Functional analysis of alternatively spliced transcripts of the human histidine decarboxylase gene and its expression in human tissues and basophilic leukemia cells

Ruriko, Mamune-Sato; Yamauchi, Kohei; Tanno, Yasuo; Ohkawara, Yuichi; Ohtsu, Hiroshi; Katayose, Dai; Maeyama, Kazutaka; Watanabe, Takehiko; Shibahara, Shigeki; Takishima, Tamotsu

doi:10.1111/j.1432-1033.1992.tb17317.x

Cited by 28 publications

(22 citation statements)

References 22 publications

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“…In addition, the specific activity of the purified human rHDC54 (1.12 mol/mg/min) was proved to be equivalent to that of the mouse and rat HDCs (800 and 260 nmol/mg/min, respectively), suggesting that human rHDC54 is functionally similar to native HDCs from mammalian tissues or cells. This is reasonable because the homology of the 54-kDa HDC molecules is considerably high among three mammals (Mamune-Sato et al, 1992). However, the activity of 74-kDa HDCs might differ among them because the homology in their C-terminal 20-kDa is not so striking.…”

Section: Fig 4 Superdex 200 Fplc Column Chromatography Of the Recommentioning

confidence: 80%

“…In addition, it is totally unknown whether 74-kDa HDCs from other mammalian sources have a molecular nature similar to that of mouse 74-kDa HDC. Although the 54-kDa HDCs purified so far characteristically resemble each other, the nature of 74-kDa HDCs might differ among man, mouse, and rat in some respects, because their C-terminal regions are not so homologous (Mamune-Sato et al, 1992).…”

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confidence: 99%

“…To our surprise, the human 74-and 54-kDa HDCs exhibited equivalent enzyme activity, and the latter existed as a monomer form. 74-and 54-kDa HDCs-A human HDC cDNA, pTN-2 (Yamauchi et al, 1990;Mamune-Sato et al, 1992), in the Okayama-Berg cDNA cloning/expression vector (Okayama and Berg, 1982) was kindly provided by Dr. Kohei Yamauchi (Tohoku University, * The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C.…”

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confidence: 99%

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Comparative Studies of Human Recombinant 74- and 54-kDa L-Histidine Decarboxylases

Yatsunami

Tsuchikawa

Kamada

et al. 1995

Journal of Biological Chemistry

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We have expressed and characterized human recombinant 74-kDa (rHDC74) and 54-kDa (rHDC54) L-histidine decarboxylases (HDCs) in Sf9 cells. By immunoblot analysis, rHDC74 and rHDC54 were shown to be localized predominantly in the particulate and soluble fractions, respectively. rHDC74 exhibited histamine-synthesizing activity equivalent to that of rHDC54. The existence of 74-and 54-kDa HDCs was also confirmed in the particulate and supernatant fractions of the cell lysate, respectively, from the human basophilic leukemia cell line KU-812-F. The ratio of HDC activity to immunoreactivity was similar for the two forms of the enzyme. The specific activity of purified rHDC54 (1.12 mol/mg/min) was comparable to those of HDCs from other mammalian tissues or cells. The purified rHDC54 was eluted as a monomer form from a Superdex-200 column; the molecular mass of the enzyme was approximately 54 kDa on SDS-polyacrylamide gel electrophoresis without 2-mercaptoethanol. The HDC activity of rHDC54 significantly decreased on dialysis against buffer without pyridoxal 5-phosphate; addition of pyridoxal 5-phosphate to the dialysate readily increased in the enzyme activity to the original activity. Taken together, these results suggest that human HDC functions as both 74-and 54-kDa forms having equivalent HDC activity, which are localized in the particulate and soluble fractions, respectively, and that the latter form exhibits its activity as a monomer form.

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Section: Fig 4 Superdex 200 Fplc Column Chromatography Of the Recommentioning

confidence: 80%

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confidence: 99%

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confidence: 99%

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Comparative Studies of Human Recombinant 74- and 54-kDa L-Histidine Decarboxylases

Yatsunami

Tsuchikawa

Kamada

et al. 1995

Journal of Biological Chemistry

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“…Finally, we examined expression of HDC mRNA in various myeloid cell lines. As visible in Figure 2D, the CMLderived basophil cell line KU812 was found to express substantial amounts of HDC mRNA (both transcripts 49 ), whereas the nonbasophil cell line K562 did not express significant amounts of HDC mRNA ( Figure 2D). Corresponding data were obtained when cellular histamine levels were measured by RIA.…”

Section: Expression Of Histidine Decarboxylase (Hdc) and Histamine Inmentioning

confidence: 93%

The CML-related oncoprotein BCR/ABL induces expression of histidine decarboxylase (HDC) and the synthesis of histamine in leukemic cells

Aichberger

Mayerhofer

Vales

et al. 2006

Blood

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“…The amount of HDC mRNA in the HMC-1 cells appeared slightly greater than that in KU-812-F cells. Two HDC mRNA species were observed in HMC-1 cells as in KU-812-F cells, which were supposed to be generated by alternative splicing (15). In order to ascertain whether mast cell-/basophil-specific expression of HDC mRNA is transcriptionally regulated, we performed a nuclear run-on assay.…”

Section: Hdc Mrna Expression and Transcription In Different Cellmentioning

confidence: 99%

Mast Cell-/Basophil-specific Transcriptional Regulation of Human l-Histidine Decarboxylase Gene by CpG Methylation in the Promoter Region

Kuramasu¹,

Saito²,

Suzuki³

et al. 1998

Journal of Biological Chemistry

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L-Histidine decarboxylase (HDC) catalyzes the formation of histamine from L-histidine, and in hematopoietic cell lineages the gene is expressed only in mast cells and basophils. We attempted here to discover how HDC gene expression is restricted in these cells. In the cultured cell lines tested, only the mast cells and basophils strongly transcribed the HDC gene. However, in transient transfection analysis, the reporter constructs with the HDC promoter were active not only in expressing cells but also in nonexpressing cells. Detailed analyses of the HDC promoter region revealed that the GC box is essential for transactivation. Also, the promoter region of the HDC gene proved to be sensitive to DNase I and restriction endonucleases exclusively in HDC-expressing cells, suggesting that the promoter region is readily accessible to trans-acting factor(s). Furthermore, the promoter region in HDC-expressing cell lines was found to be selectively unmethylated. The correlation between HDC expression and hypomethylation was also found in primary human mast cells. Methylation of the HDC promoter in vitro reduced the luciferase reporter activity in transient expression analysis, suggesting that methylation of the promoter region is functionally important for HDC gene expression. These results imply that alteration of DNA methylation is one of the mechanisms regulating cell-specific expression of the HDC gene.

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Functional analysis of alternatively spliced transcripts of the human histidine decarboxylase gene and its expression in human tissues and basophilic leukemia cells

Cited by 28 publications

References 22 publications

Comparative Studies of Human Recombinant 74- and 54-kDa L-Histidine Decarboxylases

Comparative Studies of Human Recombinant 74- and 54-kDa L-Histidine Decarboxylases

The CML-related oncoprotein BCR/ABL induces expression of histidine decarboxylase (HDC) and the synthesis of histamine in leukemic cells

Mast Cell-/Basophil-specific Transcriptional Regulation of Human l-Histidine Decarboxylase Gene by CpG Methylation in the Promoter Region

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