ArticleMolecular and cellular biochemistry2000
Signal transduction mechanism in human neutrophil: comparative study between the zeta and beta-protein kinase isotypes.
Article in Molecular and cellular biochemistry, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Leishmania donovani-induced ceramide as the key mediator of Akt dephosphorylation in murine macrophages: role of protein kinase Czeta and phosphatase.Infection and immunity · 2007Article
- An unusual pro-inflammatory role of interleukin-10 induced by arabinosylated lipoarabinomannan in murine peritoneal macrophages.Glycoconjugate journal · 2006Article
- Regulation of impaired protein kinase C signaling by chemokines in murine macrophages during visceral leishmaniasis.Infection and immunity · 2005Article
- Leishmania donovani suppresses activated protein 1 and NF-kappaB activation in host macrophages via ceramide generation: involvement of extracellular signal-regulated kinase.Infection and immunity · 2002Article
- Generation of ceramide in murine macrophages infected with Leishmania donovani alters macrophage signaling events and aids intracellular parasitic survival.Molecular and cellular biochemistry · 2001Article
- Immunomodulatory role of interleukin-10 in visceral leishmaniasis: defective activation of protein kinase C-mediated signal transduction events.Infection and immunity · 2001Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Role of protein kinase C (PKC) isotypes in the regulation of neutrophil function are not clearly known. In the present study we purified the beta-PKC and zeta-PKC isotypes from human neutrophil. Both the isotypes are immunoreactive only to their respective antibodies. Zeta-PKC was further confirmed by RT-PCR using specific primer. Co-factor requirements for both the kinases were found to be different when DG and ceramide were used as second messenger. Selective substrate specificities were determined for both beta and zeta-PKC using isotype specific pseudosubstrates viz., [Ser25]PKC[19-31] and [Ser119]PKC[113-130] respectively. Endogenous protein phosphorylation by purified beta-PKC and zeta-PKC showed their functional differences in neutrophil. Beta-PKC phosphorylated 13, 15, 19, 33, 36, 47, 80 and 92 kDa proteins and zeta-PKC phosphorylated 19, 22, 42, 47, 75 and 87 kDa proteins, only exception was the phosphorylation of 47 kDa protein which had been phosphorylated by both the kinases. Differences in phosphorylation between beta-PKC and zeta-PKC clearly indicate the selective role for these PKC isotypes in the activation sequences of neutrophil.
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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.