ArticleInfection and immunity2000
Lipoarabinomannans activate the protein tyrosine kinase Hck in human neutrophils.
Article in Infection and immunity, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 13 citations in OpenAlex.
- Human Neutrophil Granule Exocytosis in Response toPathogens (Basel, Switzerland) · 2020Article
- Opa+ Neisseria gonorrhoeae exhibits reduced survival in human neutrophils via Src family kinase-mediated bacterial trafficking into mature phagolysosomes.Cellular microbiology · 2015Article
- Mining large-scale response networks reveals 'topmost activities' in Mycobacterium tuberculosis infection.Scientific reports · 2013Article
- Role of protein tyrosine kinase p53/56lyn in diminished lipopolysaccharide priming of formylmethionylleucyl- phenylalanine-induced superoxide production in human newborn neutrophils.Infection and immunity · 2004Article
- Effect of telithromycin (HMR 3647) on polymorphonuclear neutrophil killing of Staphylococcus aureus in comparison with roxithromycin.Antimicrobial agents and chemotherapy · 2002Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mycobacterial lipoarabinomannans (LAMs) are glycosylphosphatidyl-myo-inositol-anchored lipoglycans with diverse biological activities. It has been shown that purified LAMs interact directly, or indirectly, through receptors with the plasma membrane receptors of target cells located in domains rich in glycosylphosphatidylinositol-anchored proteins that contain Src family protein tyrosine kinases. To examine whether LAMs could activate Src-related kinases, human neutrophils were exposed to mannosylated LAMs (ManLAMs) purified from the vaccinal strain Mycobacterium bovis BCG and to phosphoinositol-capped LAMs (AraLAM or PILAM) obtained from the nonpathogenic species Mycobacterium smegmatis. We report first that both ManLAMs and PILAMs activate Hck in a rapid and transient manner and second that complete deacylation of ManLAM abolished its effect on Hck activity, thereby demonstrating that acylation of LAM but not mannosylation is critical for Hck activation. These data indicate that Hck is involved in the signaling pathway of LAMs, molecules known for their ability to trigger several responses in eukaryotic cells.
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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.