TY - JOUR
T1 - Staphylococcus aureus α-toxin. 1. Effect on protein phosphorylation in myelin
AU - Chan, Kai Foon Jesse
AU - Lazarovici, Philip
PY - 1987
Y1 - 1987
N2 - K.-F. J. Chan and P. Lazarovici. Staphylococcus aureus α-toxin. 1. Effect on protein phosphorylation in myelin. Toxicon 25, 631 - 636, 1987.-It has previously been demonstrated that staphylococcal α-toxin can selectively induce disruption of myelin sheaths in the central nervous system, albeit the exact mechanism is not known. In this report we show for the first time that the staphylococcal α-toxin could stimulate the endogenous phosphorylation of several proteins, including myelin basic protein (Mr = 18,500) in purified guinea pig brain myelin. This stimulatory effect does not require the presence of calcium and is distinct from those modulated by calcium and phospholipids. In vitro phosphorylation of isolated myelin basic protein by the purified catalytic subunit of cAMP-dependent protein kinase was enhanced in the presence of α-toxin, whereas the reaction catalyzed by protein kinsase C, a Ca2+-activated and phospholipid-dependent protein kinase, was not affected. These results suggest that some of the toxic effects of staphylococcal α-toxin on myelin may be mediated through post-translation covalent modification, such as phosphorylation of specific proteins.
AB - K.-F. J. Chan and P. Lazarovici. Staphylococcus aureus α-toxin. 1. Effect on protein phosphorylation in myelin. Toxicon 25, 631 - 636, 1987.-It has previously been demonstrated that staphylococcal α-toxin can selectively induce disruption of myelin sheaths in the central nervous system, albeit the exact mechanism is not known. In this report we show for the first time that the staphylococcal α-toxin could stimulate the endogenous phosphorylation of several proteins, including myelin basic protein (Mr = 18,500) in purified guinea pig brain myelin. This stimulatory effect does not require the presence of calcium and is distinct from those modulated by calcium and phospholipids. In vitro phosphorylation of isolated myelin basic protein by the purified catalytic subunit of cAMP-dependent protein kinase was enhanced in the presence of α-toxin, whereas the reaction catalyzed by protein kinsase C, a Ca2+-activated and phospholipid-dependent protein kinase, was not affected. These results suggest that some of the toxic effects of staphylococcal α-toxin on myelin may be mediated through post-translation covalent modification, such as phosphorylation of specific proteins.
UR - http://www.scopus.com/inward/record.url?scp=0023525829&partnerID=8YFLogxK
U2 - 10.1016/0041-0101(87)90109-7
DO - 10.1016/0041-0101(87)90109-7
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C2 - 2442854
AN - SCOPUS:0023525829
SN - 0041-0101
VL - 25
SP - 631
EP - 636
JO - Toxicon
JF - Toxicon
IS - 6
ER -