Identification of different receptor types for toxic phospholipases A2 in rabbit skeletal muscle
- 1 November 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 293 (1-2) , 29-33
- https://doi.org/10.1016/0014-5793(91)81145-x
Abstract
Oxyuranus scutellatus scutellatus toxins I (OS1) and 2 (OS2) are two phospholipase A2s (PLA2) isolated from the venom of the Australian Taipan snake. Their iodinated derivatives have been used to characterize PLA2 binding sites on rabbit skeletal muscle. Competition and cross-linking experiments indicate that 125I-labelled OS2 binding sites in rabbit skeletal muscle in vivo are distributed into two classes of receptors. One class binds OS2 and OS1 and is insensitive to the bee venom PLA2. It is composed of a 180 kDa binding protein. This class of PLA2 receptor is expressed at a high level in rabbit myotube membranes. The other class of PLA2 receptor identified with 125I-OS2 also binds with high affinity the bee venom PLA2 but not OS1 and is composed of major polypeptides of 34.48 and 82 kDa. This second class of receptor is similar to the one found in brain membranes. The density of the two classes of receptors varies during muscle developmentKeywords
This publication has 12 references indexed in Scilit:
- Identification and Properties of Very High Affinity Brain Membrane-binding Sites for a Neurotoxic Phospholipase from the Taipan VenomJournal of Biological Chemistry, 1989
- Cellular and mitochondrial changes induced in the structure of murine skeletal muscle by crotoxin, a neurotoxic phospholipase A2 complexToxicon, 1984
- Dissociation of enzymatic activity from lethality and pharmacological properties by carbamylation of lysines in Naja nigricollis and Naja naja atra snake venom phospholipases A2Toxicon, 1981
- Correlation of Enzymatic Activity and Anticoagulant Properties of Phospholipase A2European Journal of Biochemistry, 1980
- Effects and Mechanisms of Polypeptide Neurotoxins that Act PresynapticallyAnnual Review of Pharmacology and Toxicology, 1980
- The lethality in mice of dangerous Australian and other snake venomToxicon, 1979
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Phospholipase A from Bee VenomEuropean Journal of Biochemistry, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970