Evidence map›Paper›PMID 11839820›Full record

ArticleMolecular and cellular biology2002

Loss of the zymogen granule protein syncollin affects pancreatic protein synthesis and transport but not secretion.

Wolfram Antonin, Martin Wagner, Dietmar Riedel, Nils Brose, Reinhard Jahn

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

13 citing papers in PubMed, 32 citations in OpenAlex.

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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

5 authors at 3 institutions in 1 country.

Wolfram AntoninDepartment of Neurobiology, Max Planck Institute for Biophysical Chemistry 37077 Göttingen, Germany.
Martin Wagner
Dietmar Riedel
Nils Brose
Reinhard Jahn
Max Planck Society · DEMax Planck Institute for Biophysical Chemistry · DEMax Planck Institute of Experimental Medicine · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Syncollin is a small protein that is abundantly expressed in pancreatic acinar cells and that is tightly associated with the lumenal side of the zymogen granule membrane. To shed light on the hitherto unknown function of syncollin, we have generated syncollin-deficient mice. The mice are viable and show a normal pancreatic morphology as well as normal release kinetics in response to secretagogue stimulation. Although syncollin is highly enriched in zymogen granules, no change was found in the overall protein content and in the levels of chymotrypsin, trypsin, and amylase. However, syncollin-deficient mice reacted to caerulein hyperstimulation with a more severe pancreatitis. Furthermore, the rates of both protein synthesis and intracellular transport of secretory proteins were reduced. We conclude that syncollin plays a role in maturation and/or concentration of zymogens in zymogen granules.

Indexed as

Amino Acid SequenceAmylasesAnimalsCarrier ProteinsEndoplasmic ReticulumGenomic LibraryHeterozygoteHomozygoteMembrane ProteinsMiceMice, Mutant StrainsMolecular ChaperonesMolecular Sequence DataPancreasProtein BiosynthesisProtein TransportAmylasesCarrier ProteinsMembrane ProteinsMolecular ChaperonesSycn protein, ratTubulin

Identifiers

PMID11839820
PMCPMC134703
OpenAlexW2139741996

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.