Receptor-mediated internalization of tuftsin by human polymorphonuclear leukocytes. Academic Article

abstract

• A high-performance liquid chromatography (HPLC) purified fluorescein-labeled analogue of tuftsin was prepared, which retains the full biological activity of the native molecule. Characterization of the derivatization site by amino acid analysis, N-terminal cleavage, and dansylation revealed a monofluorescinated derivative at the alpha-amino terminus. Binding of the fluorescent tuftsin to living polymorphonuclear leukocytes (PMN) was observed by means of video intensification microscopy. At 37 degrees C, diffuse membrane fluorescence was seen initially, followed by rapid aggregation and internalization. The latter was demonstrated by saltation of intracellular fluorescent aggregates. These processes are temperature-dependent and rely on specific binding to the tuftsin receptor.

authors

• Davies, Peter

published proceedings

• J Reticuloendothel Soc

author list (cited authors)

• Amoscato, A. A., Davies, P. J., Babcock, G. F., & Nishioka, K.

citation count

• 14

complete list of authors

• Amoscato, AA||Davies, PJ||Babcock, GF||Nishioka, K

publication date

• July 1983

published in

• Journal of the Reticuloendothelial Society  Journal

keywords

• Amino Acids
• Blood Bactericidal Activity
• Dose-Response Relationship, Drug
• Fluorescein-5-isothiocyanate
• Fluoresceins
• Humans
• Immunoglobulin Fragments
• Microscopy, Fluorescence
• Monocytes
• Motion
• Neutrophils
• Receptors, Cell Surface
• Receptors, Immunologic
• Subcellular Fractions
• Thiocyanates
• Tuftsin

PubMed Central ID

• 6308252

start page

• 53

end page

• 67

volume

• 34

issue

• 1