The cationic amino acid transporter (CAT) protein family transports lysine and arginine in cellular amino acid pools. We hypothesized that CAT expression changes in pig skeletal muscles during rapid pig postnatal development. We aimed to investigate the tissue distribution and changes in the ontogenic expression of CATs in pig skeletal muscles during postnatal development. Six piglets at 1, 12, 26, 45, and 75 days old were selected from six litters, and their longissimus dorsi (LD), biceps femoris (BF), and rhomboideus (RH) muscles, and their stomach, duodenum, jejunum, ileum, colon, liver, kidney, heart, and cerebrum were collected. CAT-1 was expressed in all the 12 tissues investigated. CAT-2 (CAT-2A isoform) expression was highest in the skeletal muscle and liver and lowest in the jejunum, ileum, kidney, and heart. CAT-3 was expressed mainly in the colon and detected in the jejunum, ileum, and cerebrum. The CAT-1 expression was higher in the skeletal muscle of day 1 pigs than in that of older pigs (P < 0.05). The CAT-2 mRNA level was lowest at day 1, but increased with postnatal development (P < 0.05). There was no significant change in CAT-1 expression among the LD, BF, and RH during postnatal development (P > 0.05); however, there was a change in CAT-2 expression. The CAT-2 expression was highest in the LD of 12-, 26-, 45-, and 75-day-old pigs, followed by the BF and RH (P < 0.05). These results suggest that CAT-1 and CAT-2 play different roles in pig skeletal muscles during postnatal development.
Cationic amino acid transporter Pig Postnatal development Skeletal muscle
This is a preview of subscription content, log in to check access
The authors are grateful to the animal care team of the Pig Unit of NARO for the care of the pigs and support for the sample collections. Part of this work was previously published as an abstract and presented as a poster at the 4th EAAP International Symposium on Energy and Protein Metabolism and Nutrition, 9–12 September, California, USA (Ishida et al. 2013). In this research, we used the supercomputer of the Agriculture, Forestry and Fisheries Research IT (AFFRIT), Ministry of Agriculture, Forestry, and Fisheries (MAFF), Japan.
Compliance with ethical standards
Conflict of interest
The authors declare that they have no conflicts of interest.
All procedures performed in studies involving animals were in accordance with the ethical standards of the institution or practice at which the studies were conducted.
This work was partially supported by a Grant-in-Aid for Young Scientists (B) (Grant No. 26850170) from the Ministry of Education, Science and Culture, Japan.
Closs EI, Lyons CR, Kelly C, Cunningham JM (1993) Characterization of the third member of the MCAT family of cationic amino acid transporters. Identification of a domain that determines the transport properties of the MCAT proteins. J Biol Chem 268:20796–20800PubMedGoogle Scholar
Closs EI, Gräf P, Habermeier A, Cunningham JM, Förstermann U (1997) Human cationic amino acid transporters hCAT-1, hCAT-2A, and hCAT-2B: three related carriers with distinct transport properties. Biochemistry 36:6462–6468. doi:10.1021/bi962829pCrossRefPubMedGoogle Scholar
Harrison AP, Latorre R, Dauncey MJ (1997) Postnatal development and differentiation of myofibres in functionally diverse porcine skeletal muscles. Reprod Fertil Dev 9:731–740. doi:10.1071/R97026CrossRefPubMedGoogle Scholar
Humphrey BD, Stephensen CB, Calvert CC, Klasing KC (2004) Glucose and cationic amino acid transporter expression in growing chickens (Gallus gallus domesticus). Comp Biochem Physiol Part A Mol Integr Physiol 138:515–525. doi:10.1016/j.cbpb.2004.06.016CrossRefGoogle Scholar
Ishida A, Kyoya T, Nakashima K, Katsumata M (2011) Muscle protein metabolism during compensatory growth with changing dietary lysine levels from deficient to sufficient in growing rats. J Nutr Sci Vitaminol 57:401–408CrossRefPubMedGoogle Scholar
Ishida A, Ashihara A, Nakashima K, Katsumata M (2013) Expression of amino acid transporter in porcine skeletal muscles during postnatal development. EAAP publication No. 134, pp 395–396 (abs.)Google Scholar
Karlsson A, Enfalt AC, Essen-Gustavsson B, Lundstrom K, Rydhmer L, Stern S (1993) Muscle histochemical and biochemical properties in relation to meat quality during selection for increased lean tissue growth rate in pigs. J Anim Sci 71:930–938. doi:10.2527/1993.714930xCrossRefPubMedGoogle Scholar
Katsumata M, Yamaguchi T, Ishida A, Ashihara A (2017) Changes in muscle fiber type and expression of mRNA of myosin heavy chain protein isoforms in porcine muscle during pre and postnatal development. Anim Sci J 88:364–371. doi:10.1111/asj.12641CrossRefPubMedGoogle Scholar
Kattesh HG, Charles SF, Baumbach GA, Gillespie BE (1990) Plasma cortisol distribution in the pig from birth to six weeks of age. Biol Neonate 58:220–226CrossRefPubMedGoogle Scholar
Stathopulos PB, Lu X, Shen J et al (2001) Increased l-arginine uptake and inducible nitric oxide synthase activity in aortas of rats with heart failure. Am J Physiol Heart Circ Physiol 280:H859–H867PubMedGoogle Scholar
Vandesompele J, De Preter K, Pattyn F, Poppe B, Van Roy N, De Paepe A, Speleman F (2002) Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol 3:RESEARCH0034CrossRefPubMedPubMedCentralGoogle Scholar
Zhi A, Feng D, Zhou X et al (2008) Molecular cloning, tissue distribution and segmental ontogenetic regulation of b[0, +] amino acid transporter in lantang pigs. Asian Aust J Anim Sci 21:9CrossRefGoogle Scholar
Zou S, Zhi A, Zhou X et al (2009) Molecular cloning, segmental distribution and ontogenetic regulation of cationic amino acid transporter 2 in pigs. Asian Aust J Anim Sci 22:712–720CrossRefGoogle Scholar
Zuo J, Xia W, Xu M et al (2013) Molecular cloning, tissue distribution and expression of the porcine cationic amino acid transporter CAT3. J Anim Vet Adv 12:1070–1077. doi:10.3923/javaa.2013.1070.1077Google Scholar