Evidence map›Paper›PMID 10880051›Full record

ArticleThe Journal of clinical investigation2000

Heat shock protein 70 prevents secretagogue-induced cell injury in the pancreas by preventing intracellular trypsinogen activation.

L Bhagat, V P Singh, A J Hietaranta, S Agrawal, M L Steer, A K Saluja

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of clinical investigation, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

24 citing papers in PubMed, 84 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. The role of protein synthesis and digestive enzymes in acinar cell injury.Nature reviews. Gastroenterology & hepatology · 2013
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Protease activation during in vivo pancreatitis is dependent on calcineurin activation.American journal of physiology. Gastrointestinal and liver physiology · 2009
    Article
  15. Article
  16. Article
  17. Functional role of J domain of cysteine string protein in Ca2+-dependent secretion from acinar cells.American journal of physiology. Gastrointestinal and liver physiology · 2009
    Article
  18. Effect of non-alcoholic compounds of alcoholic drinks on the pancreas.Pancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.] · 2007
    Review
  19. In vitro evidence for role of ERK, p38, and JNK in exocrine pancreatic cytokine production.Journal of gastrointestinal surgery : official journal of the Society for Surgery of the Alimentary Tract · 2006
    Article
  20. 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

6 authors at 2 institutions in 1 country.

L BhagatDepartment of Surgery, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts, USA. Hybridon Inc., Milford, Massachusetts, USA.
V P Singh
A J Hietaranta
S Agrawal
M L Steer
A K Saluja
Beth Israel Deaconess Medical Center · USHarvard University · US

Funding

ACUTE PANCREATITISR01DK031396 · NIDDK · TUFTS MEDICAL CENTER · PI STEER, MICHAEL · 1986 to 2010
$4.8M
ACUTE PANCREATITISR37DK031396 · NIDDK · BETH ISRAEL DEACONESS MEDICAL CENTER · PI STEER, MICHAEL · 1989 to 1996
–
NIDDK NIH HHS DK-31396NIDDK NIH HHS R01 DK031396
6 · The paper itself

Abstract

Rodents given a supramaximally stimulating dose of cholecystokinin or its analogue cerulein develop acute pancreatitis with acinar cell injury, pancreatic inflammation, and intrapancreatic digestive enzyme (i.e., trypsinogen) activation. Prior thermal stress is associated with heat shock protein 70 (HSP70) expression and protection against cerulein-induced pancreatitis. However, thermal stress can also induce expression of other HSPs. The current studies were performed using an in vitro system to determine whether HSP70 can actually mediate protection against pancreatitis and, if so, to define the mechanism underlying that protection. We show that in vitro exposure of freshly prepared rat pancreas fragments to a supramaximally stimulating dose of cerulein results in changes similar to those noted in cerulein-induced pancreatitis, i.e., intra-acinar cell trypsinogen activation and acinar cell injury. Short-term culture of the fragments results in HSP70 expression and loss of the pancreatitis-like changes noted after addition of cerulein. The culture-induced enhanced HSP70 expression can be prevented by addition of either the flavonoid antioxidant quercetin or an antisense oligonucleotide to HSP70. Under these latter conditions, addition of a supramaximally stimulating concentration of cerulein results in trypsinogen activation and acinar cell injury. These findings indicate that the protection against cerulein-induced pancreatitis that follows culture-induced (and possibly thermal) stress is mediated by HSP70. They suggest that the HSP acts by preventing trypsinogen activation within acinar cells.

Indexed as

AnimalsCeruletideEnzyme ActivationHSP70 Heat-Shock ProteinsOligonucleotides, AntisenseOligopeptidesOrgan Culture TechniquesPancreasQuercetinRatsRats, WistarTrypsinogenCeruletideHSP70 Heat-Shock ProteinsOligonucleotides, AntisenseOligopeptidesQuercetinTrypsinogentrypsinogen activation peptide

Identifiers

PMID10880051
PMCPMC314357
OpenAlexW2126914572

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.