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Priming of human neutrophils by tumour necrosis factor-alpha and substance P is associated with tyrosine phosphorylation

Lloyds, D., Brindle, N. P. and Hallett, Maurice Bartlett ORCID: https://orcid.org/0000-0001-8197-834X 1995. Priming of human neutrophils by tumour necrosis factor-alpha and substance P is associated with tyrosine phosphorylation. Immunology 84 (2) , pp. 220-226.

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Abstract

The mechanisms involved in neutrophil 'priming' are unknown. 'Priming' by substance P and tumour necrosis factor-alpha (TNF-alpha) occurred without effecting cytosolic-free Ca2+ signalling and was independent of actin polymerization. We demonstrate here that these two primers, which act on different receptor classes, both cause tyrosine phosphorylation of a number of protein substrates including a prominent 74,000 MW protein. This protein was not recognized by anti-c-raf antibodies. The concentration relationship and time-course of tyrosine phosphorylation were consistent with a role in mediating priming. Pretreatment with genistein both inhibited tyrosine phosphorylation and abolished the priming by either substance P or TNF-alpha

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
Subjects: R Medicine > R Medicine (General)
Publisher: Wiley Blackwell
ISSN: 0019-2805
Last Modified: 28 Oct 2022 09:04
URI: https://orca.cardiff.ac.uk/id/eprint/73185

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