期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1980
卷号：77
期号：2
页码：1000-1004
DOI：10.1073/pnas.77.2.1000
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The chemotactic peptide N-formyl-Nle-Leu-Phe-Nle-Tyr(125I)-Lys (formyl 125I-peptide) binds in a saturable manner to human promyelocytic leukemia cells (HL-60) grown in suspension culture. The binding is of high affinity (50% binding at 0.4--0.75 nM), is rapid (half-time at 22 degrees C = 10 min), is enhanced by divalent cations, but is poorly reversible. These characteristics are similar to those of the formyl peptide chemotactic receptor on human peripheral blood neutrophils. The relative potencies of a series of synthetic peptides in inhibiting binding to the HL-60 cell receptor correlate closely with their potencies in inhibiting binding to the peripheral neutrophil receptor. However, whereas all peripheral human neutrophils display the receptor, only a subpopulation of the cultured cells will bind and internalize tetramethylrhodamine-labeled N-formyl-Nle-Leu-Phe-Nle-Tyr-Lys. This subpopulation is distinct from the rest of the culture, displays morphological characteristics typical of well-differentiated promyelocytes, and appears to account for all of the measured fromyl 125I-peptide binding. Binding of both 125I-labeled and tetramethylrhodamine-labeled formyl peptide increases in response to treatment of the culture with polar compounds that induce cell differentiation. Cells from the differentiated culture demonstrate a chemotactic response to N-formyl-Nle-Leu-Phe-Nle-Tyr-Lys, whereas cells from the undifferentiated culture do not.
