Title : Myeloperoxidase-mediated modulation of chemotactic peptide binding to human neutrophils.

Pub. Date : 1983 Jun

PMID : 6301583






5 Functional Relationships(s)
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Protein Name
Organism
1 Methionine-containing chemotactic peptides, such as formyl-methionyl-leucyl-phenylalanine (FMLP), are inactivated via a neutrophil-derived, myeloperoxidase-mediated oxidation of the methionine residue. Methionine myeloperoxidase Homo sapiens
2 Methionine-containing chemotactic peptides, such as formyl-methionyl-leucyl-phenylalanine (FMLP), are inactivated via a neutrophil-derived, myeloperoxidase-mediated oxidation of the methionine residue. Methionine myeloperoxidase Homo sapiens
3 We report that extracellular inactivation of FMLP by myeloperoxidase modulates the apparent binding of methionine-containing chemotactic peptides to their surface receptors. Methionine myeloperoxidase Homo sapiens
4 These studies show that intact PMN inactivate methionine-containing chemotactic peptides by a pathway that is sensitive to myeloperoxidase inhibitors and is absent in myeloperoxidase-deficient PMN. Methionine myeloperoxidase Homo sapiens
5 These studies show that intact PMN inactivate methionine-containing chemotactic peptides by a pathway that is sensitive to myeloperoxidase inhibitors and is absent in myeloperoxidase-deficient PMN. Methionine myeloperoxidase Homo sapiens