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Collagens XII and XIV: Two collagen types both associated with bovine muscle and intramuscular lipid metabolism

Listrat, A., Pissavy, A.L., Micol, D., Jurie, C., Lethias, C., Pethick, D.W.ORCID: 0000-0002-3255-7677 and Hocquette, J.F. (2016) Collagens XII and XIV: Two collagen types both associated with bovine muscle and intramuscular lipid metabolism. Livestock Science, 187 . pp. 80-86.

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In continental Europe, intramuscular fat (IMF) content in beef is low but plays a key role in determining flavor. IMF expands inside the extracellular matrix (ECM) of intramuscular connective tissue. This ECM contains among others, collagens XII and XIV, two minor collagens probably involved in muscle metabolism. So, our purpose was to determine if there was an association between the contents in collagens XII and XIV and muscle metabolism. Rectus abdominis (RA, oxidative) and Semitendinosus (ST, oxido-glycolytic) muscles were sampled from steers of two genotypes with high (Angus [Ang], n=10) or low (Limousine [Lim], n=10) intramuscular fat level. Collagens XII and XIV relative abundance was evaluated by Western blot analysis. The characteristic parameters of metabolism were previously measured. Ang muscles contained more collagen XIV than Lim muscles (p<0.001). RA muscle contained more collagen XII than ST muscle (p<0.01). Across the two breeds and muscles, collagen XII was positively correlated with A- and H-fatty acid binding protein (FABP) contents (+0.43 and +0.53, respectively, p<0.05) and activities of three oxidative enzymes (cytochrome-c oxidase: +0.41, isocitrate dehydrogenase [ICDH]: +0.40, citrate synthase [CS]: +0.32) (p<0.05) and collagen XIV was positively correlated with triacylglycerol content (+0.35, p<0.35), A- and H-FABP protein contents (+0.35 and +0.38, respectively, p<0.05) and ICDH (+0.34, p<0.05) and negatively with activities of two enzymes of glycolytic metabolism (phosphofructokinase: -0.31 and lactate dehydrogenase: -0.42, p<0.05). After removing the genotype and muscle effects, only collagen XII remained correlated with A- and H-FABP and CS activity (+0.30, +0.34 and +0.46, respectively, p<0.0505). H-FABP is expressed in various tissues but predominantly in cardiac and oxidative skeletal muscles, whereas A-FABP is exclusively expressed within adipocytes. From these results, we can conclude that collagen XII and XIV are both associated with bovine muscle fiber and intramuscular lipid metabolism, but probably by different mechanisms. As a matter of fact, collagens XII is associated with intramuscular fat differentiation (from its correlation with A-FABP content) and oxidative metabolism (from its correlation with H-FABP content and CS activities) regardless of breed and muscle, whereas type XIV collagen is associated with the same parameters plus enzymes of glycolytic metabolism that discriminate breeds.

Item Type: Journal Article
Murdoch Affiliation(s): School of Veterinary and Life Sciences
Publisher: Elsevier BV
Copyright: © 2016 Elsevier B.V.
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