Short communication Pig HDL-binding protein (HDLBP) genotype is associated with intramuscular fat percentage E. Cánovas a , R. Quintanilla b , B. Badaoui a , C. Porredón a , D. Gallardo a , R.N. Pena b , I. Díaz c , M. Amills a, ⁎ a Departament de Ciència Animal i dels Aliments, Universitat Autònoma de Barcelona, Bellaterra, 08193 Spain b Genètica i Millora Animal, IRTA, Lleida, 25198 Spain c Centre de Tecnologia de la Carn, IRTA,17121 Monells, Spain article info abstract Article history: Received 1 December 2008 Received in revised form 11 June 2009 Accepted 11 June 2009 High density lipoprotein binding protein (HDLBP) or vigilin is a molecule with a broad range of functions dealing with the maintenance of heterochromatin structure and the regulation of gene expression. There is evidence that HDLBP expression is modulated by the intracellular levels of cholesterol. Moreover, vigilin is differentially expressed in the macrophages and smooth muscle cells of atherosclerotic plaques with regard to those of nondiseased coronary intima. In this work, we have sequenced 98% of the coding region of the pig HDLBP gene. Sequence alignment allowed us to identify a c.3120GNA synonymous polymorphism at exon 23 that segregated in a commercial Duroc population. Performance of an association analysis with serum lipid levels and diverse fatness and carcass traits allowed us to identify an experiment- wide significant association between this polymorphism and intramuscular fat content of longissimus thoracis et lumborum muscle (P =0.0034). Moreover, we have detected a suggestive association between HDLBP genotype and ham weight (P = 0.0078). © 2009 Published by Elsevier B.V. Keywords: Lipids HDL-binding protein Vigilin Pig Intramuscular fat 1. Introduction High density lipoprotein binding protein (HDLBP), also known as vigilin, is a 110 kDa nuclear and cytoplasmic molecule that it is upregulated in response to increased intracellular levels of cholesterol (Fidge, 1999). Consistent with this finding, HDLBP expression has been detected in human non-endothelial cells of atherosclerotic arteries, particularly in those with lipid inclusions (Chiu et al., 1997). However, this protein lacks the structural domains and motifs that are typical of HDL receptors. In consequence, its precise role in lipid metabolism is currently unclear (Fidge, 1999). Recent evidences have demonstrated that HDLBP is deeply involved in the regulation of gene expression as well as in the maintenance of heterochromatin structure and chromosome segregation (Wang et al., 2005). The human HDLBP gene maps to 2q37, and contains 28 exons that encode at least four different transcripts named as HDLBP-001, -002, -003 and -201 (Ensembl database, http//:www. ensembl.org). Human vigilin contains 14 K-homology (KH) domains which are typical of RNA-binding proteins. This feature would explain its role in mRNA stability (Cunningham et al., 2000) as well as in the nucleocytoplasmatic export of tRNA (Kruse et al., 2000). Despite the crucial involvement of HDLBP on the modulation of gene expression, this locus has not been characterized in pigs so far. In the current work, we report the nucleotide sequence and polymorphism of the coding region of the pig HDLBP gene. Moreover, we have analysed whether genetic variation at this locus is associated with lipid metab- olism and production traits in a Duroc pig population. 2. Materials and methods 2.1. Amplification and sequencing of the pig HDLBP coding region Total RNA was extracted from liver samples corresponding to 12 pigs from Duroc (N = 8), Landrace (N =2) and Large White (N =2) breeds according to a protocol reported by Livestock Science 126 (2009) 298–301 ⁎ Corresponding author. Tel.: +34 93 5812876; fax: +34 93 581 2106. E-mail address: Marcel.Amills@uab.cat (M. Amills). 1871-1413/$ – see front matter © 2009 Published by Elsevier B.V. doi:10.1016/j.livsci.2009.06.005 Contents lists available at ScienceDirect Livestock Science journal homepage: www.elsevier.com/locate/livsci