Reduced Expression of Perchloric Acid-Soluble Protein after Partial Hepatectomy in Rats

Kanouchi, Hiroaki; Taga, Masaki; Okamoto, Takeaki; Yamasaki, Masao; Oka, Tatsuzo; Yamada, Koji; Toné, Shigenobu; Minatogawa, Yohsuke

doi:10.1271/bbb.70.290

Cited by 3 publications

(1 citation statement)

References 10 publications

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“…Firstly, Der f 34, the RidA homolog of Dermatophagoides spp., appears to be responsible for house dust mite allergy (ElRamlawy et al, 2016). Furthermore, Hs RidA dysregulation, as well as post‐translational modification (Siculella et al, 2021), has been associated with tumor development (Asagi et al, 1998; Ceciliani et al, 1996; Kanouchi et al, 2000; Kanouchi et al, 2006). These different effects may be related to the unique biophysical properties of this protein.…”

Section: Introductionmentioning

confidence: 99%

Site‐directed mutagenesis reveals the interplay between stability, structure, and enzymatic activity in RidA from Capra hircus

Rizzi,

Digiovanni,

Degani

et al. 2024

Protein Science

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Reactive intermediate deaminase A (RidA) is a highly conserved enzyme that catalyzes the hydrolysis of 2‐imino acids to the corresponding 2‐keto acids and ammonia. RidA thus prevents the accumulation of such potentially harmful compounds in the cell, as exemplified by its role in the degradation of 2‐aminoacrylate, formed during the metabolism of cysteine and serine, catalyzing the conversion of its stable 2‐iminopyruvate tautomer into pyruvate. Capra hircus (goat) RidA (ChRidA) was the first mammalian RidA to be isolated and described. It has the typical homotrimeric fold of the Rid superfamily, characterized by remarkably high thermal stability, with three active sites located at the interface between adjacent subunits. ChRidA exhibits a broad substrate specificity with a preference for 2‐iminopyruvate and other 2‐imino acids derived from amino acids with non‐polar non‐bulky side chains. Here we report a biophysical and biochemical characterization of eight ChRidA variants obtained by site‐directed mutagenesis to gain insight into the role of specific residues in protein stability and catalytic activity. Each mutant was produced in Escherichia coli cells, purified and characterized in terms of quaternary structure, thermal stability and substrate specificity. The results are rationalized in the context of the high‐resolution structures obtained by x‐ray crystallography.

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Section: Introductionmentioning

confidence: 99%

Site‐directed mutagenesis reveals the interplay between stability, structure, and enzymatic activity in RidA from Capra hircus

Rizzi,

Digiovanni,

Degani

et al. 2024

Protein Science

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Perchloric acid-soluble protein is expressed in enterocytes and goblet cells in the intestine and upregulated by dietary lipid

Kanouchi

Miyamoto

Oka

et al. 2006

Biochimica et Biophysica Acta (BBA) - General Subjects

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Evidence for a Negative Correlation between Human Reactive Enamine-Imine Intermediate Deaminase A (RIDA) Activity and Cell Proliferation Rate: Role of Lysine Succinylation of RIDA

Siculella

Giannotti

Stanca

et al. 2021

IJMS

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Reactive intermediate deaminase (Rid) proteins are enzymes conserved in all domains of life. UK114, a mammalian member of RidA subfamily, has been firstly identified as a component of liver perchloric acid-soluble proteins (L-PSP). Although still poorly defined, several functions have been attributed to the mammalian protein UK114/RIDA, including the reactive intermediate deamination activity. The expression of UK114/RIDA has been observed in some tumors, arousing interest in this protein as an evaluable tumor marker. However, other studies reported a negative correlation between UK114/RIDA expression, tumor differentiation degree and cell proliferation. This work addressed the question of UK114/RIDA expression in human non-tumor HEK293 cell lines and in some human tumor cell lines. Here we reported that human RIDA (hRIDA) was expressed in all the analyzed cell line and subjected to lysine (K-)succinylation. In HEK293, hRIDA K-succinylation was negatively correlated to the cell proliferation rate and was under the control of SIRT5. Moreover, K-succinylation clearly altered hRIDA quantification by immunoblotting, explaining, at least in part, some discrepancies about RIDA expression reported in previous studies. We found that hRIDA was able to deaminate reactive enamine-imine intermediates and that K-succinylation drastically reduced deaminase activity. As predicted by in silico analysis, the observed reduction of deaminase activity has been related to the drastic alterations of hRIDA structure inferred by K-succinylation. The role of hRIDA and the importance of its K-succinylation in cell metabolism, especially in cancer biology, have been discussed.

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Reduced Expression of Perchloric Acid-Soluble Protein after Partial Hepatectomy in Rats

Cited by 3 publications

References 10 publications

Site‐directed mutagenesis reveals the interplay between stability, structure, and enzymatic activity in RidA from Capra hircus

Site‐directed mutagenesis reveals the interplay between stability, structure, and enzymatic activity in RidA from Capra hircus

Perchloric acid-soluble protein is expressed in enterocytes and goblet cells in the intestine and upregulated by dietary lipid

Evidence for a Negative Correlation between Human Reactive Enamine-Imine Intermediate Deaminase A (RIDA) Activity and Cell Proliferation Rate: Role of Lysine Succinylation of RIDA

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