ArticleThe Biochemical journal1994
Mastoparan may activate GTP hydrolysis by Gi-proteins in HL-60 membranes indirectly through interaction with nucleoside diphosphate kinase.
Article in The Biochemical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 54 citations in OpenAlex.
- Clinical manifestations of wasp stings: a case report and a review of literature.Tropical medicine and health · 2022Article
- Mastoparans: A Group of Multifunctional α-Helical Peptides With Promising Therapeutic Properties.Frontiers in molecular biosciences · 2022Review
- MrgX2 is a promiscuous receptor for basic peptides causing mast cell pseudo-allergic and anaphylactoid reactions.Pharmacology research & perspectives · 2019Article
- How do basic secretagogues activate mast cells?Naunyn-Schmiedeberg's archives of pharmacology · 2015Article
- Actin dynamics rapidly reset chemoattractant receptor sensitivity following adaptation in neutrophils.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
- Initiation of Plasmodium sporozoite motility by albumin is associated with induction of intracellular signalling.International journal for parasitology · 2010Article
- Mastoparan rapidly activates plant MAP kinase signaling independent of heterotrimeric G proteins.Plant physiology · 2004Article
- Mechanism of peptide-induced mast cell degranulation. Translocation and patch-clamp studies.The Journal of general physiology · 1998Article
- Phosphotransfer reactions as a means of G protein activation.Molecular and cellular biochemistryReview
- Histamine release from mast cells of EAE rats by Gi protein-dependent and IgE-dependent pathways.Journal of molecular neuroscience : MNArticle
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The wasp venom, mastoparan (MP), activates reconstituted pertussis toxin (PTX)-sensitive G-proteins in a receptor-independent manner. We studied the effects of MP and its analogue, mastoparan 7 (MP 7), on G-protein activation in HL-60 cells and a reconstituted system and on nucleoside diphosphate kinase (NDPK)-catalysed GTP formation. MP activated high-affinity GTP hydrolysis in HL-60 membranes with an EC50 of 1-2 microM and a maximum at 10 microM. Unlike the effects of the formyl peptide receptor agonist, N-formyl-L-methionyl-L-leucyl-L-phenylalanine (fMet-Leu-Phe), on GTPase, those of MP were only partially PTX-sensitive. MP-induced rises in cytosolic Ca2+ concentration and superoxide-anion formation in intact HL-60 cells were also only incompletely PTX-sensitive. N-Ethylmaleimide inhibited MP-stimulated GTP hydrolysis to a greater extent than that stimulated by fMet-Leu-Phe. Unlike the latter, MP did not enhance incorporation of GTP azidoanilide into, and cholera toxin-catalysed ADP-ribosylation of, Gi-protein alpha-subunits in HL-60 membranes. By contrast to fMet-Leu-Phe, MP did not or only weakly stimulated binding of guanosine 5'-[gamma-thio]triphosphate to Gi-protein alpha-subunits. MP 7 was considerably more effective than MP at activating the GTPase of reconstituted Gi/G(o)-proteins, whereas in HL-60 membranes, MP and MP 7 were similarly effective. MP and MP 7 were similarly effective at activating [3H]GTP formation from [3H]GDP and GTP in HL-60 membranes and by NDPK purified from bovine liver mitochondria. Our data suggest the following: (1) MP activates Gi-proteins in HL-60 cells, but (2) the venom does not simply mimic receptor activation. (3) MP and MP 7 may activate GTP hydrolysis in HL-60 membranes indirectly through interaction with NDPK. (4) MP 7 is a more effective direct activator of PTX-sensitive G-proteins than MP, whereas with regard to NDPK, MP and MP 7 are similarly effective.
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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.