Evidence map›Paper›PMID 1313813›Full record

ArticleThe Journal of cell biology1992

Proteins are secreted by both constitutive and regulated secretory pathways in lactating mouse mammary epithelial cells.

M D Turner, M E Rennison, S E Handel, C J Wilde, R D Burgoyne

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

27 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
  2. Article
  3. 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
  4. Article
  5. Article
  6. Isolation of Endoplasmic Reticulum Fractions from Mammary Epithelial Tissue.Journal of mammary gland biology and neoplasia · 2016
    Article
  7. Article
  8. Milk secretion: The role of SNARE proteins.Journal of mammary gland biology and neoplasia · 2014
    Review
  9. Article
  10. Article
  11. The contribution of adhesion signaling to lactogenesis.Journal of cell communication and signaling · 2010
    Article
  12. Review
  13. Article
  14. Secretion of milk proteins.Journal of mammary gland biology and neoplasia · 1998
    Review
  15. Origin and secretion of milk lipids.Journal of mammary gland biology and neoplasia · 1998
    Review
  16. Article
  17. Feedback control of milk secretion from milk.Journal of mammary gland biology and neoplasia · 1996
    Review
  18. Molecular mechanisms in exocytosis.The Journal of membrane biology · 1995
    Review
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

M D TurnerDepartment of Physiology, University of Liverpool, United Kingdom.
M E Rennison
S E Handel
C J Wilde
R D Burgoyne
University of Liverpool · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lactating mammary epithelial cells secrete high levels of caseins and other milk proteins. The extent to which protein secretion from these cells occurs in a regulated fashion was examined in experiments on secretory acini isolated from the mammary glands of lactating mice at 10 d postpartum. Protein synthesis and secretion were assayed by following the incorporation or release, respectively, of [35S]methionine-labeled TCA-precipitable protein. The isolated cells incorporated [35S]methionine into protein linearly for at least 5 h with no discernible lag period. In contrast, protein secretion was only detectable after a lag of approximately 1 h, consistent with exocytotic secretion of proteins immediately after passage through the secretory pathway and package into secretory vesicles. The extent of protein secretion was unaffected by the phorbol ester PMA, 8-bromo-cAMP, or 8-bromo-cGMP but was doubled by the Ca2+ ionophore ionomycin. In a pulse-label protocol in which proteins were prelabeled for 1 h before a chase period, constitutive secretion was unaffected by depletion of cytosolic Ca2+ but ionomycin was found to give a twofold stimulation of the secretion of presynthesized protein in a Ca(2+)-dependent manner. Ionomycin was still able to stimulate protein secretion after constitutive secretion had terminated. These results suggest that lactating mammary cells possess both a Ca(2+)-independent constitutive pathway and a Ca(2+)-activated regulatory pathway for protein secretion. The same proteins were secreted by both pathways. No ultrastructural evidence for apocrine secretion was seen in response to ionomycin and so it appears that regulated casein release involves exocytosis. Ionomycin was unlikely to be acting by disassembling the cortical actin network since cytochalasin D did not mimic its effects on secretion. The regulated pathway may be controlled by Ca2+ acting at a late step such as exocytotic membrane fusion.

Indexed as

Lactation8-Bromo Cyclic Adenosine MonophosphateActin CytoskeletonAnimalsCalciumCaseinsCyclic GMPCytochalasin DExocytosisFemaleIonomycinMammary Glands, AnimalMiceMicroscopy, ElectronMilk Proteins8-Bromo Cyclic Adenosine Monophosphate8-bromocyclic GMPCalciumCaseinsCyclic GMPCytochalasin DIonomycinMilk Proteins

Identifiers

PMID1313813
PMCPMC2289423
OpenAlexW2114363713

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.