Submitted to: Society for Leukocyte Biology Meetings Proceedings
Publication Type: Abstract Only
Publication Acceptance Date: 11/9/2001
Publication Date: N/A
Citation: N/A Interpretive Summary:
Technical Abstract: Protein tyrosine phosphorylation is a central mechanism that mediates signal transduction events involved in many cellular processes. Protein tyrosine kinase (PTK) is the mediating enzyme in this signal transduction pathway. Previous studies from our laboratory have demonstrated a dramatic inhibition of oxidative burst and degranulation in chicken heterophils following treatment with the PTK inhibitor, genistein. These results are indicative of the critical nature of protein tyrosine phosphoryltion as a signaling event during functional activity. The purpose of these experiments was to detect and quantitate PTK in heterophils isolated from day of hatch chicks with a commercial kit. Our data demonstrate a significant increase (P<0.05) in the quantity of PTK present in control heterophils vs LPS stimulated heterophils isolated from day-old chicks. Quantitatively, PTK levels were significantly decreased (P<0.05) between genistein treated heterophils (PTK inhibitor) and LPS stimulated heterophils. Our data demonstrate PTK is present in the heterophils of day-old chicks. The presence of PTK and our ability to detect increased and decreased levels in day-old chicken heterophils is indicative of protein tyrosine phosphorylation which mediates signal transduction events at the cellular level.