Characterization of an androgen-responsive, ornithine decarboxylase-related protein in mouse kidney

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Silander , K M , Pihlajamaa , P , Sahu , B , Janne , O A & Andersson , L C 2017 , ' Characterization of an androgen-responsive, ornithine decarboxylase-related protein in mouse kidney ' , Bioscience Reports , vol. 37 , 20170163 . https://doi.org/10.1042/BSR20170163

Title: Characterization of an androgen-responsive, ornithine decarboxylase-related protein in mouse kidney
Author: Silander, Kristian M.; Pihlajamaa, Paivi; Sahu, Biswajyoti; Janne, Olli A.; Andersson, Leif C.
Contributor: University of Helsinki, Research Programs Unit
University of Helsinki, Research Programs Unit
University of Helsinki, Medicum
University of Helsinki, Medicum
Date: 2017-08-31
Language: eng
Number of pages: 15
Belongs to series: Bioscience Reports
ISSN: 0144-8463
URI: http://hdl.handle.net/10138/228290
Abstract: We have investigated and characterized a novel ornithine decarboxylase (ODC) related protein (ODCrp) also annotated as gm853. ODCrp shows 41% amino acid sequence identity with ODC and 38% with ODC antizyme inhibitor 1 (AZIN1). The Odcrp gene is selectively expressed in the epithelium of proximal tubuli of mouse kidney with higher expression in males than in females. Like Odc in mouse kidney, Odcrp is also androgen responsive with androgen receptor (AR)-binding loci within its regulatory region. ODCrp forms homodimers but does not heterodimerize with ODC. Although ODCrp contains 20 amino acid residues known to be necessary for the catalytic activity of ODC, no decarboxylase activity could be found with ornithine, lysine or arginine as substrates. ODCrp does not function as an AZIN, as it neither binds ODC antizyme 1 (OAZ1) nor prevents OAZ-mediated inactivation and degradation of ODC. ODCrp itself is degraded via ubiquination and mutation of Cys(363) (corresponding to Cys(360) of ODC) appears to destabilize the protein. Evidence for a function of ODCrp was found in ODC assays on lysates from transfected Cos-7 cells where ODCrp repressed the activity of endogenous ODC while Cys(363)Ala mutated ODCrp increased the enzymatic activity of endogenous ODC.
Subject: AMINO-ACID DECARBOXYLASES
X-RAY-STRUCTURE
ANTIZYME INHIBITOR
REGULATED DEGRADATION
REQUIRES INTERACTION
ANGSTROM RESOLUTION
HOMOLOGOUS PROTEIN
TRYPANOSOMA-BRUCEI
SUBSTRATE-BINDING
END-PRODUCTS
3111 Biomedicine
1182 Biochemistry, cell and molecular biology
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