Cloning of a 67-kD neutrophil oxidase factor with similarity to a noncatalytic region of p60c-src.

Autor: Leto TL; Laboratory of Clinical Investigation, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892., Lomax KJ, Volpp BD, Nunoi H, Sechler JM, Nauseef WM, Clark RA, Gallin JI, Malech HL
Jazyk: angličtina
Zdroj: Science (New York, N.Y.) [Science] 1990 May 11; Vol. 248 (4956), pp. 727-30.
DOI: 10.1126/science.1692159
Abstrakt: Chronic granulomatous diseases (CGDs) are characterized by recurrent infections resulting from impaired superoxide production by a phagocytic cell, nicotinamide adenine dinucleotide phosphate (reduced) (NADPH) oxidase. Complementary DNAs were cloned that encode the 67-kilodalton (kD) cytosolic oxidase factor (p67), which is deficient in 5% of CGD patients. Recombinant p67 (r-p67) partially restored NADPH oxidase activity to p67-deficient neutrophil cytosol from these patients. The p67 cDNA encodes a 526-amino acid protein with acidic middle and carboxyl-terminal domains that are similar to a sequence motif found in the noncatalytic domain of src-related tyrosine kinases. This motif was recently noted in phospholipase C-gamma, nonerythroid alpha-spectrin (fodrin), p21ras-guanosine triphophatase-activating protein (GAP), myosin-1 isoforms, yeast proteins cdc-25 and fus-1, and the 47-kD phagocyte oxidase factor (p47), which suggests the possibility of common regulatory features.
Databáze: MEDLINE