AJP - Regulatory, Integrative and Comparative Physiology, Vol 267, Issue 2 602-R611, Copyright © 1994 by American Physiological Society
Histamine H2 receptors and histidine decarboxylase in normal and leukemic human monocytes and macrophages
L. Mirossay, E. Chastre, J. Callebert, J. M. Launay, B. Housset, A. Zimber, J. P. Abita and C. Gespach
Institut National de la Sante et de la Recherche Medicale U55, Hopital Saint-Antoine, Paris, France.
Spontaneous and all-trans-retinoic acid (RA)-induced differentiation of
normal human monocytes and of leukemic THP-1 monocytes into macrophages
resulted in a progressive loss of adenosine 3',5'-cyclic monophosphate
production induced by histamine via typical H2 receptors (H2R). In THP-1
cells and in HL-60 human acute myelocytic leukemia cells, RA treatment
increased the abundance of the 4.5-kb messenger RNA of the H2R gene
fourfold, suggesting transcriptional control by a RA response element.
Scatchard plots of [3H]tiotidine binding indicated the expression of H2R
with similar affinity and binding capacity in THP-1 monocytes and
macrophages, while the conversion of normal monocytes into macrophages
decreased H2R density from 91.8 to 43.1 fmol/mg protein, with no change in
affinity (Kd = 9.9 to 11.2 nM). In THP-1 macrophages, histamine inhibited 4
beta-phorbol 12-myristate 13-acetate (PMA)-induced H2O2 formation via the
activation of H2 receptors. Expression of the H2R gene, histamine
accumulation, and histidine decarboxylase activity were also demonstrated
in normal human monocytes/macrophages and peripheral lymphocytes. Histamine
and H2R may therefore affect, via intracrine, autocrine, and paracrine
pathways, various immune and inflammatory responses of the lymphoid and
myeloid progenitors and lineages in the bone marrow and peripheral tissues.
