Expression of l-Histidine Decarboxylase in Mouse Male Germ Cells

Safina, Faizah; Tanaka, Satoshi; Inagaki, Mariko; Tsuboi, Kazuhito; Sugimoto, Yukihiko; Ichikawa, Atsushi

doi:10.1074/jbc.m200702200

Cited by 36 publications

(23 citation statements)

References 26 publications

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“…Unlike with tumor tissue, we found that both the 54-and 74-kDa histidine decarboxylases are equally represented in all three colon cancer cell lines. Because multiple forms of histidine decarboxylase have been shown to be generated by tissue-or cell-specific posttranslational processing (42,44), it might be hypothesized that different processing pathways are responsible for the different expression of the 54-kDa subunit form in either the tumor tissue or the colon cancer cell lines. Our study showed that high levels of histidine decarboxylase activity and histamine content were correlated with the presence of lymph node and/or distant metastases in colorectal cancer.…”

Section: Discussionmentioning

confidence: 99%

The Role of Cyclooxygenase-2 in Mediating the Effects of Histamine on Cell Proliferation and Vascular Endothelial Growth Factor Production in Colorectal Cancer

Cianchi

Cortesini

Schiavone³

et al. 2005

Clinical Cancer Research

104

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Purpose: Activity of histidine decarboxylase, the key enzyme in the synthesis of histamine, has been shown to be increased in several types of human tumors.We attempted to establish whether the possible involvement of histidine decarboxylase and histamine in colorectal carcinogenesis might be mediated by the activation of the cyclooxygenase-2 (COX-2) pathway. Experimental Design: Expression/activity of histidine decarboxylase, histamine content, and prostaglandin E 2 (PGE 2 ) production were analyzed in 33 colorectal cancer samples and in the HT29, Caco-2, and HCT116 colon cancer cell lines. The effects of histamine, celecoxib, and H 1 , H 2 , and H 4 receptor antagonists on COX-2 expression/activity, cell proliferation, and vascular endothelial growth factor (VEGF) production were assessed in the three colon cancer lines that showed different constitutive COX-2 expression. Results: We showed the up-regulation of histidine decarboxylase protein expression and activity in the tumor specimens when compared with normal colonic mucosa. Histidine decarboxylase activity and histamine content were also significantly higher in metastatic tumors than in nonmetastatic ones.These variables significantly correlated with tumor PGE 2 production.The administration of histamine increased COX-2 expression/activity, cell proliferation, and VEGF production in the COX-2-positive HT29 and Caco-2 cells. Treatment with either H 2 /H 4 receptor antagonists or celecoxib prevented these effects. Histamine had no effect on both the COX-2 pathway andVEGF production in the COX-2-negative HCT116 cells. Conclusions: Our data showed that histamine exerts both a proproliferative and a proangiogenic effect via H 2 /H 4 receptor activation. These effects are likely to be mediated by increasing COX-2-related PGE 2 production in COX-2-expressing colon cancer cells.

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Section: Discussionmentioning

confidence: 99%

The Role of Cyclooxygenase-2 in Mediating the Effects of Histamine on Cell Proliferation and Vascular Endothelial Growth Factor Production in Colorectal Cancer

Cianchi

Cortesini

Schiavone³

et al. 2005

Clinical Cancer Research

104

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“…On the other hand, only 74-kDa form was detected in lipopolysaccharide-activated mouse macrophages and monomeric IgE-activated immature bone marrow-derived cultured mast cells, in both of which a large increase in histamine synthesis is observed (21,22). Other variants with intermediate sizes (58ϳ64-kDa) have also been reported in the stomach, fetal liver, and testis (18,23,24). These findings have highlighted the complexity in the regulation of enzyme activity and intracellular localization of HDC through the post-translational processing.…”

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confidence: 93%

Activation of Histidine Decarboxylase through Post-translational Cleavage by Caspase-9 in a Mouse Mastocytoma P-815

Furuta

Nakayama

Sugimoto

et al. 2007

Journal of Biological Chemistry

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L-Histidine decarboxylase (HDC) is the rate-limiting enzyme for histamine synthesis in mammals. Although accumulating evidence has indicated the post-translational processing of HDC, it remains unknown what kinds of proteases are involved. We investigated the processing of HDC in a mouse mastocytoma, P-815, using a lentiviral expression system. HDC was expressed as a 74-kDa precursor form, which is cleaved to yield the 55-and 60-kDa forms upon treatment with butyrate. Alanine-scanning mutations revealed that two tandem aspartate residues (Asp 517 -Asp 518 , Asp 550 -Asp 551 ) are critical for the processing. Treatment with butyrate caused an increase in the enzyme activity of the cells expressing the wild type HDC, but not in the cells expressing the processing-incompetent mutant. An increase in histamine synthesis by butyrate was accompanied by formation of the 55-and 60-kDa form of HDC. In addition, the in vitro translated 74-kDa form of HDC was found to undergo a limited cleavage by purified human caspase-9, whereas the alanine-substituted mutants were not. Processing and enzymatic activation of HDC in P-815 cells was enhanced in the presence of a Zn 2؉ chelator, TPEN. Although treatment with butyrate and TPEN drastically augmented the protease activity of caspase-3, and -9, no apoptotic cell death was observed. Both enzymatic activation and processing of HDC were completely suppressed by a pan-caspase inhibitor, partially but significantly by a specific inhibitor for caspase-9, but not by a caspase-3 inhibitor. These results suggest that, in P-815 cells, histamine synthesis is augmented through the post-translational cleavage of HDC, which is mediated by caspase-9.Histamine plays diverse roles in physiological and pathological responses, such as inflammation, gastric acid secretion, neurotransmission, and immune modulation, by acting on its specific membrane receptors, H 1 , H 2 , H 3 , and H 4 (1-7). L-Histidine decarboxylase (HDC, 2 EC 4.1.1.22) is the rate-limiting enzyme for histamine synthesis in mammals, and targeted disruption of mouse HDC gene resulted in the complete loss of de novo synthesis of histamine (8). Several groups purified HDC from various sources including a mouse mastocytoma, P-815, indicating that purified HDC is a homodimer consisting of a 53-55-kDa subunit (9 -11). In 1990, Joseph et al. (12) succeeded in cDNA cloning of rat HDC for the first time, and demonstrated that the HDC cDNA encodes a protein, of which the molecular mass is 74 kDa. Subsequent cDNA cloning from P-815 cells revealed that mouse HDC cDNA also encodes a 74-kDa protein (13). These results indicate that HDC is initially translated as a 74-kDa form and then converted into the 53-55-kDa form through the post-translational processing. HDC belongs in the fold type I pyridoxal phosphate-dependent enzyme (13,14). Although the region around the active lysine residue of HDC shows homology with the other enzymes in this group, such as the aromatic L-amino acid decarboxylase and glutamate decarboxylase, the C-terminal 20-kDa ...

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“…Total RNA was extracted from the BMMCs, and first-strand cDNA was generated from 1 µg of RNA by using oligo (dT) [12][13][14][15][16][17][18] primer and SuperScriptIII RNase H Reverse Transcriptase (Invitrogen) according to the manufacturer's protocol. The reaction mixture was amplified with the oligonucleotides specific for HDC, MMCP-1, MMCP-2, MMCP-4 and β-actin (11-13).…”

Section: Rna Isolation and Rt-pcr Analysismentioning

confidence: 99%

Activation of peroxisome proliferator‐activated receptor gamma suppresses mast cell maturation involved in allergic diseases

Tachibana

Wada

Katayama

et al. 2008

Allergy

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Background-Mast cells play a central role in allergic and inflammatory diseases. Several reports indicated role of peroxisome proliferator-activated receptor gamma (PPARγ) on mast cell function. However, there is no report about the role of PPARγ on differentiation of mast cells from the progenitors. In this study, we investigated the role of PPARγ in regulating bone marrowderived mast cell maturation and the therapeutic implications for mast cell-related diseases such as atopic or contact dermatitis.

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Expression of l-Histidine Decarboxylase in Mouse Male Germ Cells

Cited by 36 publications

References 26 publications

The Role of Cyclooxygenase-2 in Mediating the Effects of Histamine on Cell Proliferation and Vascular Endothelial Growth Factor Production in Colorectal Cancer

The Role of Cyclooxygenase-2 in Mediating the Effects of Histamine on Cell Proliferation and Vascular Endothelial Growth Factor Production in Colorectal Cancer

Activation of Histidine Decarboxylase through Post-translational Cleavage by Caspase-9 in a Mouse Mastocytoma P-815

Activation of peroxisome proliferator‐activated receptor gamma suppresses mast cell maturation involved in allergic diseases

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