The occurrence of L-lactate dehydrogenase in the inner mitochondrial compartment of pig liver

被引:11
|
作者
Paventi, Gianluca [1 ]
Pizzuto, Roberto [1 ]
Passarella, Salvatore [1 ,2 ]
机构
[1] Univ Molise, Dept Med & Hlth Sci Vincenzo Tiberio, Via Sanctis, I-86100 Campobasso, Italy
[2] Univ Bari, Hosp Policlin, Sch Med & Surg, Piazza Giulio Cesare 11, I-70124 Bari, Italy
关键词
Mitochondria; L-lactate dehydrogenase; Pig liver; L-lactate; Sus scrofa; SUBCELLULAR-LOCALIZATION; METABOLISM; PROTEINS; TRANSPLANTATION; OXALOACETATE; OXIDATION; PYRUVATE; SHUTTLE; CITRATE; CELLS;
D O I
10.1016/j.bbrc.2017.05.154
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Although pig represents a model species in biomedical research including studies dealing with liver patho-physiology, some aspects of liver metabolism need to be addressed. In particular, whether and how pig mitochondria can metabolize L-lactate remains to be established. We show here that pig liver mitochondria (PLM) possess their own L-lactate dehydrogenase (mL-LDH). This was shown both via immunological analysis and by assaying photometrically the L-LDH reaction in solubilised PLM. The mL-LDH reaction shows hyperbolic dependence on the substrate concentration, it is inhibited by oxamate and proves to differ from the cytosolic activity (cL-LDH), as revealed by the difference found in both pH profiles and temperature dependence of m- and cL-LDH. Titration experiments with digitonin show that mL-LDH is restricted in mitochondrial inner compartment. In agreement with the above findings, three genes in Sus scrofa genome encoded for L-LDH subunits which are predicted to have mitochondrial localization, as investigated by Target P 1.1 and PredSL analysis. (C) 2017 Elsevier Inc. All rights reserved.
引用
收藏
页码:255 / 261
页数:7
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