Evidence map›Paper›PMID 22069054›Full record

ArticleCellular & molecular biology letters2012

p38 Mitogen-activated protein kinase modulates exocrine secretion in rabbit lacrimal gland.

Stina K Carlsson, J Peter Gierow

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Article in Cellular & molecular biology letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 86% 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

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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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

2 authors at 1 institution in 1 country.

Stina K CarlssonSchool of Natural Sciences, Linnaeus University, Kalmar, Sweden. stina.carlsson@lnu.se
J Peter Gierow
Linnaeus University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The lacrimal gland (LG) is an exocrine gland important for secretion of the tear film. The kinase p38 has important signal transduction functions, e.g. in gene transcription, but has previously not been known to modulate exocrine secretion. The aim of the current study was to investigate the role of p38 in carbachol (Cch)-induced LG secretion in LG acinar cells in vitro. Western blotting was used to determine the phosphorylation status of p38 and p42/44 and determine expression of p38 isoforms. To determine the effect of p38 inhibition on LG secretion, PD 169316, a general p38 inhibitor, and SB 239063, an inhibitor of p38α and β, were added to the cells prior to secretion measurements. The results revealed activation of p38 mediated by Cch stimulation and inhibition of Cch-induced secretion as a result of p38 inhibition. The inhibition was observed with PD 169316 isoforms, but not with SB 239063. The p38δ isoform was shown to have robust expression both by Western blotting of acinar cells and immunofluorescence of the whole gland. In conclusion, p38 activation mediates secretion in cholinergic stimulation of rabbit LG cells.

Indexed as

Acinar CellsAnimalsCarbacholCells, CulturedCholinergic AgonistsFemaleImidazolesLacrimal ApparatusMitogen-Activated Protein Kinase 11Mitogen-Activated Protein Kinase 12Mitogen-Activated Protein Kinase 13Mitogen-Activated Protein Kinase 14p38 Mitogen-Activated Protein KinasesPhosphorylationPyrimidinesRabbits2-(4-nitrophenyl)-4-(4-fluorophenyl)-5-(4-pyridinyl)-1H-imidazoleCarbacholCholinergic AgonistsImidazolesMitogen-Activated Protein Kinase 11Mitogen-Activated Protein Kinase 12Mitogen-Activated Protein Kinase 13Mitogen-Activated Protein Kinase 14p38 Mitogen-Activated Protein KinasesPyrimidinesSB 239063

Identifiers

PMID22069054
PMCPMC6275742
OpenAlexW1999252129

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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.