Evidence map›Paper›PMID 7520866›Full record

ArticleThe EMBO journal1994

Exocrine granule specific packaging signals are present in the polypeptide moiety of the pancreatic granule membrane protein GP2 and in amylase: implications for protein targeting to secretory granules.

V Colomer, K Lal, T C Hoops, M J Rindler

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.7field-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

15 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
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  4. A duplicated motif controls assembly of zona pellucida domain proteins.Proceedings of the National Academy of Sciences of the United States of America · 2004
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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

4 authors at 1 institution in 1 country.

V ColomerDepartment of Cell Biology, New York University Medical Center, NY 10016.
K Lal
T C Hoops
M J Rindler
Columbia University Irving Medical Center · US

Funding

BIOGENESIS OF EXOCRINE SECRETORY GRANULE MEMBRANESR01DK044238 · NIDDK · NEW YORK UNIVERSITY · PI RINDLER, MICHAEL J. · 1991 to 1993
–
NIDDK NIH HHS DK 44238
6 · The paper itself

Abstract

The mechanisms for segregation of secretory and membrane proteins incorporated into storage granules from those transported constitutively have been thought to be conserved in diverse cell types, including exocrine and endocrine cells. However, GP2, the major protein of pancreatic zymogen granule membranes, in its native glycosyl phosphatidylinositol (GPI)-linked form, is incorporated into secretory granules when expressed in exocrine pancreatic AR42J cells, but not in the endocrine cells such as pituitary AtT20. To determine whether the protein moiety of GP2 contains the cell-type specific information for packaging into granules, a secretory form of GP2 (GP2-GPI-), with the GPI attachment site deleted, was generated and introduced into AR42J and AtT20 cells. Like native GP2, GP2-GPI- localized to the zymogen-like granules of AR42J cells and underwent regulated secretion. In AtT20 cells expressing GP2-GPI-, however, the protein was secreted by the constitutive pathway. Thus, a granule packaging signal is present in the luminal portion of GP2 that is functional only in the exocrine cells. However, this cell-type dependent sorting process is not limited to GP2 or membrane proteins. Amylase, a major content protein of pancreatic acinar and serous salivary gland granules, was also secreted exclusively by the constitutive pathway when expressed in AtT20 cells. The cell-type specific targeting of GP2 to granules correlated with its behavior in an in vitro aggregation assay where it co-aggregated more effectively with content proteins from pancreatic zymogen granules than with those from pituitary granules.(ABSTRACT TRUNCATED AT 250 WORDS)

Indexed as

AmylasesAnimalsBiological TransportCytoplasmic GranulesFluorescent Antibody TechniqueGlycosylphosphatidylinositolsGPI-Linked ProteinsMembrane GlycoproteinsMiceOrgan SpecificityPancreasPituitary GlandRatsRecombinant ProteinsTransfectionTransformation, GeneticAmylasesGlycosylphosphatidylinositolsGp2 protein, ratGPI-Linked ProteinsG protein, vesicular stomatitis virusMembrane GlycoproteinsRecombinant ProteinsViral Envelope Proteins

Identifiers

PMID7520866
PMCPMC395281
OpenAlexW162502581

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.