AJP - Endocrinology and Metabolism, Vol 250, Issue 3 243-E247, Copyright © 1986 by American Physiological Society
LPS-caused secretion of corticosterone is mediated by histamine through histidine decarboxylase
S. Suzuki and K. Nakano
Escherichia coli lipopolysaccharide (LPS) induced strong time- and
dose-dependent secretion of corticosterone (CS) in C3H/HeN mice. In
contrast, C3H/HeJ mice were very insensitive to LPS; 100,000 times more LPS
was required with C3H/HeJ mice for producing a similar degree of CS
secretion as that of C3H/HeN mice. However, C3H/HeJ mice could efficiently
respond to other types of stressors, immobilization stress or injection of
histamine, a possible mediator of LPS-induced CS secretion (28), leading to
a striking increase in the serum levels of CS. Adoptive transfer of spleen
cells from C3H/HeN mice converted x-irradiated C3H/HeJ mice to the donor
phenotype. Injection of LPS produced a large increase in the activity of
histidine decarboxylase (EC 4.1.1.22) in the spleen, lung, and liver of
C3H/HeN mice, whereas C3H/HeJ mice were far less responsive. Transfer of
spleen cells from the C3H/HeN mice made C3H/HeJ mice sensitive to LPS,
leading to an increase in histidine decarboxylase activity in the spleen.
There was a statistically significant relationship between the activity of
splenic histidine decarboxylase and the serum levels of CS. These results
suggest that the LPS-induced secretion of CS is mediated by histamine
through induction of histidine decarboxylase in the spleen, lung, and
liver. This may be significant in relation to the host-defense mechanism
against endotoxemia.
