Induction of L-histidine decarboxylase in a human mast cell line, HMC-1

K. Maeda, H. Taniguchi, I. Ohno, H. Ohtsu, K. Yamauchi, E. Sakurai, Y. Tanno, J. H. Butterfield, T. Watanabe, K. Shirato

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

Histamine is an important mediator in allergic reactions, gastric acid secretions, and neurotransmission in the central nervous system. Basophils and mast cells are the main sources of histamine, which is formed from L- histidine by histidine decarboxylase (HDC). However, the regulatory mechanism of HDC in these cells remains unclear. We examined the regulation of HDC activity and gene expression using a unique human mast cell line, HMC-1, after stimulation with phorbol 12-myristate 13-acetate (PMA) or ionomycin. HDC activity was increased from 52.1 ± 0.4 (mean ± standard deviation) to 154 ± 6.9, or 105.6 ± 6.2 pmol/min/mg protein (n = 3), 4 hours after stimulation with PMA (10 ng/mL) or ionomycin (10-6 M). Although actinomycin D had no effect on this increase, cycloheximide completely inhibited the increase caused by these stimuli. The population of HMC-1 cells containing HDC protein was increased after stimulation with either PMA or ionomycin as evaluated by immunocytochemical analysis with anti-HDC antibody as a marker. HMC-1 constitutively expressed HDC mRNA, and its level was not increased with these stimuli. These results suggest that the increase of HDC activity in HMC-1 induced by PMA or ionomycin is regulated at the translational level.

Original languageEnglish (US)
Pages (from-to)325-331
Number of pages7
JournalExperimental Hematology
Volume26
Issue number4
StatePublished - 1998
Externally publishedYes

Fingerprint

Histidine Decarboxylase
Histidine
Mast Cells
Cell Line
Ionomycin
Acetates
Histamine
Basophils
Gastric Acid
Dactinomycin
Cycloheximide
Synaptic Transmission
Hypersensitivity
Proteins
Central Nervous System
Gene Expression
Messenger RNA
phorbol-12-myristate
Antibodies

Keywords

  • Basophils
  • HDC
  • Ionomycin
  • Mast cells
  • PMA

ASJC Scopus subject areas

  • Cancer Research
  • Cell Biology
  • Genetics
  • Hematology
  • Oncology
  • Transplantation

Cite this

Maeda, K., Taniguchi, H., Ohno, I., Ohtsu, H., Yamauchi, K., Sakurai, E., ... Shirato, K. (1998). Induction of L-histidine decarboxylase in a human mast cell line, HMC-1. Experimental Hematology, 26(4), 325-331.

Induction of L-histidine decarboxylase in a human mast cell line, HMC-1. / Maeda, K.; Taniguchi, H.; Ohno, I.; Ohtsu, H.; Yamauchi, K.; Sakurai, E.; Tanno, Y.; Butterfield, J. H.; Watanabe, T.; Shirato, K.

In: Experimental Hematology, Vol. 26, No. 4, 1998, p. 325-331.

Research output: Contribution to journalArticle

Maeda, K, Taniguchi, H, Ohno, I, Ohtsu, H, Yamauchi, K, Sakurai, E, Tanno, Y, Butterfield, JH, Watanabe, T & Shirato, K 1998, 'Induction of L-histidine decarboxylase in a human mast cell line, HMC-1', Experimental Hematology, vol. 26, no. 4, pp. 325-331.
Maeda K, Taniguchi H, Ohno I, Ohtsu H, Yamauchi K, Sakurai E et al. Induction of L-histidine decarboxylase in a human mast cell line, HMC-1. Experimental Hematology. 1998;26(4):325-331.
Maeda, K. ; Taniguchi, H. ; Ohno, I. ; Ohtsu, H. ; Yamauchi, K. ; Sakurai, E. ; Tanno, Y. ; Butterfield, J. H. ; Watanabe, T. ; Shirato, K. / Induction of L-histidine decarboxylase in a human mast cell line, HMC-1. In: Experimental Hematology. 1998 ; Vol. 26, No. 4. pp. 325-331.
@article{bd636c57e55d4f4f9414304cd3cbf7fd,
title = "Induction of L-histidine decarboxylase in a human mast cell line, HMC-1",
abstract = "Histamine is an important mediator in allergic reactions, gastric acid secretions, and neurotransmission in the central nervous system. Basophils and mast cells are the main sources of histamine, which is formed from L- histidine by histidine decarboxylase (HDC). However, the regulatory mechanism of HDC in these cells remains unclear. We examined the regulation of HDC activity and gene expression using a unique human mast cell line, HMC-1, after stimulation with phorbol 12-myristate 13-acetate (PMA) or ionomycin. HDC activity was increased from 52.1 ± 0.4 (mean ± standard deviation) to 154 ± 6.9, or 105.6 ± 6.2 pmol/min/mg protein (n = 3), 4 hours after stimulation with PMA (10 ng/mL) or ionomycin (10-6 M). Although actinomycin D had no effect on this increase, cycloheximide completely inhibited the increase caused by these stimuli. The population of HMC-1 cells containing HDC protein was increased after stimulation with either PMA or ionomycin as evaluated by immunocytochemical analysis with anti-HDC antibody as a marker. HMC-1 constitutively expressed HDC mRNA, and its level was not increased with these stimuli. These results suggest that the increase of HDC activity in HMC-1 induced by PMA or ionomycin is regulated at the translational level.",
keywords = "Basophils, HDC, Ionomycin, Mast cells, PMA",
author = "K. Maeda and H. Taniguchi and I. Ohno and H. Ohtsu and K. Yamauchi and E. Sakurai and Y. Tanno and Butterfield, {J. H.} and T. Watanabe and K. Shirato",
year = "1998",
language = "English (US)",
volume = "26",
pages = "325--331",
journal = "Experimental Hematology",
issn = "0301-472X",
publisher = "Elsevier Inc.",
number = "4",

}

TY - JOUR

T1 - Induction of L-histidine decarboxylase in a human mast cell line, HMC-1

AU - Maeda, K.

AU - Taniguchi, H.

AU - Ohno, I.

AU - Ohtsu, H.

AU - Yamauchi, K.

AU - Sakurai, E.

AU - Tanno, Y.

AU - Butterfield, J. H.

AU - Watanabe, T.

AU - Shirato, K.

PY - 1998

Y1 - 1998

N2 - Histamine is an important mediator in allergic reactions, gastric acid secretions, and neurotransmission in the central nervous system. Basophils and mast cells are the main sources of histamine, which is formed from L- histidine by histidine decarboxylase (HDC). However, the regulatory mechanism of HDC in these cells remains unclear. We examined the regulation of HDC activity and gene expression using a unique human mast cell line, HMC-1, after stimulation with phorbol 12-myristate 13-acetate (PMA) or ionomycin. HDC activity was increased from 52.1 ± 0.4 (mean ± standard deviation) to 154 ± 6.9, or 105.6 ± 6.2 pmol/min/mg protein (n = 3), 4 hours after stimulation with PMA (10 ng/mL) or ionomycin (10-6 M). Although actinomycin D had no effect on this increase, cycloheximide completely inhibited the increase caused by these stimuli. The population of HMC-1 cells containing HDC protein was increased after stimulation with either PMA or ionomycin as evaluated by immunocytochemical analysis with anti-HDC antibody as a marker. HMC-1 constitutively expressed HDC mRNA, and its level was not increased with these stimuli. These results suggest that the increase of HDC activity in HMC-1 induced by PMA or ionomycin is regulated at the translational level.

AB - Histamine is an important mediator in allergic reactions, gastric acid secretions, and neurotransmission in the central nervous system. Basophils and mast cells are the main sources of histamine, which is formed from L- histidine by histidine decarboxylase (HDC). However, the regulatory mechanism of HDC in these cells remains unclear. We examined the regulation of HDC activity and gene expression using a unique human mast cell line, HMC-1, after stimulation with phorbol 12-myristate 13-acetate (PMA) or ionomycin. HDC activity was increased from 52.1 ± 0.4 (mean ± standard deviation) to 154 ± 6.9, or 105.6 ± 6.2 pmol/min/mg protein (n = 3), 4 hours after stimulation with PMA (10 ng/mL) or ionomycin (10-6 M). Although actinomycin D had no effect on this increase, cycloheximide completely inhibited the increase caused by these stimuli. The population of HMC-1 cells containing HDC protein was increased after stimulation with either PMA or ionomycin as evaluated by immunocytochemical analysis with anti-HDC antibody as a marker. HMC-1 constitutively expressed HDC mRNA, and its level was not increased with these stimuli. These results suggest that the increase of HDC activity in HMC-1 induced by PMA or ionomycin is regulated at the translational level.

KW - Basophils

KW - HDC

KW - Ionomycin

KW - Mast cells

KW - PMA

UR - http://www.scopus.com/inward/record.url?scp=18544400009&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=18544400009&partnerID=8YFLogxK

M3 - Article

VL - 26

SP - 325

EP - 331

JO - Experimental Hematology

JF - Experimental Hematology

SN - 0301-472X

IS - 4

ER -