Evidence map›Paper›PMID 19662378›Full record

ArticleDiabetologia2009

C-peptide is internalised in human endothelial and vascular smooth muscle cells via early endosomes.

P Luppi, X Geng, V Cifarelli, P Drain, M Trucco

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Diabetologia, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
6.8field-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

19 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Insights into the physiology of C-peptide.Physiological research · 2020
    Review
  5. Article
  6. Article
  7. Physiological effects and therapeutic potential of proinsulin C-peptide.American journal of physiology. Endocrinology and metabolism · 2014
    Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. C-peptide reduces pro-inflammatory cytokine secretion in LPS-stimulated U937 monocytes in condition of hyperglycemia.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2012
    Article
  13. Article
  14. Proinsulin C-peptide regulates ribosomal RNA expression.The Journal of biological chemistry · 2010
    Article
  15. Breakthrough in diabetes therapy ... Just around the corner?The review of diabetic studies : RDS · 2009
    Article
  16. C-Peptide in the vessel wall.The review of diabetic studies : RDS · 2009
    Article
  17. Article
  18. Anti-inflammatory properties of C-Peptide.The review of diabetic studies : RDS · 2009
    Article
  19. The beneficial effects of C-Peptide on diabetic polyneuropathy.The review of diabetic studies : RDS · 2009
    Article
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 2 institutions in 1 country.

P LuppiDepartment of Pediatrics, Children's Hospital of Pittsburgh of UPMC, Rangos Research Center, PA 15201, USA. luppip@pitt.edu
X Geng
V Cifarelli
P Drain
M Trucco
Children's Hospital of Pittsburgh · USUniversity of Pittsburgh · US

Funding

JUVENILE DIABETES MELLITUS EPIDEMIOLOGY &ETIOLOGYR01DK024021 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BECKER, DOROTHY J · 1986 to 2013
$7.1M
NIDDK NIH HHS DK 024021-24
6 · The paper itself

Abstract

aims/hypothesisThere is increasing evidence that C-peptide exerts intracellular effects in a variety of cells and could be beneficial in patients with type 1 diabetes. Exactly how C-peptide achieves these effects, however, is unknown. Recent reports showed that C-peptide internalised in the cytoplasm of HEK-293 and Swiss 3T3 cells, where it was not degraded for at least 1 h after uptake. In this study, we investigated the hypothesis that C-peptide is internalised via an endocytic pathway and traffics to classic endocytic organelles, such as endosomes and lysosomes.

methodsWe studied the internalisation of C-peptide in vascular endothelial and smooth muscle cells, two relevant targets of C-peptide activity, by using Alexa Fluor-labelled C-peptide probes in living cells and immunohistochemistry employing confocal laser-scanning microscopy. To examine trafficking to subcellular compartments, we used fluorescent constructs tagged to RAB5A, member RAS oncogene family (RAB5A) to identify early endosomes, or to lysosomal-associated membrane protein 1 (LAMP1) to identify lysosomes.

resultsC-peptide internalised in the cytoplasm of cells within punctate structures identified as early endosomes. Internalisation was clearly detectable after 10 min of incubation and was blocked at 4 degrees C as well as with excess of unlabelled C-peptide. A minor fraction of vesicles, which increased with culture time, co-localised with lysosomes. Uptake of C-peptide was reduced by monodansylcadaverine, a pharmacological compound that blocks clathrin-mediated endocytosis, and by nocodazole, which disrupts microtubule assembly. CONCLUSIONS/

interpretationC-peptide internalises in the cytoplasm of cells by endocytosis, as demonstrated by its localisation in early endosomes. Endosomes might represent a signalling station, through which C-peptide might achieve its cellular effects.

Indexed as

AnisolesCell LineC-PeptideCycloheptanesCytochalasin DEndocytosisEndosomesEndothelial CellsFilipinHumansImmunohistochemistryMicroscopy, ConfocalMuscle, Smooth, VascularMyocytes, Smooth MuscleNocodazoleTemperature2-methoxy-5-(2',4'-dimethoxyphenyl)-2,4,6-cycloheptatrien-1-oneAnisolesC-PeptideCycloheptanesCytochalasin DFilipinNocodazole

Identifiers

PMID19662378
OpenAlexW2009683531

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.