Explore the lactation function of Protein phosphorylation sites in goat mammary tissues by phosphoproteome

ABSTRACT: Background: Protein phosphorylation plays an important role in lactation. Differentially modified phosphorylation sites between peak lactation (PL, 90 days postpartum) and late lactation (LL, 280 days postpartum) were investigated using an integrated approach, namely, liquid chromatography with tandem mass spectrometry (LC-MS/MS) and tandem mass tag (TMT) labelling, to know the molecular changes in different stages of goat mammary tissues. Results: A total of 1,938 (1,111 up-regulated, 827 down-regulated) differentially modified phosphorylation sites of 1,172 proteins were identified (P values < 0.05 and fold change of phosphorylation ratios > 1.5). In addition, the Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analysis showed that calcium signalling pathway, oxytocin signalling pathway and MAPK signalling pathway were enriched. The results of western blot showed phosphorylation levels of ACACA, EIF4EBP1 and IRS1 increased and JUN decreased in PL compared with LL. The results were consistent with the results of phosphoproteome. Conclusions: In this study, we first differentially proteins modified phosphorylation sites between PL and LL in goat mammary tissues. On the other hand, these results analysis indicate that multiple differentially modified phosphorylation sites of FASN, ACACA, mTOR, PRKAA, IRS1, RPS6KB, EIF4EBP1, TSC2 and proteins of Calcium signalling pathway, Oxytocin signalling pathway, and MAPK signalling pathway are worthy of further exploration.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Capra Hircus (goat)

SUBMITTER: Xiaopeng An  

LAB HEAD: Xiaopeng An

PROVIDER: PXD026437 | Pride | 2022-02-17

REPOSITORIES: Pride