Evidence map›Paper›PMID 37396121›Full record

ArticleFrontiers in nutrition2023

Changes in glycosylated proteins in colostrum and mature milk and their implication.

Jing Lu, Wenyuan Zhang, Changlu Ma, Xiaoyang Pang, Ying Dai, Tong Zhu, Jinqi Liu, Lina Xing, Shuwen Zhang, Jiaping Lv

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in nutrition, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Jing LuBeijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Engineering and Technology Research Center of Food Additives, School of Food and Health, Beijing Technology and Business University, Beijing, China.
Wenyuan ZhangInstitute of Food Science and Technology, Chinese Academy of Agricultural Science, Beijing, China.
Changlu MaDepartment of Food and Bio-Engineering, Beijing Vocational College of Agriculture, Beijing, China.
Xiaoyang PangInstitute of Food Science and Technology, Chinese Academy of Agricultural Science, Beijing, China.
Ying DaiBeijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Engineering and Technology Research Center of Food Additives, School of Food and Health, Beijing Technology and Business University, Beijing, China.
Tong ZhuBeijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Engineering and Technology Research Center of Food Additives, School of Food and Health, Beijing Technology and Business University, Beijing, China.
Jinqi LiuBeijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Engineering and Technology Research Center of Food Additives, School of Food and Health, Beijing Technology and Business University, Beijing, China.
Lina XingBeijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Engineering and Technology Research Center of Food Additives, School of Food and Health, Beijing Technology and Business University, Beijing, China.
Shuwen ZhangInstitute of Food Science and Technology, Chinese Academy of Agricultural Science, Beijing, China.
Jiaping LvInstitute of Food Science and Technology, Chinese Academy of Agricultural Science, Beijing, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Introduction: Glycosylation is one of the essential post-translational modifications that influences the function of milk proteins. Methods: 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. Results: 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. Discussion: This study helps us figure out the critical glycosylated sites in proteins that might influence their biological function in an unbiased way.

Indexed as

colostrumglycoproteinshost defenseIgAmature milk

Identifiers

PMID37396121
PMCPMC10311556

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.