title: Distribution of monocarboxylate transporter isoforms MCT1, MCT2 and MCT4 in porcine muscles.
abstract: OBJECTIVE
  Monocarboxylate transporters (MCT), which cotransport lactate anions and protons across cell membranes, are important for regulation of muscle pH. We measured amounts of MCT1, MCT2 and MCT4 by immunoblotting in five different porcine muscles, to study MCT-isoform distribution both in oxidative and highly glycolytic muscles.
  
  
  METHODS
  Samples from the longissimus dorsi, gluteus superficialis, semimembranosus, infraspinatus and masseter were taken from 18 slaughtered pigs.
  
  
  RESULTS
  Oxidative capacity, estimated on the basis of the activities of lactate dehydrogenase (LDH), citrate synthase (CS) and 3-OH-acyl-CoA dehydrogenase (HAD), was highest in the infraspinatus and masseter, and was very low in the gluteus, semimembranosus and longissimus dorsi. In all muscles, the amount of MCT1 was small but variable. The amount of MCT2 was more abundant in the glycolytic than in the oxidative muscles, while MCT4 was found in equal amounts in all muscles. MCT2, but not MCT4, correlated negatively with CS and HAD.
  
  
  CONCLUSIONS
  The results together with measured concentrations of lactate suggest that MCT2 may function as the housekeeping lactate transporter, preventing acidification especially in highly glycolytic muscles in which the capacity to oxidize lactate is low. The results also support the view that, as in other species, MCT4 would be important at high lactate concentrations that occur during stress.
authors.affiliation: Department of Basic Veterinary Sciences, University of Helsinki, PO Box 57 (Hämeentie 57), FIN-00014 Helsinki, Finland.
authors.forename: K
authors.initials: K
authors.lastname: Sepponen
authors.forename: N
authors.initials: N
authors.lastname: Koho
authors.forename: E
authors.initials: E
authors.lastname: Puolanne
authors.forename: M
authors.initials: M
authors.lastname: Ruusunen
authors.forename: A R
authors.initials: AR
authors.lastname: Pösö
mesh_terms: D015094:3-Hydroxyacyl CoA Dehydrogenases / Q000378:metabolism; D000818:Animals; D015153:Blotting, Western / Q000379:methods; D002352:Carrier Proteins / Q000032:analysis; D002950:Citrate (si)-Synthase / Q000378:metabolism; D005260:Female; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D019344:Lactic Acid / Q000032:analysis; D008297:Male; D026901:Membrane Transport Proteins; D027501:Monocarboxylic Acid Transporters / Q000032:analysis*; D018482:Muscle, Skeletal / Q000201:enzymology / Q000378:metabolism*; D013552:Swine; D027981:Symporters / Q000032:analysis; D000099233:Monocarboxylate Transport Protein 1
chemical_list: D015094:3-Hydroxyacyl CoA Dehydrogenases; D002352:Carrier Proteins; D002950:Citrate (si)-Synthase; D007770:L-Lactate Dehydrogenase; D019344:Lactic Acid; D026901:Membrane Transport Proteins; D027501:Monocarboxylic Acid Transporters; D027981:Symporters; D000099233:Monocarboxylate Transport Protein 1; C491393:Mct3 protein, rat; C490427:SLC16A7 protein, human