Agmatine transport in brain mitochondria: a different mechanism from that in liver mitochondria

被引：18

作者：

Battaglia, V. ^{[1
]}

Grancara, S. ^{[1
]}

Mancon, M. ^{[1
]}

Cravanzola, C. ^{[4
]}

Colombatto, S. ^{[4
]}

Grillo, M. A. ^{[4
]}

Tempera, G. ^{[2
,3
,5
]}

Agostinelli, E. ^{[2
,3
,5
]}

Toninello, A. ^{[1
]}

机构：

[1] Univ Padua, Dept Biol Chem, I-35121 Padua, Italy

[2] Univ Roma La Sapienza, Dept Biochem Sci, Inst Biol, I-00185 Rome, Italy

[3] CNR, I-00185 Rome, Italy

[4] Univ Turin, Biochem Unit, Dept Med & Expt Oncol, I-10126 Turin, Italy

[5] Univ Roma La Sapienza, Dept Biochem Sci, Inst Mol Pathol, I-00185 Rome, Italy

来源：

AMINO ACIDS | 2010年 / 38卷 / 02期

关键词：

Rat brain mitochondria; Agmatine; Kinetics; Polyamine; Transport; Imidazoline receptor; METABOLIC PATHWAY; RAT-BRAIN; SPERMINE; AMINE; LOCALIZATION; INHIBITION; LIGAND;

D O I：

10.1007/s00726-009-0401-1

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：

The diamine agmatine (AGM), exhibiting two positive charges at physiological pH, is transported into rat brain mitochondria (RBM) by an electrophoretic mechanism, requiring high membrane potential values and exhibiting a marked non-ohmic force-flux relationship. The mechanism of this transport apparently resembles that observed in rat liver mitochondria (RLM), but there are several characteristics that strongly suggest the presence of a different transporter of agmatine in RBM. In this type of mitochondria, the extent of initial binding and total accumulation is higher and lower, respectively, than that in liver; saturation kinetics and the flux-voltage relationship also exhibit different trends, whereas idazoxan and putrescine, ineffective in RLM, act as inhibitors. The characteristics of agmatine uptake in RBM lead to the conclusion that its transporter is a channel with two asymmetric energy barriers, showing some characteristics similar to those of the imidazoline receptor I-2 and the sharing with the polyamine transporter.

引用

页码：423 / 430

页数：8

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