Overview
- Peptide (C)GRRYQSTVEAYK, corresponding to amino acid residues 153-164 of rat mitochondrial uncoupling protein 2 (UCP2) (Accession P56500).
- Mouse heart, mouse muscle myoblast (C2C12), rat skeletal muscle, rat adipose tissue, rat pancreas, human brain glioblastoma (U-87 MG), human colorectal adenocarcinoma (HT-29) cell lysates (1:200-1:1000).
Western blot analysis of mouse heart (lanes 1 and 5), rat skeletal muscle (lanes 2 and 6), rat adipose tissue (lanes 3 and 7) and rat pancreas (lanes 4 and 8):1-4. Anti-UCP2 Antibody (#ANT-128), (1:200).
5-8. Anti-UCP2 Antibody, preincubated with UCP2 Blocking Peptide (#BLP-NT128).
Western blot analysis of mouse muscle myoblast (C2C12), human brain glioblastoma (U-87 MG), human colorectal adenocarcinoma (HT-29) cell lines:1-3. Anti-UCP2 Antibody (#ANT-128), (1:200).
4-6. Anti-UCP2 Antibody, preincubated with UCP2 Blocking Peptide (#BLP-NT128).
- Mouse muscle myoblast (C2C12) cells (1:50-1:200).
Mitochondrial carriers (MCs) transport a variety of metabolites across the inner mitochondrial membrane. All MCs belong to the same family since their polypeptide chains consist of three tandemly related sequences of about 100 amino acids. MCs are encoded in humans by SLC25 genes.
UCP2 (Uncoupling protein 2) is a member of the MC family encoded by the SLC25A8 gene. It is expressed on the inner mitochondrial membrane of cells in the lungs, kidneys, spleen, heart and mainly in the hypothalamus, pituitary and brain stem. The expression of UCP2 is upregulated by fatty acids, prostaglandins, TNFα and other cytokines. UCP2 is involved in regulation of body temperature and the control of oxygen radical production.
Each monomer of UCP2 has six helices crossing the cell membrane connected by hydrophilic loops with both the N- and C- termini on the cytosolic side of the inner mitochondrial membrane. UCP2 catalyzes the unidirectional transport of H+. Charge balance can be achieved by cotransport (symport) of solutes, counter-transport of solutes and uniport of electroneutral metabolites. The transport of H+ is stimulated by fatty acids and inhibited by purine nucleotides. In addition, activation of H+ transport by superoxidase has been observed.
Recent studies suggest that UCP2 and other uncoupling proteins are involved in pathologies such as obesity, type-2 diabetes and atherosclerosis. Mice lacking UCP2 have been shown to over-produce reactive oxygen but not to gain weight or be insensitive to cold stimuli1.
