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Research Article Free access | 10.1172/JCI114740

Proenkephalin system in human polymorphonuclear cells. Production and release of a novel 1.0-kD peptide derived from synenkephalin.

O Vindrola, M R Padrós, A Sterin-Prync, A Ase, S Finkielman, and V Nahmod

Instituto de Investigaciones Médicas, Sección de Sustancias Vasoactivas, Buenos Aires, Argentina.

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Instituto de Investigaciones Médicas, Sección de Sustancias Vasoactivas, Buenos Aires, Argentina.

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Instituto de Investigaciones Médicas, Sección de Sustancias Vasoactivas, Buenos Aires, Argentina.

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Instituto de Investigaciones Médicas, Sección de Sustancias Vasoactivas, Buenos Aires, Argentina.

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Instituto de Investigaciones Médicas, Sección de Sustancias Vasoactivas, Buenos Aires, Argentina.

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Instituto de Investigaciones Médicas, Sección de Sustancias Vasoactivas, Buenos Aires, Argentina.

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Published August 1, 1990 - More info

Published in Volume 86, Issue 2 on August 1, 1990
J Clin Invest. 1990;86(2):531–537. https://doi.org/10.1172/JCI114740.
© 1990 The American Society for Clinical Investigation
Published August 1, 1990 - Version history
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Abstract

In the hematopoietic system a pluripotent stem cell generates precursors for lymphoid and myeloid lineages. Proenkephalin-derived peptides were previously detected in differentiated lymphoid cells. We have studied whether the proenkephalin system is expressed in a typical differentiated cell of the myeloid lineage, the neutrophil. Human peripheral polymorphonuclear cells contain and release proenkephalin-derived peptides. The opioid portion of proenkephalin (met-enkephalin-containing peptides) was incompletely processed, resulting in the absence of low molecular weight products. The nonopioid synenkephalin (proenkephalin 1-70) molecule was completely processed to a 1.0-kD peptide derived from the COOH-terminal. This molecule was characterized in neutrophils by biochemical and immunocytochemical methods. The chemotactic peptide FMLP and the calcium ionophore A23187 induced the release of the proenkephalin-derived peptides, and this effect was potentiated by cytochalasin B. The materials secreted were similar to those present in the cell, although in the supernatant a higher proportion corresponded to more processed products. The 1.0-kD peptide was detected in human, bovine, and rat neutrophils, but the chromatographic pattern of synenkephalin-derived peptides suggests a differential posttranslational processing among species. These findings demonstrate the existence of the proenkephalin system in human neutrophils and the production and release of a novel 1.0-kD peptide derived from the synenkephalin molecule. The presence of opioid peptides in neutrophils suggests their participation in the inflammatory process, including a local analgesic effect.

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