Extra- and intracellular Ca2+ requirements for lysosomal enzyme secretion in human neutrophils
| Autor: | Roger M. Lyons, J. O. Shaw, Isabel Brodersen |
|---|---|
| Rok vydání: | 1982 |
| Předmět: |
Cytochalasin B
Neutrophils Immunology Ionophore Complement C5a Biology In Vitro Techniques Toxicology chemistry.chemical_compound Gallic Acid medicine Extracellular Humans Pharmacology (medical) Secretion Egtazic Acid Calcimycin Glucuronidase Pharmacology Complement component 5 N-Formylmethionine Antagonist Complement C5 hemic and immune systems N-Formylmethionine leucyl-phenylalanine Molecular biology N-Formylmethionine Leucyl-Phenylalanine Biochemistry chemistry Verapamil Calcium Lysosomes Oligopeptides Intracellular medicine.drug |
| Zdroj: | Agents and actions. 12(3) |
| ISSN: | 0065-4299 |
| Popis: | Ca2+-EGTA combinations were utilized in Hank's buffers to fix extracellular free Ca2+ concentrations [Ca2+f] for the study of human neutrophil lysosomal enzyme secretion. Ca2+-dependent neutrophil secretion initiated by formyl-methionyl-leucyl-phenylalanine (FMLP) and C5a required small amounts of [Ca2+f] (1-3 x 10(-6) M) while that caused by ionophore A23187 required 10(-5) M or greater [Ca2+f]. The inhibition of FMLP- and C5a-induced lysosomal enzyme secretion by the intracellular Ca2+ antagonist, 8-(N,N-diethylamino)octyl-3,4,5-trimethoxybenzoate (TMB-8) was additive to lowering extracellular [Ca2+f] from 10(-4) M to 10(-6) M or blocking plasma membrane Ca2+ flux with verapamil. These results suggest that extracellular and intracellular Ca2+ flux may be coupled in the initiation of neutrophil secretion caused by FMLP and C5a. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|