Evidence map›Paper›PMID 10677354›Full record

ArticleThe Biochemical journal2000

Stimulation of cleavage of membrane proteins by calmodulin inhibitors.

E Díaz-Rodríguez, A Esparís-Ogando, J C Montero, L Yuste, A Pandiella

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 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
2.6field-weighted citation impact, top 11% 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, 60 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Calmodulin Binding Proteins and Alzheimer's Disease.Journal of Alzheimer's disease : JAD · 2015
    Article
  5. Article
  6. Article
  7. Article
  8. Article
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  11. Glycoprotein nonmetastatic melanoma protein b, a melanocytic cell marker, is a melanosome-specific and proteolytically released protein.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010
    Article
  12. Article
  13. The secreted form of a melanocyte membrane-bound glycoprotein (Pmel17/gp100) is released by ectodomain shedding.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010
    Article
  14. Article
  15. Article
  16. High shed antigen levels within tumors: an additional barrier to immunoconjugate therapy.Clinical cancer research : an official journal of the American Association for Cancer Research · 2008
    Review
  17. Article
  18. Article
  19. 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

5 authors at 2 institutions in 1 country.

E Díaz-RodríguezInstituto de Microbiología Bioquímica, Edificio Departamental, Consejo Superior de Investigaciones Científicas-Universidad de Salamanca, Avenida del Campo Charro s/n, 37007-Salamanca, Spain.
A Esparís-Ogando
J C Montero
L Yuste
A Pandiella
Consejo Superior de Investigaciones Científicas · ESUniversidad de Salamanca · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ectodomain of several membrane-bound proteins can be shed by proteolytic cleavage. The activity of the proteases involved in shedding is highly regulated by several intracellular second messenger pathways, such as protein kinase C (PKC) and intracellular Ca(2+). Recently, the shedding of the adhesion molecule L-selectin has been shown to be regulated by the interaction of calmodulin (CaM) with the cytosolic tail of L-selectin. Prevention of CaM-L-selectin interaction by CaM inhibitors or mutation of a CaM binding site in L-selectin induced L-selectin ectodomain shedding. Whether this action of CaM inhibitors also affects other membrane-bound proteins is not known. In the present paper we show that CaM inhibitors also stimulate the cleavage of several other transmembrane proteins, such as the membrane-bound growth factor precursors pro-transforming growth factor-alpha and pro-neuregulin-alpha2c, the receptor tyrosine kinase, TrkA, and the beta-amyloid precursor protein. Cleavage induced by CaM inhibitors was a rapid event, and resulted from the activation of a mechanism that was independent of PKC or intracellular Ca(2+) increases, but was highly sensitive to hydroxamic acid-based metalloprotease inhibitors. Mutational analysis of the intracellular domain of the TrkA receptor indicated that CaM inhibitors may stimulate membrane-protein ectodomain cleavage by mechanisms independent of CaM-substrate interaction.

Indexed as

AnimalsCalmodulinCell LineHumansMembrane ProteinsMetalloendopeptidasesPeptide HydrolasesCalmodulinMembrane ProteinsMetalloendopeptidasesPeptide Hydrolases

Identifiers

PMID10677354
PMCPMC1220861
OpenAlexW1968098564

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.