ArticleThe Biochemical journal1991
Investigation of the role of calpain as a stimulus-response mediator in human platelets using new synthetic inhibitors.
Article in The Biochemical journal, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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.
Who cites it
7 citing papers in PubMed, 31 citations in OpenAlex.
- Improvement in recovery after experimental intracerebral hemorrhage using a selective cathepsin B and L inhibitor.Journal of neurosurgery · 2011Article
- Proteomic and phospho-proteomic profile of human platelets in basal, resting state: insights into integrin signaling.PloS one · 2009Article
- Identification and optimization of a novel inhibitor of mitochondrial calpain 10.Journal of medicinal chemistry · 2009Article
- Inhibition of calpain blocks platelet secretion, aggregation, and spreading.The Journal of biological chemistry · 1999Article
- Calpain regulates actin remodeling during cell spreading.The Journal of cell biology · 1998Article
- Affinity labelling of the Ca(2+)-activated neutral proteinase (calpain) in intact human platelets.The Biochemical journal · 1993Article
- Comparative behaviour of calpain and cathepsin B toward peptidyl acyloxymethyl ketones, sulphonium methyl ketones and other potential inhibitors of cysteine proteinases.The Biochemical journal · 1992Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A series of peptidyl diazomethanes and monofluoromethane with structures specific for calpain have been synthesized and tested for their ability to inhibit calpain activity in vivo, using human platelets as a model system. Calpain activity in vivo was determined by observing proteolysis of actin-binding protein and talin, two known substrates of calpain. Very potent inhibitors, which emerged from this study, were used to investigate the role of calpain in some platelet response processes. Our results show that calpain-mediated proteolysis in platelets is not an obligatory event leading to change of cell shape, adhesion to glass and spreading, aggregation and 5-hydroxytryptamine release. Two of the inhibitors were iodinated with 125I and used to radiolabel the enzyme in vivo. To our knowledge, this work also represents the first report describing the affinity labelling of calpain in human platelets using irreversible radioactive inhibitors.
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Registered trials
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.