Hostname: page-component-586b7cd67f-gb8f7 Total loading time: 0 Render date: 2024-11-22T23:12:24.320Z Has data issue: false hasContentIssue false
  • English
  • Français

Mapping, tissue distribution and polymorphism of porcine genes encoding retinol binding proteins (RBP1 and RBP4)

Published online by Cambridge University Press:  27 June 2008

Gong Wei-Hua ,
Tang Zhong-Lin ,
Cui Wen-Tao ,
Yang Shu-Lin  and
Li Kui
Gong Wei-Hua
Affiliation:
Key Laboratory of Animal Genetics, Breeding and Reproduction, Ministry of Education, Huazhong Agricultural University, Wuhan 430070, China Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100094, China
Tang Zhong-Lin
Affiliation:
Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100094, China
Cui Wen-Tao
Affiliation:
Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100094, China
Yang Shu-Lin
Affiliation:
Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100094, China
Li Kui*
Affiliation:
Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100094, China
*
*Corresponding author. E-mail: [email protected]
Get access Rights & Permissions [Opens in a new window]

Abstract

Using the INRA – University of Minnesota porcine 7000 Rad Radiation Hybrid panel (IMpRH) containing 118 clones, porcine cellular retinol binding protein gene 1 (RBP1) and plasma retinol binding protein gene 4 (RBP4) were assigned to porcine chromosomes 13 and 14, respectively. The mRNA distributions of the two genes in adult Wuzhishan pig tissues (lung, skeletal muscle, spleen, heart, stomach, large intestine, lymph node, small intestine, liver, brain, kidney and fat) were examined. One single nucleotide polymorphism (SNP) was identified in Laiwu, Wuzhishan, Guizhou, Bama pig breeds and a Tongcheng experimental population and analysed using a polymerase chain reaction–restriction fragment length polymorphism (PCR–RFLP) method. Significant associations were found between different genotypes of A/G156 and maximum carcass length (LM), minimum carcass length (LN), haemoglobin (HGB), mean corpuscular volume haemoglobin (MCH), and day to slaughter weight (age) traits in the Tongcheng experimental population. This SNP locus might be used as a genetic marker in pig breeding and production.

Keywords

retinol binding proteingenotypesingle nucleotide polymorphism
Type
Research Papers
Information
Chinese Journal of Agricultural Biotechnology , Volume 5 , Issue 1 , April 2008 , pp. 61 - 65
Copyright
Copyright © China Agricultural University 2008

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

Footnotes

First published in Journal of Agricultural Biotechnology 2007, 15(5): 729–734

References

Budhu, AS and Noy, N (2002) Direct channeling of retinoic acid between cellular retinoic acid-binding protein II and retinoic acid receptor sensitizes mammary carcinoma cells to retinoic acid-induced growth arrest. Molecular and Cellular Biology 22(8): 2632–2641.CrossRefGoogle ScholarPubMed
Chambon, P (1996) A decade of molecular biology of retinoic acid receptors. The Journal of the Federation of American Societies for Experimental Biology 10(9): 940–954.CrossRefGoogle ScholarPubMed
Folli, C, Calderone, V, Ottonello, S, Bolchi, A, Zanotti, G, Stoppini, M and Berni, R (2001) Identification, retinoid binding, and x-ray analysis of a human retinol-binding protein. Proceedings of the National Academy of Sciences of the USA 98(7): 3710–3715.CrossRefGoogle ScholarPubMed
Folli, C, Calderone, V, Ramazzina, I, Zanotti, G and Berni, R (2002) Ligand binding and structural analysis of a human putative cellular retinol-binding protein. Journal of Biological Chemistry 277(44): 41970–41977.CrossRefGoogle ScholarPubMed
Goureau, A, Yerle, M, Schmitz, A, et al. (1996) Human and porcine correspondence of chromosome segments using bidirectional chromosome painting. Genomics 36(2): 252–262.CrossRefGoogle ScholarPubMed
Katska-Ksiazkiewicz, L, Lechniak-Cieslak, D, Korwin-Kossakowska, A, et al. (2006) Genetical and biotechnological methods of utilization of female reproductive potential in mammals. Reproductive Biology 6(Suppl. 1): 21–36.Google ScholarPubMed
Messer, LA, Wang, L, Yelich, J, Pomp, D, Geisert, RD and Rothschild, MF (1996) Linkage mapping of the retinol-binding protein 4 (RBP4) gene to porcine chromosome 14. Mammalian Genome 7(5): 396.CrossRefGoogle ScholarPubMed
Molotkov, A, Ghyselinck, NB, Chambon, P and Duester, G (2004) Opposing actions of cellular retinol-binding protein and alcohol dehydrogenase control the balance between retinol storage and degradation. Biochemical Journal 383(Pt 2): 295–302.CrossRefGoogle ScholarPubMed
Orlandi, A, Francesconi, A, Clement, S, Ropraz, P, Spagnoli, LG and Gabbiani, G (2002) High levels of cellular retinol binding protein-1 expression in leiomyosarcoma: Possible implications for diagnostic evaluation. Virchows Archive 441(1): 31–40.CrossRefGoogle ScholarPubMed
Quadro, L, Blaner, WS, Hamberger, L, et al. (2004) The role of extrahepatic retinol binding protein in the mobilization of retinoid stores. The Journal of Lipid Research 45(11): 1975–1982.CrossRefGoogle ScholarPubMed
Rothschild, MF, Messer, L, Day, A, et al. (2000) Investigation of the retinol-binding protein 4 (RBP4) gene as a candidate gene for increased litter size in pigs. Mammalian Genome 11: 75–77.CrossRefGoogle ScholarPubMed
Saari, JC, Nawrot, M, Garwin, GG, et al. (2002) Analysis of the visual cycle in cellular retinol-binding protein type I (CRBPI) knockout mice. Investigative Ophthalmology and Visual Science 43(6): 1730–1735.Google ScholarPubMed
Thompson, CL, Blaner, WS, Van Gelder, RN, et al. (2001) Preservation of light signaling to the suprachiasmatic nucleus in vitamin A-deficient mice. Proceedings of the National Academy of Sciences of the USA 98(20): 11708–11713.CrossRefGoogle Scholar
Vogel, S, Mendelsohn, CL, Mertz, JR, et al. (2001) Characterization of a new member of the fatty acid-binding protein family that binds all-trans-retinol. Journal of Biological Chemistry 276(2): 1353–1360.CrossRefGoogle ScholarPubMed
Wang, H, Zhu, ZM, Yang, SL, Mo, DL and Li, K (2006a) Characterization of different expression patterns of calsarcin-1 and calsarcin-2 in porcine muscle. Gene 374: 104–111.CrossRefGoogle ScholarPubMed
Wang, HL, Wang, H, Zhu, ZM, et al. (2006b) Subcellular localization, expression patterns, SNPs and association analyses of the porcine HUMMLC2B gene. Molecular Genetics and Genomics 276(3): 264–272.CrossRefGoogle ScholarPubMed
Wang, YF, Yang, J, Yu, M, et al. (2005) Polymorphism detection of porcine PSMC3, PSMC6, and PSMD3 genes and their association with partial growth, carcass traits, meat quality, and immune traits. Canadian Journal of Animal Science 85: 475–480.CrossRefGoogle Scholar
Wendler, CC, Schmoldt, A, Flentke, GR, et al. (2003) Increased fibronectin deposition in embryonic hearts of retinol-binding protein-null mice. Circulation Research 92(8): 920–928.CrossRefGoogle ScholarPubMed
Yang, Q, Graham, TE, Mody, N, et al. (2005) Serum retinol binding protein 4 contributes to insulin resistance in obesity and type 2 diabetes. Nature 436(7049): 356–362.CrossRefGoogle ScholarPubMed
Yerle, M, Pinton, P, Robic, A, et al. (1998) Construction of a whole-genome radiation hybrid panel for high-resolution gene mapping in pigs. Cytogenetics and Cell Genetics 82(3–4): 182–188.CrossRefGoogle ScholarPubMed
Yu, M, Wang, Y, Pas, MFWT, et al. (2004) Investigation of the porcine PA28 activator γ-subunit (PSME3) genes: isolation, polymorphism and its chromosomal localization. Journal of Animal Breeding and Genetics 121(2): 142–148.CrossRefGoogle Scholar