Characterization of phorbol esters binding to K 562 cells.

Abstract:

:Binding of 20-[3H]-phorbol 2, 13-dibutyrate [( 3H] PDB) to intact human K 562 cells was characterized. Specific binding of [3H] PDB to K 562 cells at 20 degrees C or 37 degrees C reached a maximum within 15-20 min. Maximal specific [3H] PDB binding to K 562 cells was followed by a decline (down regulation) of radioacticity. This down regulation was temperature dependent; no loss of radioactivity occurred by 1 hour at 4 degrees C. When [3H] PDB binding was carried out a 4 degrees C, [3HDB bound to K 562 cells in a rapid, specific, and reversible manner. Phorbol esters which lack tumor-promoting activity, did not inhibit [3H] PDB binding. A Scatchard analysis was compatible with one class of binding sites, Kd = 50 nM and about 2 X 10(5) binding sites per cell. Human serum inhibited specific binding of [3H] PDB. The effect of several chemical compounds on [3H] PDB binding was also investigated. Most of the compounds tested such as butyrate, hemin, gamma-globulins, transferrin, insulin, EGF, and albumin failed to significantly affect the binding of [3H] PDB. In contrast, retinoic acid and quinacrine significantly affected the binding of [3H] PDB: retinoic acid induced a marked increase of [3H] PDB binding which was dose dependent; quinacrine induced a decrease of [3H] PDB binding, even at low concentration.

journal_name

Anticancer Res

journal_title

Anticancer research

authors

Louache F,Villeval JL,Pelicci PG,Rouis M,Titeux M,Henri A,Rochant H,Thomopoulos P,Testa U

subject

Has Abstract

pub_date

1984-01-01 00:00:00

pages

33-9

issue

1-2

eissn

0250-7005

issn

1791-7530

journal_volume

4

pub_type

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