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.

Full text not available from this repository.

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:	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

Citation Data

Cited 46 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item