Structure and neutrophil-activating properties of a novel inflammatory peptide (ENA-78) with homology to interleukin 8.
A new neutrophil-activating peptide, termed ENA-78, was identified in the conditioned media of stimulated human type II epithelial cell line A549. In response to stimulation with either interleukin 1 beta (IL-1 beta) or tumor necrosis factor alpha (TNF-alpha), ENA-78 was produced and secreted concomitantly with IL-8, GRO alpha, and GRO gamma. ENA-78 consists of 78 amino acids [sequence; see text] and has a molecular weight of 8,357. It has four cysteines positioned identically to those of IL-8 and analogues, and thus belongs to the CXC family of peptides. ENA-78 is related to neutrophil-activating peptide 2 (NAP-2) and GRO alpha (sequence identity, 53% and 52%, respectively) and IL-8 (22% identity). Like NAP-2 and GRO alpha, ENA-78 stimulates neutrophils, inducing chemotaxis, a rise in intracellular free calcium and exocytosis. Cross-desensitization experiments indicate that ENA-78 acts through the same type of receptors as IL-8, NAP-2, and GRO alpha.
Walz
A
A
Theodor Kocher Institute, University of Bern, Switzerland.
Burgener
R
R
Car
B
B
Baggiolini
M
M
Kunkel
S L
SL
Strieter
R M
RM
D000595:Amino Acid Sequence; D001483:Base Sequence; D002118:Calcium / Q000378:metabolism; D002460:Cell Line; D054365:Chemokine CXCL5; D019743:Chemokines, CXC; D006801:Humans; D016209:Interleukin-8 / Q000031:analogs & derivatives* / Q000737:chemistry / Q000494:pharmacology*; D008969:Molecular Sequence Data; D009504:Neutrophils / Q000187:drug effects*; D010455:Peptides / Q000737:chemistry / Q000494:pharmacology*; D001620:beta-Thromboglobulin
C486263:CXCL5 protein, human; D054365:Chemokine CXCL5; D019743:Chemokines, CXC; D016209:Interleukin-8; C061615:PPBP protein, human; D010455:Peptides; D001620:beta-Thromboglobulin; C009862:connective tissue-activating peptide; D002118:Calcium