Inhibition of normal and psoriatic epidermal phospholipase A2 by picomolar concentrations of recombinant human lipocortin I.
Normal human and psoriatic epidermal phospholipase A2 (PLA2) was inhibited by human recombinant lipocortin I when the substrate was present in a several million-fold molar excess. Inhibition was not total, even at relatively high concentrations of lipocortin I. It is therefore suggested that human epidermis contains two species of PLA2: one that is controlled by lipocortin I and one that is not.
Cartwright
P H
PH
Department of Dermatology, North Staffordshire Hospital Centre, Stoke-on-Trent, U.K.
Ilderton
E
E
Sowden
J M
JM
Yardley
H J
HJ
D017302:Annexins; D002135:Calcium-Binding Proteins / Q000494:pharmacology*; D004305:Dose-Response Relationship, Drug; D004817:Epidermis / Q000187:drug effects / Q000201:enzymology*; D006801:Humans; D066298:In Vitro Techniques; D010740:Phospholipases / Q000037:antagonists & inhibitors*; D010741:Phospholipases A / Q000037:antagonists & inhibitors* / Q000378:metabolism; D054467:Phospholipases A2; D011565:Psoriasis / Q000201:enzymology*; D011994:Recombinant Proteins / Q000494:pharmacology
D017302:Annexins; D002135:Calcium-Binding Proteins; D011994:Recombinant Proteins; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2