 4°C, was not saturable at concentrations between 5 βg/mL (11.8 μM) and 100 μg/mL (235.3 μM), indicating that cell surface binding is not receptor‐mediated. Furthermore, the effects of inhibitors of endocytosis were investigated. We observed a pronounced inhibitory effect by monensin and cytochalasin B. Colchicine was somewhat less effective whereas chloroquine was almost without effect. From these data we conclude that uptake of HePC is most probably mediated via a receptor‐independent endocytotic mechanism.