Article
Mammalian cell mutants resistant to a sphingomyelin-directed cytolysin. Genetic and biochemical evidence for complex formation of the LCB1 protein with the LCB2 protein for serine palmitoyltransferase.
The Journal of biological chemistry - 11 Dec 1998
Hanada K, Hara T, Fukasawa M, Yamaji A, Umeda M, Nishijima M
Abstract excerpt
Lysenin, a hemolytic protein derived from the earthworm Eisenia foetida, has a high affinity for sphingomyelin. Chinese hamster ovary (CHO) cells exhibited a high cytolytic sensitivity to lysenin, but treatment with sphingomyelinase rendered the cells resistant to lysenin. Temperature-sensitive CHO mutant cells defective in sphingolipid synthesis were resistant to lysenin, and this lysenin resistance was...
Topics
- Acyltransferases
- Amino Acid Sequence
- Animals
- CHO Cells
- Cricetinae
- Cytotoxins
- Molecular Sequence Data
- Mutation
- Protein Binding
- Proteins
- Serine C-Palmitoyltransferase
- Sphingomyelin Phosphodiesterase
- Sphingomyelins