Processing and activation of recombinant mouse mastocytoma histidine decarboxylase in the particulate fraction of Sf9 cells by porcine pancreatic elastase

Tanaka, Satoshi; Fukui, Tetsuya; Yamamoto, Jun; Shima, Yoh ichiro; Kume, Toshiaki; Ohgo, Makoto; Ichikawa, Atsushi

doi:10.1016/0167-4838(95)00185-w

Cited by 22 publications

(12 citation statements)

References 12 publications

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“…In the baculovirus-insect cell expression system, the 74-kDa form with a relatively low activity was recovered in the insoluble fraction, while the 53-kDa form in the soluble fraction (15). In vitro digestion of the 74-kDa form in the insoluble fraction of the insect cells by porcine pancreatic elastase resulted in liberation of the soluble 53-kDa form, which exhibited a similar characteristics to the purified enzyme (16). We also found that the 74-kDa form of HDC is accumulated in the ER in COS-7 cells while the 54-kDa mutant lacking the C-terminal region is in the cytosol (17).…”

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confidence: 82%

“…Although we previously showed that in vitro cleavage by elastase of the 74-kDa form, which exhibited a low enzyme activity, resulted in generation of an active 53-kDa form (16), it remains to be clarified whether enzymatical activation occurs upon post-translational processing of HDC in histamine-forming cells. In expression systems, mouse and rat 74-kDa form of HDC were found to exhibit no or little enzyme activity, although enzyme activity of human 74-kDa form was reported to be equivalent to that of the 54-kDa C-terminal deletion mutant (15,18,32).…”

Section: Discussionmentioning

confidence: 99%

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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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confidence: 82%

Section: Discussionmentioning

confidence: 99%

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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“…The recombinant 74-kDa form expressed in the particulate fraction of Sf9 cells had a low activity, while the recombinant 54-kDa form that lacks the C-terminal region of the 74-kDa form had a full activity (20,21). Furthermore, the particulate recombinant 74-kDa form was converted into soluble 53-kDa form with a high catalytic activity by porcine pancreatic elastase in vitro (22). These results suggest that the translated HDC is post-translationally processed to active mature form.…”

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confidence: 89%

Intracellular Localization of the 74- and 53-kDa Forms ofl-Histidine Decarboxylase in a Rat Basophilic/Mast Cell Line, RBL-2H3

Tanaka

Nemoto

Yamamura

et al. 1998

Journal of Biological Chemistry

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“…However, the size of cDNA-deduced HDC is around 74 kDa [2]. The expressed recombinant 74 kDa HDC in Sf9 cells was inactive and present in the particulate fraction [3] and the particulate recombinant 74 kDa HDC was converted into its soluble 53 kDa HDC form with a high catalytic activity by porcine pancreas elastase in vitro [4]. These results suggest that the translated mouse mastocytoma HDC is posttranslationally processed to an active mature form.…”

Section: Introductionmentioning

confidence: 61%

Benzamidine-sensitive proteinase in activated cleavage of recombinant 74 kDa histidine decarboxylase into its 53 kDa form in mastocytoma cells

Ichikawa

Funakoshi

Tanaka

et al. 1998

Inflammation Research

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Processing and activation of recombinant mouse mastocytoma histidine decarboxylase in the particulate fraction of Sf9 cells by porcine pancreatic elastase

Cited by 22 publications

References 12 publications

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

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

Intracellular Localization of the 74- and 53-kDa Forms ofl-Histidine Decarboxylase in a Rat Basophilic/Mast Cell Line, RBL-2H3

Benzamidine-sensitive proteinase in activated cleavage of recombinant 74 kDa histidine decarboxylase into its 53 kDa form in mastocytoma cells

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