|Title||The genetic background of bovine αs1- and αs2-casein phosphorylation|
|Source||University. Promotor(en): E. Verrier; Henk Bovenhuis, co-promotor(en): P. Martin; Marleen Visker. - Wageningen : Wageningen University - ISBN 9789463438148 - 141|
Animal Breeding and Genetics
|Publication type||Dissertation, internally prepared|
|Keyword(s)||dairy cattle - alpha-s1-casein - alpha-s2-casein - phosphorylation - milk composition - milk proteins - genetic variation - genetic factors - animal genetics - melkvee - alfa-s-1-caseïne - alfa-s-2-caseïne - fosforylering - melksamenstelling - melkeiwitten - genetische variatie - genetische factoren - diergenetica|
Phosphorylation of caseins (CN) is a crucial post-translational modification allowing caseins to aggregate as micelles. The formation and stability of casein micelles are important for transporting abundant minerals to the neonate and manufacturing of dairy products. Therefore, it is of great interest to explore variation in degrees of phosphorylation of caseins and study to what extent genetic and other factors contribute to this variation. This thesis aimed to investigate the genetic background of bovine milk protein composition with a focus on phosphorylation of αs1- and αs2-CN. Two studies were conducted to quantify phosphorylation levels of αs1- and αs2-CN: one in French Montbéliarde using liquid chromatography coupled with electrospray ionization mass spectrometry and the other in Dutch Holstein Friesian using capillary zone electrophoresis. In French Montbéliarde, in addition to the known isoforms αs1-CN-8P and-9P and αs2-CN-10P to -13P, three new phosphorylation isoforms were detected, namely αs2-CN-9P, αs2-CN-14P, and αs2-CN-15P. Relative concentrations of the phosphorylation isoforms varied considerably among cows. Phenotypic correlations showed that isoforms phosphorylated at higher degrees (αs1-CN-9P and αs2-CN-12P to -14P) correlated negatively with isoforms phosphorylated at lower degrees (αs1-CN-8P, αs2-CN-10P, and -11P). Furthermore, it was shown that αs1- and αs2-CN phosphorylation profiles changed across parity and lactation, and exploitable genetic variation for the phosphorylation degrees of αs1- and αs2-CN (defined as the proportion of higher-degree isoforms in αs1- and αs2-CN, respectively) exist. In Dutch Holstein Friesian, three αs2-CN isoforms, namely αs2-CN-10P to -12P, and the phosphorylation degrees of αs1- and αs2-CN were quantified. High intra-herd heritabilities were estimated for individual αs2-CN phosphorylation isoforms and the phosphorylation degrees of αs1- and αs2-CN (ranging from 0.54 to 0.89). This suggests that genetic factors contribute substantially to observed differences in αs1- and αs2-CN phosphorylation profiles. The highly positive correlation between the phosphorylation degrees of αs1- and αs2-CN (0.94) suggest that phosphorylation of αs1- and αs2-CN is related. Additionally, a total of 10 regions, distributed across Bos taurus autosomes (BTA) 1, 2, 6, 9, 11, 14, 15, 18, 24 and 28, were detected to be associated with individual αs1- and αs2-CN phosphorylation isoforms and their phosphorylation degrees. Regions on BTA1, 6, 11 and 14 were associated with multiple traits studied. Two quantitative trait loci (QTL) regions were detected on BTA1: one affecting αs2-CN production, and the other affecting αs1-CN PD and αs2-CN PD. The QTL region on BTA6 affected only individual αs2-CN isoforms. The QTL region on BTA11 and 14 affected relative concentrations of αs2-CN-10P and αs2-CN-11P, αs1-CN PD and αs2-CN PD. Results suggested that effects of identified genomic regions on αs1-CN PD and αs2-CN PD are probably due to changes in milk synthesis and phosphorus secretion in milk.