Changes in glycosylated proteins in colostrum and mature milk and their implication.
IgA
colostrum
glycoproteins
host defense
mature milk
Journal
Frontiers in nutrition
ISSN: 2296-861X
Titre abrégé: Front Nutr
Pays: Switzerland
ID NLM: 101642264
Informations de publication
Date de publication:
2023
2023
Historique:
received:
08
02
2023
accepted:
26
05
2023
medline:
3
7
2023
pubmed:
3
7
2023
entrez:
3
7
2023
Statut:
epublish
Résumé
Glycosylation is one of the essential post-translational modifications that influences the function of milk proteins. In the present study, 998 proteins and 764 glycosylated sites from 402 glycoproteins were identified in human milk by TMT labeling proteomics. Compared to human milk proteins, the glycoproteins were mainly enriched in cell adhesion, proteolysis, and defense/immune process. The abundance of 353 glycosylated sites and their 179 parent proteins was quantified. After normalization to their parent protein's abundance, 78 glycosylated sites in 56 glycoproteins and 10 glycosylated sites in 10 glycoproteins were significantly higher in colostrum and mature milk, respectively. These changed glycoproteins were mainly related to host defense. Intriguingly, one glycosylated site (Asp144) in IgA and two glycosylated sites (Asp38 and Asp1079) in tenascin are significantly upregulated even though their protein abundance was downregulated during lactation. This study helps us figure out the critical glycosylated sites in proteins that might influence their biological function in an unbiased way.
Identifiants
pubmed: 37396121
doi: 10.3389/fnut.2023.1161310
pmc: PMC10311556
doi:
Types de publication
Journal Article
Langues
eng
Pagination
1161310Informations de copyright
Copyright © 2023 Lu, Zhang, Ma, Pang, Dai, Zhu, Liu, Xing, Zhang and Lv.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
Références
Nucleic Acids Res. 2022 Jul 5;50(W1):W216-W221
pubmed: 35325185
Curr Biol. 2019 Apr 1;29(7):R229-R231
pubmed: 30939300
Cell. 1986 Oct 10;47(1):131-9
pubmed: 2428505
J Nutr. 2019 Aug 1;149(8):1317-1325
pubmed: 31098625
Cancer Cell. 2019 Jul 8;36(1):6-16
pubmed: 31287993
Cell. 1996 Feb 9;84(3):345-57
pubmed: 8608588
Glycoconj J. 2012 Dec;29(8-9):599-607
pubmed: 22565826
Food Chem. 2019 Mar 15;276:266-273
pubmed: 30409594
Ann Clin Biochem. 1975 Mar;12(2):48-50
pubmed: 15637923
J Agric Food Chem. 2017 Nov 29;65(47):10360-10367
pubmed: 29110469
Br J Nutr. 2013 Jul 14;110(1):105-15
pubmed: 23182305
Anal Bioanal Chem. 2018 Jan;410(3):1019-1027
pubmed: 28948319
Int J Mol Sci. 2017 Apr 20;18(4):
pubmed: 28425960
Appl Environ Microbiol. 2016 May 31;82(12):3622-3630
pubmed: 27084007
J Agric Food Chem. 2010 May 26;58(10):6440-8
pubmed: 20415418
Mol Cell Proteomics. 2012 Jun;11(6):M111.015248
pubmed: 22261723
J Agric Food Chem. 2021 Jun 16;69(23):6690-6700
pubmed: 34087070
Eur J Biochem. 2004 Feb;271(4):678-84
pubmed: 14764083
Mol Cell Proteomics. 2019 Nov;18(11):2165-2177
pubmed: 31409668
Int J Mol Sci. 2016 Nov 25;17(12):
pubmed: 27898009
Mol Cell Proteomics. 2012 Sep;11(9):775-85
pubmed: 22745059
J Biol Chem. 2010 Nov 26;285(48):37293-301
pubmed: 20855890
Cancer Res. 2001 Dec 1;61(23):8586-94
pubmed: 11731446
Nucleic Acids Res. 2013 Jan;41(Database issue):D377-86
pubmed: 23193289
Proc Natl Acad Sci U S A. 2013 Nov 5;110(45):18220-5
pubmed: 24145401
Cell Adh Migr. 2015;9(1-2):48-82
pubmed: 25482829
Food Funct. 2018 Feb 21;9(2):1163-1172
pubmed: 29363704
J Autoimmun. 2015 Feb;57:1-13
pubmed: 25578468
Cells. 2020 Aug 28;9(9):
pubmed: 32872358
Genome Res. 2003 Sep;13(9):2129-41
pubmed: 12952881