Evidence map›Paper›PMID 11739739›Full record

ArticleMolecular and cellular biology2002

v-Src-induced modulation of the calpain-calpastatin proteolytic system regulates transformation.

N O Carragher, M A Westhoff, D Riley, D A Potter, P Dutt, J S Elce, P A Greer, M C Frame

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

35 citing papers in PubMed, 108 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. A Tale of Two States: Normal and Transformed, With and Without Rigidity Sensing.Annual review of cell and developmental biology · 2019
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. The Critical Role of Calpain in Cell Proliferation.Journal of biomolecular research & therapeutics · 2014
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The calpain system and cancer.Nature reviews. Cancer · 2011
    Review
  18. Article
  19. Calpains as potential anti-cancer targets.Expert opinion on therapeutic targets · 2011
    Review
  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

8 authors at 3 institutions in 3 countries.

N O CarragherThe Beatson Institute for Cancer Research, Cancer Research Campaign Beatson Laboratories, Glasgow, Scotland, United Kingdom. n.carragher@beatson.gla.ac.uk
M A Westhoff
D Riley
D A Potter
P Dutt
J S Elce
P A Greer
M C Frame
Cancer Research UK Scotland Institute · GBQueen's University · CAWalther Cancer Foundation · US

Funding

PILOT AND FEASIBILITY STUDIESP30DK034928 · NIDDK · TUFTS MEDICAL CENTER · PI PLAUT, ANDREW GEORGE · 1986 to 2007
$8.5M
FUNCTIONAL ANALYSIS OF TRANSCRIPTION FACTORS IN HIV-1K08CA001562 · NCI · TUFTS MEDICAL CENTER · PI POTTER, DAVID ALEXANDER · 1991 to 1996
–
NCI NIH HHS K08 CA001562NIDDK NIH HHS DK34928NIDDK NIH HHS P30 DK034928
6 · The paper itself

Abstract

v-Src-induced oncogenic transformation is characterized by alterations in cell morphology, adhesion, motility, survival, and proliferation. To further elucidate some of the signaling pathways downstream of v-Src that are responsible for the transformed cell phenotype, we have investigated the role that the calpain-calpastatin proteolytic system plays during oncogenic transformation induced by v-Src. We recently reported that v-Src-induced transformation of chicken embryo fibroblasts is accompanied by calpain-mediated proteolytic cleavage of the focal adhesion kinase (FAK) and disassembly of the focal adhesion complex. In this study we have characterized a positive feedback loop whereby activation of v-Src increases protein synthesis of calpain II, resulting in degradation of its endogenous inhibitor calpastatin. Reconstitution of calpastatin levels by overexpression of exogenous calpastatin suppresses proteolytic cleavage of FAK, morphological transformation, and anchorage-independent growth. Furthermore, calpastatin overexpression represses progression of v-Src-transformed cells through the G(1) stage of the cell cycle, which correlates with decreased pRb phosphorylation and decreased levels of cyclins A and D and cyclin-dependent kinase 2. Calpain 4 knockout fibroblasts also exhibit impaired v-Src-induced morphological transformation and anchorage-independent growth. Thus, modulation of the calpain-calpastatin proteolytic system plays an important role in focal adhesion disassembly, morphological transformation, and cell cycle progression during v-Src-induced cell transformation.

Indexed as

CDC2-CDC28 KinasesCell Transformation, NeoplasticActinsAnimalsCalcium-Binding ProteinsCalpainCell DivisionCells, CulturedCell SizeChick EmbryoCyclin ACyclin DCyclin-Dependent Kinase 2Cyclin-Dependent KinasesCyclinsCytoskeletonActinsCalcium-Binding ProteinsCalpaincalpastatinCDC2-CDC28 KinasesCdk2 protein, mouseCyclin ACyclin DCyclin-Dependent Kinase 2Cyclin-Dependent KinasesCyclinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesOncogene Protein p65(gag-jun)Oncogene Protein pp60(v-src)Oncogene Proteins v-fosProtein IsoformsProtein Serine-Threonine KinasesProtein-Tyrosine KinasesPtk2 protein, mouseRetinoblastoma Protein

Identifiers

PMID11739739
PMCPMC134206
OpenAlexW2012801471

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.