Evidence map›Paper›PMID 24264376›Full record

ReviewJournal of mammary gland biology and neoplasia2014

Milk secretion: The role of SNARE proteins.

Sandrine Truchet, Sophie Chat, Michèle Ollivier-Bousquet

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of mammary gland biology and neoplasia, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.3field-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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Occludin protects secretory cells from ER stress by facilitating SNARE-dependent apical protein exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Review
  11. Article
  12. Article
  13. Developmental Expression of Claudins in the Mammary Gland.Journal of mammary gland biology and neoplasia · 2017
    Article
  14. Article
  15. Isolation of Endoplasmic Reticulum Fractions from Mammary Epithelial Tissue.Journal of mammary gland biology and neoplasia · 2016
    Article
  16. 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

3 authors at 2 institutions in 2 countries.

Sandrine TruchetINRA, UR1196 Génomique et Physiologie de la Lactation, 78352, Jouy-en-Josas Cedex, France, sandrine.truchet@jouy.inra.fr.
Sophie Chat
Michèle Ollivier-Bousquet
Institut National de la Recherche Agronomique · MAMathématiques et Informatique Appliquées du Génome à l'Environnement · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During lactation, polarized mammary epithelial secretory cells (MESCs) secrete huge quantities of the nutrient molecules that make up milk, i.e. proteins, fat globules and soluble components such as lactose and minerals. Some of these nutrients are only produced by the MESCs themselves, while others are to a great extent transferred from the blood. MESCs can thus be seen as a crossroads for both the uptake and the secretion with cross-talks between intracellular compartments that enable spatial and temporal coordination of the secretion of the milk constituents. Although the physiology of lactation is well understood, the molecular mechanisms underlying the secretion of milk components remain incompletely characterized. Major milk proteins, namely caseins, are secreted by exocytosis, while the milk fat globules are released by budding, being enwrapped by the apical plasma membrane. Prolactin, which stimulates the transcription of casein genes, also induces the production of arachidonic acid, leading to accelerated casein transport and/or secretion. Because of their ability to form complexes that bridge two membranes and promote their fusion, SNARE (Soluble N-ethylmaleimide-Sensitive Factor Attachment Protein Receptor) proteins are involved in almost all intracellular trafficking steps and exocytosis. As SNAREs can bind arachidonic acid, they could be the effectors of the secretagogue effect of prolactin in MESCs. Indeed, some SNAREs have been observed between secretory vesicles and lipid droplets suggesting that these proteins could not only orchestrate the intracellular trafficking of milk components but also act as key regulators for both the coupling and coordination of milk product secretion in response to hormones.

Indexed as

AnimalsFemaleHumansLactationMammary Glands, AnimalMammary Glands, HumanMilkSNARE ProteinsSNARE Proteins

Identifiers

PMID24264376
OpenAlexW1966327369

What OpenQuestion holds

Textmetadata
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.