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Gene Review

SLC16A3  -  solute carrier family 16 (monocarboxylate...

Homo sapiens

Synonyms: MCT 3, MCT 4, MCT-3, MCT-4, MCT3, ...
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Disease relevance of SLC16A3

  • Of 6000 genes, 32 were hypoxia inducible in vitro more than two-fold, five of which were novel, including lactate transporter SLC16A3 and RNAse 4 [1].
  • MCT1 and MCT4 were expressed in BM vesicles, but there was no difference in expression between the IUGR and AGA groups [2].

High impact information on SLC16A3


Biological context of SLC16A3

  • Expression of MCT3 mRNA increased over time as ARPE-19 cells established a differentiated phenotype [5].
  • Inhibition of L-lactic acid transport mediated by MCT4 might to lead to collapse of muscle homeostasis [6].
  • Exercise training can increase the expression of both MCT1 and MCT4 in human muscle, although the extent of this up-regulation may be related to the intensity of training [7].
  • These genes are of special interest, because their products have important roles in cellular glucose metabolism, from glucose uptake (GLUT1) to glycolysis (PFKP) and lactate export (MCT4) [8].

Anatomical context of SLC16A3


Other interactions of SLC16A3

  • CONCLUSIONS: These studies demonstrate for the first time that human RPE expresses two proton-coupled monocarboxylate transporters: MCT1 in the apical membrane and MCT3 in the basolateral membrane [5].
  • In contrast, MCT3 and MCT4 harbor dominant sorting information that cotargets CD147 to the basolateral membrane in both epithelia [12].
  • MCT1 antibody labeled the apical membrane of the RPE intensely, whereas MCT3 labeling was restricted to the basolateral membrane [5].
  • MCT2 was localized in the postsynaptic membrane of parallel fiber-Purkinje cell synapses and MCT4 was situated in the membrane of glial cells in the cerebellum [13].

Analytical, diagnostic and therapeutic context of SLC16A3

  • Western blot analysis revealed that ARPE-19 cells expressed high levels of MCT1 and MCT4 but very little MCT3 protein [5].


  1. Comparison of hypoxia transcriptome in vitro with in vivo gene expression in human bladder cancer. Ord, J.J., Streeter, E.H., Roberts, I.S., Cranston, D., Harris, A.L. Br. J. Cancer (2005) [Pubmed]
  2. Placental lactate transporter activity and expression in intrauterine growth restriction. Settle, P., Sibley, C.P., Doughty, I.M., Johnston, T., Glazier, J.D., Powell, T.L., Jansson, T., D'Souza, S.W. J. Soc. Gynecol. Investig. (2006) [Pubmed]
  3. CD147 is tightly associated with lactate transporters MCT1 and MCT4 and facilitates their cell surface expression. Kirk, P., Wilson, M.C., Heddle, C., Brown, M.H., Barclay, A.N., Halestrap, A.P. EMBO J. (2000) [Pubmed]
  4. Testosterone increases lactate transport, monocarboxylate transporter (MCT) 1 and MCT4 in rat skeletal muscle. Enoki, T., Yoshida, Y., Lally, J., Hatta, H., Bonen, A. J. Physiol. (Lond.) (2006) [Pubmed]
  5. Polarized expression of monocarboxylate transporters in human retinal pigment epithelium and ARPE-19 cells. Philp, N.J., Wang, D., Yoon, H., Hjelmeland, L.M. Invest. Ophthalmol. Vis. Sci. (2003) [Pubmed]
  6. Inhibitory effects of statins on human monocarboxylate transporter 4. Kobayashi, M., Otsuka, Y., Itagaki, S., Hirano, T., Iseki, K. International journal of pharmaceutics. (2006) [Pubmed]
  7. The expression of lactate transporters (MCT1 and MCT4) in heart and muscle. Bonen, A. European journal of applied physiology. (2001) [Pubmed]
  8. Thyroid hormone mediated changes in gene expression can be initiated by cytosolic action of the thyroid hormone receptor beta through the phosphatidylinositol 3-kinase pathway. Moeller, L.C., Cao, X., Dumitrescu, A.M., Seo, H., Refetoff, S. Nuclear receptor signaling [electronic resource] : the e-journal of NURSA. (2006) [Pubmed]
  9. Characterisation of human monocarboxylate transporter 4 substantiates its role in lactic acid efflux from skeletal muscle. Manning Fox, J.E., Meredith, D., Halestrap, A.P. J. Physiol. (Lond.) (2000) [Pubmed]
  10. The proton-linked monocarboxylate transporter (MCT) family: structure, function and regulation. Halestrap, A.P., Price, N.T. Biochem. J. (1999) [Pubmed]
  11. Expression of monocarboxylate transporter 4 in human platelets, leukocytes, and tissues assessed by antibodies raised against terminal versus pre-terminal peptides. Merezhinskaya, N., Ogunwuyi, S.A., Fishbein, W.N. Mol. Genet. Metab. (2006) [Pubmed]
  12. Mechanisms regulating tissue-specific polarity of monocarboxylate transporters and their chaperone CD147 in kidney and retinal epithelia. Deora, A.A., Philp, N., Hu, J., Bok, D., Rodriguez-Boulan, E. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  13. Immunogold cytochemistry identifies specialized membrane domains for monocarboxylate transport in the central nervous system. Bergersen, L., Rafiki, A., Ottersen, O.P. Neurochem. Res. (2002) [Pubmed]
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