Enhancement of pertussis-toxin-sensitive Na+-dependent uridine transporter activity in HL-60 granulocytes by N-formylmethionyl-leucyl-phenylalanine
نویسندگان
چکیده
منابع مشابه
Influence of antibiotics on formylmethionyl-leucyl-phenylalanine-induced leukocyte chemiluminescence.
The effect of three antimicrobial agents, penicillin G, ampicillin, and chloramphenicol, on luminol-enhanced chemiluminescence of polymorphonuclear leukocytes stimulated by the chemoattractant formylmethionyl-leucyl-phenylalanine was studied. An inhibitory effect of penicillin G and of ampicillin was demonstrated, whereas chloramphenicol gave rise to an enhancement of the chemiluminescence resp...
متن کاملPattern of formylmethionyl-leucyl-phenylalanine-induced luminol- and lucigenin-dependent chemiluminescence in human neutrophils.
The stimulation of neutrophils by formylmethionyl-leucyl-phenylalanine results in a bimodal luminol-dependent chemiluminescence pattern. We observed, however, only a single peak chemiluminescence pattern in the response to the peptide when we used lucigenin as an amplifying substance. We suggest that lucigenin, the larger molecule, (510 daltons; luminol is 177 daltons) only exerts an extracellu...
متن کاملPriming of human neutrophils with N-formyl-methionyl-leucyl-phenylalanine by a calcium-independent, pertussis toxin-insensitive pathway.
Resting neutrophils may be "primed" to augmented effector function, eg, superoxide (O2-) production in the respiratory burst, upon a second stimulation with a variety of soluble agonists including formylated methionyl-leucyl-phenylalanine (FMLP) and phorbol myristate acetate (PMA). At priming concentrations of FMLP (5 x 10(-9) mol/L) that did not initiate O2- generation, two metabolic activitie...
متن کاملSubcellular localization and translocation of the receptor for N-formylmethionyl-leucyl-phenylalanine in human neutrophils.
The subcellular localization of N-formylmethionyl-leucyl-phenylalanine (fMLP) receptors in human neutrophils was investigated. The fMLP receptor was detected with a high-affinity, photoactivatable, radioiodinated derivative of N-formyl-methionyl-leucyl-phenylalanyl-lysine (fMLFK). Neutrophils were disrupted by nitrogen cavitation and fractionated on Percoll density gradients. fMLP receptors wer...
متن کاملN - Formylmethionyl - Leucyl - [ 3 H ] Phenylalanine Binding , Superoxide Release , and Chemotactic Responses of Human Blood Monocytes
Human blood monocytes comprise two subpopulations: one migrates to the chemoattractant. N-formylmethionylleucyl-phenylalanine (fMet-Leu-Phe). and has saturable binding sites for this peptide; the other does not migrate and exhibits little peptide binding. To determine if expression of binding sites was a function of monocyte maturation. we depleted human subjects of blood monocytes by leukapher...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1993
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2940693