Evidence map›Paper›PMID 29464498›Full record

ArticleJournal of mammary gland biology and neoplasia2017

Milk Proteins Are Predigested Within the Human Mammary Gland.

Søren D Nielsen, Robert L Beverly, David C Dallas

Abstract read
In one paragraph

Article in Journal of mammary gland biology and neoplasia, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 13% of its field
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

23 citing papers in PubMed, 1 synthesis or guideline pooled it, 49 citations in OpenAlex.

  1. Guideline
  2. Article
  3. Review
  4. Bioactive milk peptides: an updated comprehensive overview and database.Critical reviews in food science and nutrition · 2024
    Review
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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

3 authors at 1 institution in 1 country.

Søren D NielsenNutrition Program, School of Biological and Population Health Sciences, College of Public Health and Human Sciences, Oregon State University, 118G Milam Hall, Corvallis, OR, 97331, USA.ORCID 0000-0002-6990-2200
Robert L BeverlyNutrition Program, School of Biological and Population Health Sciences, College of Public Health and Human Sciences, Oregon State University, 118G Milam Hall, Corvallis, OR, 97331, USA.
David C DallasNutrition Program, School of Biological and Population Health Sciences, College of Public Health and Human Sciences, Oregon State University, 118G Milam Hall, Corvallis, OR, 97331, USA. dave.dallas@oregonstate.edu.ORCID 0000-0002-9696-0967
Oregon State University · US

Funding

Deciphering the function of naturally occurring peptides in human milkR00HD079561 · NICHD · OREGON STATE UNIVERSITY · PI DALLAS, DAVID CHARLES · 2016 to 2018
$741k
Orbitrap Elite with ETDS10OD020111 · OD · OREGON STATE UNIVERSITY · PI MAIER, CLAUDIA S · 2015 to 2015
$600k
Deciphering the function of naturally occurring peptides in human milkK99HD079561 · NICHD · UNIVERSITY OF CALIFORNIA AT DAVIS · PI DALLAS, DAVID CHARLES · 2014 to 2015
$157k
Eunice Kennedy Shriver National Institute of Child Health and Human Development R00HD079561NICHD NIH HHS K99 HD079561NICHD NIH HHS R00 HD079561NIH HHS S10 OD020111
6 · The paper itself

Abstract

Previous work demonstrates that proteases present in human milk release hundreds of peptides derived from milk proteins. However, the question of whether human milk protein digestion begins within the mammary gland remains incompletely answered. The primary objective of this study was to determine whether proteolytic degradation of human milk proteins into peptides begins within the mammary gland. The secondary objectives were to determine which milk proteases participate in the proteolysis and to predict which released peptides have bioactivity. Lactating mothers (n = 4) expressed their milk directly into a mixture of antiproteases on ice followed by immediate freezing of the milk to limit post-expression protease activity. Samples were analyzed for their peptide profiles via mass spectrometry and database searching. Peptidomics-based protease prediction and bioactivity prediction were each performed with several different approaches. The findings demonstrate that human milk contains more than 1,100 unique peptides derived from milk protein hydrolysis within the mammary gland. These peptides derived from 42 milk proteins and included 306 potential bioactive peptides. Based on the peptidomics data, plasmin was predicted to be the milk protease most active in the hydrolysis of human milk proteins within the mammary gland. Milk proteases actively cleave milk proteins within the mammary gland, initiating the release of functional peptides. Thus, the directly breastfed infant receives partially pre-digested proteins and numerous bioactive peptides.

Indexed as

AdultBreast FeedingFemaleHumansLactationMammary Glands, HumanMilk, HumanMilk ProteinsPeptide HydrolasesPeptidesProteolysisMilk ProteinsPeptide HydrolasesPeptidesCaseinHumanMother’s milkPeptidesWhey

Identifiers

PMID29464498
PMCPMC5856648
OpenAlexW2791246917

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.