Palmitoyl carnitine, a lysophospholipase-transacylase inhibitor, prevents Candida adherence in vitro.
Candida adherence is poorly understood. The results of this study indicate that interactions of Candida with the lyso-forms of phospholipids may be one important attachment mechanism. C. tropicalis and C. albicans adhered to purified lysophospholipids immobilized on microtiter wells, as well as to a human laryngeal epidermoid carcinoma (HEp-2) cell line. Adherence to both lysophospholipids and HEp-2 cells was significantly reduced by palmitoyl carnitine, a lysophospholipase-transacylase inhibitor. Over time there was a positive correlation between Candida adherence and its transacylase activity. The data suggest that palmitoyl carnitine interferes with Candida adherence to lysophospholipids and the HEp-2 cell line by blocking the interaction between the Candida-associated transacylase enzyme receptor site and its lysophospholipid substrate ligand.
Prakobphol
A
A
Department of Stomatology, University of California San Francisco 94143, USA.
Leffler
H
H
Hoover
C I
CI
Fisher
S J
SJ
D000217:Acyltransferases / Q000037:antagonists & inhibitors*; D002175:Candida / Q000187:drug effects* / Q000201:enzymology / Q000472:pathogenicity; D002176:Candida albicans / Q000187:drug effects / Q000201:enzymology / Q000472:pathogenicity; D002448:Cell Adhesion / Q000187:drug effects; D002478:Cells, Cultured; D008099:Liver / Q000166:cytology / Q000382:microbiology; D008245:Lysophospholipase / Q000037:antagonists & inhibitors*; D008246:Lysophospholipids / Q000502:physiology*; D009097:Multienzyme Complexes / Q000037:antagonists & inhibitors*; D010172:Palmitoylcarnitine / Q000494:pharmacology*
D008246:Lysophospholipids; D009097:Multienzyme Complexes; D010172:Palmitoylcarnitine; D000217:Acyltransferases; D008245:Lysophospholipase; C021782:lysophospholipase-transacylase