The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Slc16a1  -  solute carrier family 16 (monocarboxylate...

Rattus norvegicus

Synonyms: MCT 1, MCT1, Mct1, Monocarboxylate transporter 1, RATMCT1, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Slc16a1


High impact information on Slc16a1

  • Adenovirus-mediated overexpression of MCT-1 increased lactate transport activity 3.7-fold in INS-1 cells [6].
  • Adenovirus-mediated overexpression of MCT-1 caused an increase in pyruvate oxidation and conferred pyruvate-stimulated insulin release to isolated rat islets [6].
  • In this study the significance of these characteristics was explored by overexpressing type A LDH (LDH-A) and/or type 1 MCT (MCT-1) in the clonal INS-1 beta cells and isolated rat islets [6].
  • The data demonstrate the direct modulation of MCT1 kinetic function in cerebral endothelial cells by agents known to affect the beta-adrenergic receptor/adenylyl cyclase/cAMP/protein kinase A intracellular signaling pathway [1].
  • MCT1-independent intracellular pH control mechanisms did not contribute to the forskolin or H89 effects on MCT1 kinetic function as determined with amiloride, monocarboxylate-independent acid loading, or the transport inhibitor alpha-cyano-4-hydroxycinnamate [1].

Chemical compound and disease context of Slc16a1


Biological context of Slc16a1


Anatomical context of Slc16a1


Associations of Slc16a1 with chemical compounds

  • Comparison of lactate transport in astroglial cells and monocarboxylate transporter 1 (MCT 1) expressing Xenopus laevis oocytes. Expression of two different monocarboxylate transporters in astroglial cells and neurons [12].
  • Furthermore, the cellular uptake of benzoic acid, a representative substrate of MCT1, was significantly (p<0.05) enhanced following the activation of IGF-IR via the pre-incubation with IGF-I (10 ng/ml) [15].
  • This process was reduced by a protonophore, carbonylcyanide p-trifluoromethoxyphenylhydrazone, and a typical monocarboxylate transporter (MCT) inhibitor, alpha-cyano-4-hydroxycinnamic acid, suggesting that nicotinate uptake by rat astrocytes is mediated by H(+)-coupled monocarboxylate transport system [14].
  • The distribution of MCT2 transporters within the individual postsynaptic densities mimicked that of the delta2 glutamate receptor, as shown by use of two different gold-particle sizes [9].
  • Differences in stereoselectivity were also detected; both carriers showed a lower Km for L-lactate than D-lactate, while hepatocyte MCT exhibited a lower Km for D- than L-2-chloropropionate and for L- than D-3-hydroxybutyrate; this is not the case for MCT1 [10].

Other interactions of Slc16a1


Analytical, diagnostic and therapeutic context of Slc16a1


  1. Modulation of monocarboxylic acid transporter-1 kinetic function by the cAMP signaling pathway in rat brain endothelial cells. Smith, J.P., Drewes, L.R. J. Biol. Chem. (2006) [Pubmed]
  2. Expression of monocarboxylic acid transporters (MCT) in brain cells. Implication for branched chain alpha-ketoacids transport in neurons. Mac, M., Nałecz, K.A. Neurochem. Int. (2003) [Pubmed]
  3. Changes in MCT 1, MCT 4, and LDH expression are tissue specific in rats after long-term hypobaric hypoxia. McClelland, G.B., Brooks, G.A. J. Appl. Physiol. (2002) [Pubmed]
  4. Vagal complex monocarboxylate transporter-2 expression during hypoglycemia. Vavaiya, K.V., Paranjape, S.A., Patil, G.D., Briski, K.P. Neuroreport (2006) [Pubmed]
  5. Cellular and subcellular expression of the monocarboxylate transporter MCT1 in rat heart. A high-resolution immunogold analysis. Jóhannsson, E., Nagelhus, E.A., McCullagh, K.J., Sejersted, O.M., Blackstad, T.W., Bonen, A., Ottersen, O.P. Circ. Res. (1997) [Pubmed]
  6. Overexpression of monocarboxylate transporter and lactate dehydrogenase alters insulin secretory responses to pyruvate and lactate in beta cells. Ishihara, H., Wang, H., Drewes, L.R., Wollheim, C.B. J. Clin. Invest. (1999) [Pubmed]
  7. Brain lactate is an obligatory aerobic energy substrate for functional recovery after hypoxia: further in vitro validation. Schurr, A., Payne, R.S., Miller, J.J., Rigor, B.M. J. Neurochem. (1997) [Pubmed]
  8. Induction of Fos immunoreactivity labeling in rat forebrain metabolic loci by caudal fourth ventricular infusion of the monocarboxylate transporter inhibitor, alpha-cyano-4-hydroxycinnamic acid. Briski, K.P., Patil, G.D. Neuroendocrinology (2005) [Pubmed]
  9. A novel postsynaptic density protein: the monocarboxylate transporter MCT2 is co-localized with delta-glutamate receptors in postsynaptic densities of parallel fiber-Purkinje cell synapses. Bergersen, L., Waerhaug, O., Helm, J., Thomas, M., Laake, P., Davies, A.J., Wilson, M.C., Halestrap, A.P., Ottersen, O.P. Experimental brain research. Experimentelle Hirnforschung. Expérimentation cérébrale. (2001) [Pubmed]
  10. The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver cells determined using the fluorescent intracellular pH indicator, 2',7'-bis(carboxyethyl)-5(6)-carboxyfluorescein. Jackson, V.N., Halestrap, A.P. J. Biol. Chem. (1996) [Pubmed]
  11. Interaction with antigen-specific T cells regulates expression of the lactate transporter MCT1 in primary rat astrocytes: specific link between immunity and homeostasis. Korn, T., Magnus, T., Jung, S. Glia (2005) [Pubmed]
  12. Comparison of lactate transport in astroglial cells and monocarboxylate transporter 1 (MCT 1) expressing Xenopus laevis oocytes. Expression of two different monocarboxylate transporters in astroglial cells and neurons. Bröer, S., Rahman, B., Pellegri, G., Pellerin, L., Martin, J.L., Verleysdonk, S., Hamprecht, B., Magistretti, P.J. J. Biol. Chem. (1997) [Pubmed]
  13. Distribution of monocarboxylate transporters MCT1 and MCT2 in rat retina. Gerhart, D.Z., Leino, R.L., Drewes, L.R. Neuroscience (1999) [Pubmed]
  14. Functional characteristics of H+ -dependent nicotinate transport in primary cultures of astrocytes from rat cerebral cortex. Shimada, A., Nakagawa, Y., Morishige, H., Yamamoto, A., Fujita, T. Neurosci. Lett. (2006) [Pubmed]
  15. IGF-I receptor gene activation enhanced the expression of monocarboxylic acid transporter 1 in hepatocarcinoma cells. Kang, K.W., Jin, M.J., Han, H.K. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  16. Aluminum citrate uptake by immortalized brain endothelial cells: implications for its blood-brain barrier transport. Yokel, R.A., Wilson, M., Harris, W.R., Halestrap, A.P. Brain Res. (2002) [Pubmed]
  17. Effect of a myocardial volume overload on lactate transport in skeletal muscle sarcolemmal vesicles. Aschenbach, W.G., Brower, G.L., Talmadge, R.J., Dobson, J.L., Gladden, L.B. Am. J. Physiol. Regul. Integr. Comp. Physiol. (2001) [Pubmed]
  18. Transport activity of MCT1 expressed in Xenopus oocytes is increased by interaction with carbonic anhydrase. Becker, H.M., Hirnet, D., Fecher-Trost, C., Sültemeyer, D., Deitmer, J.W. J. Biol. Chem. (2005) [Pubmed]
  19. Cloning of the monocarboxylate transporter isoform MCT2 from rat testis provides evidence that expression in tissues is species-specific and may involve post-transcriptional regulation. Jackson, V.N., Price, N.T., Carpenter, L., Halestrap, A.P. Biochem. J. (1997) [Pubmed]
  20. Regulation of cytosolic pH and lactic acid release in mesangial cells overexpressing GLUT1. Lang, K.S., Mueller, M.M., Tanneur, V., Wallisch, S., Fedorenko, O., Palmada, M., Lang, F., Bröer, S., Heilig, C.W., Schleicher, E., Weigert, C. Kidney Int. (2003) [Pubmed]
WikiGenes - Universities