cDNA‐derived amino acid sequence of L‐histidine decarboxylase from mouse mastocytoma P‐815 cells

Yamamoto, Jun; Yatsunami, Kimio; Ohmori, Eiji; Sugimoto, Yukihiko; Fukui, Tetsuya; Katayama, Toyoko; Ichikawa, Atsushi

doi:10.1016/0014-5793(90)80545-t

Cited by 82 publications

(50 citation statements)

References 14 publications

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“…The reported molecular mass of purified enzymes from various mammalian tissues has all been 53-55-kDa (19,20,27) while the mouse HDC cDNA codes a protein with a predicted molecular mass of 74 kDa (28 kDa) are expressed in the male reproductive tissues. We recently generated a mouse strain, genetically lacking the pyridoxal-binding site of HDC, and exhibiting no HDC activity (29,30).…”

Section: Discussionmentioning

confidence: 99%

Expression of l-Histidine Decarboxylase in Mouse Male Germ Cells

Safina

Tanaka

Inagaki

et al. 2002

Journal of Biological Chemistry

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Histamine synthesis in male reproductive tissues remains largely unknown. The interaction between stem cell factor and its receptor, c-Kit, has been found to be essential for the maturation of male germ cells and peripheral mast cells. Based on this analogy, we investigated the expression of histidine decarboxylase (HDC), the rate-limiting enzyme of histamine synthesis, in mouse male germ cells. Immunohistochemical analyses revealed that HDC is localized in the acrosomes of spermatids and spermatozoa. In the testis, epididymis, and spermatozoa, a significant amount of histamine and HDC activity were detected. W/W V mice, known to lack most of their germ cells in the seminiferous tubules, were found to lack HDC protein expression as well as HDC activity in the testis. An in vitro acrosome reaction induced by a calcium ionophore, A23187, caused the release of histamine from epididymal spermatozoa. Our observations indicate that histamine is produced in and released from the acrosomes.

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Section: Discussionmentioning

confidence: 99%

Expression of l-Histidine Decarboxylase in Mouse Male Germ Cells

Safina

Tanaka

Inagaki

et al. 2002

Journal of Biological Chemistry

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“…Comparison of the deduced amino acid sequence of human HisDC with rat and mouse HisDC Human HisDC shares high similarity with rat [13] and mouse HisDC [20], and the similarity is 92% and 91 %, respectively, in regions A, B and C (Fig. 3).…”

Section: Al-------o---mentioning

confidence: 99%

“…These results suggest that HisDC gene transcripts in human lung and brain are spliced predominantly to generate the 2.4-kb species, and the 3.4-kb transcript is specific for KU-812-F cells. Two types of HisDC mRNA (major 2.7 kb and minor 3.5 kb) were also detected in rat tissues including liver [13], stomach [21] and basophilic leukemia cells (unpublished data), although only one type of HisDC mRNA (2.7 kb) was detected in mouse mastocytoma P-815 cells [20]. Thus, the alternative splicing of the HisDC gene transcripts may be cell or species specific.…”

Section: Expression Of Hisdc Mrna In Human Tissuesmentioning

confidence: 99%

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

Ruriko

Yamauchi

Tanno

et al. 1992

European Journal of Biochemistry

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L‐Histidine decarboxylase (HisDC) is the enzyme catalyzing the formation of histamine from L‐histidine. HisDC activity is expressed specifically in mast cells/basophils, endocrine cells in stomach, and histaminergic neurons in brain. As a first step in the analysis of the regulation of HisDC gene expression, we have cloned the cDNA coding for HisDC from a cDNA library of a human basophilic leukemia cell line, KU‐812‐F. We identified two types of HisDC cDNA, representing the 2.4‐kb and 3.4‐kb HisDC mRNA constitutively expressed in these cells. Sequence analysis of these cDNA revealed that the 3.4‐kb mRNA contains the insert sequence of 824 bases and suggests that both 2.4‐kb and 3.4‐kb mRNA may represent the alternatively spliced transcripts of the HisDC gene. Using expression plasmids containing a cDNA for each HisDC mRNA, we analyzed the function of possible HisDC isoforms. We show that only the 2.4‐kb mRNA encodes functional HisDC and is expressed in human brain and lung. However, we were unable to detect the 3.4‐kb mRNA in these tissues. Thus, the 3.4‐kb mRNA may be generated by KU‐812‐F cell‐specific splicing of the HisDC gene transcripts. Furthermore, we demonstrated the increase in the level of 2.4‐kb HisDC mRNA and HisDC activity in KU‐812‐F cells following treatment with phorbol 12‐myristate 13‐acetate.

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“…Human ␤-galactosidase is post-translationally processed by cleavage at a similar RDS motif. The protease that performs this maturation is known as "protective protein" and post-proteolytically acts to stabilize ␤-galactosidase and regulate its intralysosomal degradation (28,29). These are the first data that implicate a specific cellular protease with HDC processing in vivo, and it is interesting that this protease is linked to the lysosome.…”

Section: -55-kda Isoforms Are Not Required For Rat Hdc Activitymentioning

confidence: 99%

“…This is highlighted in, but by no means limited to, studies on mouse mastocytoma cells. Hammar and Hjerten (5) described production of a ϳ55-kDa isoform, whereas Yamamoto et al (7,29) described the production of a carboxyl-truncated ϳ53-kDa isoform from the same cell type. Although we cannot completely rule out slight variations in the exact size estimations performed in other studies, our results on this are clear, the ϳ53.7-kDa HDC1/477 isoform is the minimal unit of carboxyl-truncated rat HDC that is capable of retaining enzymatic activity.…”

Section: -55-kda Isoforms Are Not Required For Rat Hdc Activitymentioning

confidence: 99%

The Production of 53–55-kDa Isoforms Is Not Required for Ratl-Histidine Decarboxylase Activity

Fleming

Wang

2003

Journal of Biological Chemistry

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Post-translational processing of the histamine-producing enzyme, L-histidine decarboxylase (HDC), leads to the formation of multiple carboxyl-truncated isoforms. Nevertheless, it has been widely reported that the mature catalytically active dimer is dependent specifically on the production of carboxyl-truncated 53-55-kDa monomers. Here we use transiently transfected COS-7 cells to study the properties of carboxyl-truncated rat HDC isoforms in the 52-58-kDa size range. Amino acid sequences important for the production of a 55-kDa HDC isoform were identified by successive truncations through amino acids 502, 503, and 504. Mutating this sequence in the full-length protein prevented the production of 55-kDa HDC but did not affect enzymatic activity. Further truncations to amino acid 472 generated an inactive 53-kDa HDC isoform that was degraded by the proteasome pathway. These results suggested that processed isoforms, apart from 53-55-kDa ones, contribute toward histamine biosynthesis in vivo. This was confirmed in physiological studies where regulated increases in HDC activity were associated with the expression of isoforms that were greater than 55 kDa in size. We provide evidence to show that regulation of HDC expression can be achieved by the differential production or differential stabilization of multiple enzyme isoforms.

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cDNA‐derived amino acid sequence of L‐histidine decarboxylase from mouse mastocytoma P‐815 cells

Cited by 82 publications

References 14 publications

Expression of l-Histidine Decarboxylase in Mouse Male Germ Cells

Expression of l-Histidine Decarboxylase in Mouse Male Germ Cells

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

The Production of 53–55-kDa Isoforms Is Not Required for Ratl-Histidine Decarboxylase Activity

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