Evidence map›Paper›PMID 7758873›Full record

ArticleDiabetologia1995

Intracellular localization and molecular heterogeneity of the sulphonylurea receptor in insulin-secreting cells.

S E Ozanne, P C Guest, J C Hutton, C N Hales

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Diabetologia, 1995. 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
7.2field-weighted citation impact, top 3% 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, 71 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. α-Synuclein binds the K(ATP) channel at insulin-secretory granules and inhibits insulin secretion.American journal of physiology. Endocrinology and metabolism · 2011
    Article
  9. Human K(ATP) channelopathies: diseases of metabolic homeostasis.Pflugers Archiv : European journal of physiology · 2010
    Review
  10. Article
  11. Article
  12. Review
  13. Nuclear KATP channels trigger nuclear Ca(2+) transients that modulate nuclear function.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  14. Article
  15. Review
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 2 institutions in 1 country.

S E OzanneDepartment of Clinical Biochemistry, University of Cambridge, Addenbrooke's Hospital, UK.
P C Guest
J C Hutton
C N Hales
University of Cambridge · GBAddenbrooke's Hospital · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Sulphonylureas stimulate insulin secretion by binding to a receptor in the pancreatic beta-cell plasma membrane resulting in inhibition of ATP-sensitive K+ channels, membrane depolarization and thus influx of Ca2+ through voltage-dependent Ca2+ channels. Sulphonylureas can also induce hormone release at fixed membrane potentials without Ca2+ entry suggesting that these drugs may have other modes of action. We have determined whether different forms of sulphonylurea-binding proteins are present in insulin-secreting cells and their subcellular localization by density gradient centrifugation. Binding studies using [3H]-glibenclamide showed that islet and insulinoma membranes contained a single high affinity sulphonylurea binding site (Kd = 1 nmol/l). Photo-crosslinking of the drug to the membranes resulted in labelling of two proteins with apparent molecular weights of 170 and 140 kDa. The same analyses of insulinoma subcellular fractions showed that the majority (> 90%) of binding proteins were localized to intracellular membranes with only minor levels (< 10%) on plasma membranes. The 170 kDa sulphonylurea binding protein was present in both plasma and granule membrane fractions whereas the 140 kDa form was not present in the plasma membrane fraction. The differences in the molecular forms and subcellular distribution of the receptor are consistent with sulphonylureas having multiple sites of action in the pancreatic beta cell.

Indexed as

ATP-Binding Cassette TransportersPotassium Channels, Inwardly RectifyingAnimalsBinding SitesBiomarkersCell FractionationCell MembraneCross-Linking ReagentsElectrophoresis, Polyacrylamide GelGlyburideInsulinomaIntracellular MembranesIslets of LangerhansKineticsMolecular WeightPancreatic NeoplasmsATP-Binding Cassette TransportersBiomarkersCross-Linking ReagentsGlyburidePotassium ChannelsPotassium Channels, Inwardly RectifyingReceptors, DrugSulfonylurea CompoundsSulfonylurea Receptors

Identifiers

PMID7758873
OpenAlexW2129475346

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.