Evidence map›Paper›PMID 9151667›Full record

ArticleThe Journal of cell biology1997

Differential sorting of lysosomal enzymes out of the regulated secretory pathway in pancreatic beta-cells.

R Kuliawat, J Klumperman, T Ludwig, P Arvan

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
17.7field-weighted citation impact, top 1% 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

65 citing papers in PubMed, 168 citations in OpenAlex.

  1. Article
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  11. ELAPOR1 is a secretory granule maturation-promoting factor that is lost during paligenosis.American journal of physiology. Gastrointestinal and liver physiology · 2022
    Article
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  13. Review
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  15. Article
  16. Article
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  20. Article

5 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

R KuliawatDiabetes Research Center and Division of Endocrinology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
J Klumperman
T Ludwig
P Arvan
Albert Einstein College of Medicine · USColumbia University · USVrije Universiteit Amsterdam · NL

Funding

Proinsulin Trafficking for Insulin BiosynthesisR01DK048280 · NIDDK · YESHIVA UNIVERSITY · PI ARVAN, PETER · 1994 to 2024
$10.5M
NIDDK NIH HHS DK48280NIDDK NIH HHS R01 DK048280
6 · The paper itself

Abstract

In cells specialized for secretory granule exocytosis, lysosomal hydrolases may enter the regulated secretory pathway. Using mouse pancreatic islets and the INS-1 beta-cell line as models, we have compared the itineraries of procathepsins L and B, two closely related members of the papain superfamily known to exhibit low and high affinity for mannose-6-phosphate receptors (MPRs), respectively. Interestingly, shortly after pulse labeling INS cells, a substantial fraction of both proenzymes exhibit regulated exocytosis. After several hours, much procathepsin L remains as precursor in a compartment that persists in its ability to undergo regulated exocytosis in parallel with insulin, while procathepsin B is efficiently converted to the mature form and can no longer be secreted. However, in islets from transgenic mice devoid of cation-dependent MPRs, the modest fraction of procathepsin B normally remaining within mature secretory granules is increased approximately fourfold. In normal mouse islets, immunoelectron microscopy established that both cathepsins are present in immature beta-granules, while immunolabeling for cathepsin L, but not B, persists in mature beta-granules. By contrast, in islets from normal male Sprague-Dawley rats, much of the proenzyme sorting appears to occur earlier, significantly diminishing the stimulus-dependent release of procathepsin B. Evidently, in the context of different systems, MPR-mediated sorting of lysosomal proenzymes occurs to a variable extent within the trans-Golgi network and is continued, as needed, within immature secretory granules. Lysosomal proenzymes that fail to be sorted at both sites remain as residents of mature secretory granules.

Indexed as

AnimalsCathepsin BCathepsin LCathepsinsCell CompartmentationCell LineEnzyme InhibitorsEnzyme PrecursorsExocytosisGlycosylationGolgi ApparatusImmunohistochemistryInsulinInsulin SecretionIslets of LangerhansLysosomesCathepsin BCathepsin LCathepsinsEnzyme InhibitorsEnzyme PrecursorsInsulinprocathepsin Bprocathepsin LReceptor, IGF Type 2Tunicamycin

Identifiers

PMID9151667
PMCPMC2139876
OpenAlexW2129139575

What OpenQuestion holds

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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.