Bovine αs2-casein D is generated by exon VIII skipping

Bouniol, Christine; Printz, Christiane; Mercier, Jean‐Claude

doi:10.1016/0378-1119(93)90577-p

Cited by 25 publications

(12 citation statements)

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“…Dephosphorylated forms can also be distinguished from native caseins by RP-HPLC analysis, where the loss of hydrophilic groups leads to stronger interactions [15,36]. This was also veri¢ed for variant D of Ks2-casein which lacks sequence 51^59, which includes a major phosphorylation site [37,38]. However, chromatographic behavior during anion exchange chromatography was more complex.…”

Section: Discussionmentioning

confidence: 99%

Post‐translational phosphorylation affects the IgE binding capacity of caseins

et al. 2000

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IgE response specific to those molecular regions of casein that contain a major phosphorylation site was analyzed using native and modified caseins and derived peptides. This study included (i) the naturally occurring common variants A1 and A from L L-and K Ks2-caseins, respectively, which were purified in the native form and then dephosphorylated, (ii) a purified rare variant D of K Ks2-casein which lacks one major phosphorylation site, and (iii) the native and dephosphorylated tryptic fragment f(1^25) from L L-casein. Direct and indirect ELISA using sera from patients allergic to milk showed that the IgE response to caseins is affected by modifying or eliminating the major phosphorylation site.z 2000 Federation of European Biochemical Societies.

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Section: Discussionmentioning

confidence: 99%

Post‐translational phosphorylation affects the IgE binding capacity of caseins

et al. 2000

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“…a,,-casein also exists, in caprine and ovine milks, as two non-allelic forms arising from alternative skipping of exon 6 during the processing of pre-messengers (Boisnard et al, 1991). Thus, complete exon skipping due to mutations occurring within consensus splice site sequences of a,,-, and even (human) p-casein is now well documented Menon et al, 1992;Bouniol et al, 1993;Mohr et al, 1994;Martin and Leroux, 1994). Therefore, it would be worthwhile to investigate if alternative exon splicing occurs in /%casein and K--casein genes, which would further add to the complexity of the casein fraction; this has not yet been reported.…”

Section: Discussionmentioning

confidence: 99%

Differential Splicing of Pre‐Messenger RNA Produces Multiple Forms of Mature Caprine α_s1‐Casein

Ferranti

Addeo

Malorni³

et al. 1997

European Journal of Biochemistry

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The identity of multiple forms of caprine a,,-casein in variants A, B, and C has been determined by structural characterisation using mass spectrometry, automated Edman degradation and peptide mapping. Mature goat a,,-casein exists as a mixture of at least four molecular species which differ in peptide chain length. The main component corresponds to the 199-residues form already described. The other three, in lesser amounts, were shorter forms of a,,-casein and differed for the deleted peptides 141 -148, as shown previously for ovine a,,-casein, peptide 110-1 17, or Gln78. Analysis of a,,-casein mRNA from milk somatic cells demonstrated that these forms originated from skipping events at the level of exon 13 (codifying for peptide 210-117) and 16 (codifying for peptide 141-148) and from the presence of a cryptic splice site within exon 11 (whose first CAG triplet encodes Gln78) during primary transcript processing. The finding of these splicing abnormalities in the three common variants A, B, and C suggests that this is a general feature of a,,-casein in goat.A further source of heterogeneity of caprine a,,-casein was identified in the discrete phosphorylation of seryl residues. Eight serine residues (at positions 44, 46, 64 to 68 and 75) are fully phosphorylated (except in variant A because of the replacement Glu77-+Gln which prevents phosphorylation of Ser7.5). Conversely, SerllS and Ser41 are phosphorylated only to about SO% and 20%, respectively. Ser12, although located in a consensus triplet, is never phosphorylated, similarly to the ovine a,,-casein variants.These results confirm that there are stabilised mechanisms of simultaneous synthesis of a,,-casein at different length and of post-translational modification in both caprine and ovine species.Keywords: a,,-casein ; phosphorylation ; differential splicing ; non-allelic deletion ; polymorphism Previous studies performed on the goat milk protein fraction have shown an extensive qualitative polymorphism of a,,-casein, associated with quantitative variation (Boulanger et al., 1984; Grosclaude et a]., 1987). The most recent genoinic data showed the existence of at least 14 autosomal alleles at the goat a5,-casein locus, distributed in seven different classes of protein variants associated with four levels of expression, ranging between 0 (a,,-Cad) and 3.6 g/l (a,,-CasA, B and C)/allele (Martin, 1993;Martin and Leroux, 1994). a,,-casein A, B, C and E variants differ from each other by amino acid substitutions, while a,,-casein D, F and G variants, associated with a low level of protein synthesis, are internally deleted (Brignon et al., 1989(Brignon et al., , 1990. The establishment of the overall organisation of the goat a,,-casein gene (19 exons scattered along 17 kb), the characterisation of alleles F Martin and Leroux, 1994) and E (Jansa Perez et al., 1994) at the genomic level as well as a detailed analysis of their transcription products demonstrated that the deletion occurring within variant F arises from the outsplicing of three exons (9, 10, and 11)...

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“…Since the initial discovery of polymorphism of the whey protein, β-lactoglobulin (-Lg) and a quantitative distribution of its variants (Aschaffenburg & Drewry, 1955;1957) researchers have become interested in the genetic polymorphism of milk proteins. It is known today that there are at least 39 genetic variants of six milk protein fractions (Eigel et al, 1984;Bouniol et al, 1993;Miranda et al, 1993;Mariani et al, 1995;Visser et al, 1995;Godovac-Zimmermann et al, 1996;Prinzenberg et al, 1996;1998;Han et al, 2000). These genetic variants occur as a consequence of either substitution or deletion of amino acids within the polypeptide chain (Eigel et al, 1984).…”

Section: Introductionmentioning

confidence: 99%

Effects of genetic variants in milk protein on yield and composition of milk from Holstein-Friesian and Simmentaler cows

Çardak¹

2007

SA J. An. Sci.

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Milk samples from 237 Holstein-Friesian (HF) and 177 Simmentaler cows in six herds were typed for genetic variants of α S1 -, β-and κ-caseins (Cn) and β-lactoglobulin (-Lg) using ultrathin-layer polyacrylamide isoelectric focusing in the presence of carrier ampholytes (3-10 pH). The frequency distribution of genetic variants of all four milk protein systems was different in HF and Simmentaler. In addition, milk production

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Bovine αs2-casein D is generated by exon VIII skipping

Cited by 25 publications

References 24 publications

Post‐translational phosphorylation affects the IgE binding capacity of caseins

Post‐translational phosphorylation affects the IgE binding capacity of caseins

Differential Splicing of Pre‐Messenger RNA Produces Multiple Forms of Mature Caprine α_s1‐Casein

Effects of genetic variants in milk protein on yield and composition of milk from Holstein-Friesian and Simmentaler cows

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Bovine αs2-casein D is generated by exon VIII skipping

Cited by 25 publications

References 24 publications

Post‐translational phosphorylation affects the IgE binding capacity of caseins

Post‐translational phosphorylation affects the IgE binding capacity of caseins

Differential Splicing of Pre‐Messenger RNA Produces Multiple Forms of Mature Caprine αs1‐Casein

Effects of genetic variants in milk protein on yield and composition of milk from Holstein-Friesian and Simmentaler cows

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Differential Splicing of Pre‐Messenger RNA Produces Multiple Forms of Mature Caprine α_s1‐Casein