Actin polymerization contributes to neutrophil chemotactic dysfunction following thermal injury

• Published in: Journal of leukocyte biology Vol. 52; no. 5; pp. 495 - 500
• Main Authors: Hasslen, Sharon R., Ahrenholz, David H., Solem, Lynn D., Nelson, Robert D.
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Society for Leukocyte Biology 01.11.1992; Federation of American Societies for Experimental Biology
• Subjects: Actin Cytoskeleton - physiology; Actins - physiology; Biological and medical sciences; Burns; Burns - immunology; chemotaxis; Chemotaxis, Leukocyte; Ethylmaleimide - pharmacology; Exudates and Transudates - immunology; F‐actin; Humans; Medical sciences; migration; NBD‐phallacidin; Neutrophils - immunology; Traumas. Diseases due to physical agents; Burn; Human; Motility; Migration; Contractile protein; Actins; Polymerization; Attenuation; Neutrophil; Chemotaxis; Trauma
• ISSN: 0741-5400; 1938-3673
• DOI: 10.1002/jlb.52.5.495

The agent(s) and mechanism(s) responsible for suppression of neutrophil chemotaxis in association with major thermal injury have not been identified. We have proposed that the reduced random motility characterizing patients' cells may contribute to their generalized chemotactic dysfunction. Here we report that actin polymerization may be responsible for the loss of neutrophil motility associated with major thermal injury. Using a fluorescent ligand specific for polymerized or filamentous actin (NBD‐phallacidin) in conjunction with flow cytometry, we have discovered that peripheral blood and exudate neutrophils from patients with major thermal injury contain increased levels of actin in a stably polymerized form. Because cyclic polymerization and depolymerization of actin is essential to cell motility, we suggest that actin polymerization may contribute in a major way to the attenuation of neutrophil random and chemotactic functions induced by major thermal injury.