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A unique phospholipase A2 in human epidermis: its physiologic function and its level in certain dermatoses.
M Bergers1, D R Verhagen, M Jongerius
1Department of Dermatology, University of Nijmegen, The Netherlands.
The Journal of Investigative Dermatology
|January 1, 1988
Summary
Human epidermis contains a novel phospholipase A2 (PLA2) enzyme with high activity against soluble phospholipids. This distinct PLA2 enzyme is linked to keratinocyte differentiation and terminal keratinization.
Area of Science:
- Biochemistry
- Dermatology
- Enzymology
Background:
- The epidermis utilizes phospholipase A2 (PLA2) to initiate the arachidonic acid cascade.
- A classic cutaneous PLA2 enzyme is known in epidermal tissue.
Purpose of the Study:
- To identify and characterize a second, distinct phospholipase A2 enzyme in human epidermis.
- To investigate the unique properties and cellular localization of this novel PLA2.
Main Methods:
- Enzyme activity assays on epidermal homogenates.
- Investigating enzyme activity following corticosteroid pretreatment and alkaline phosphatase treatment.
- Analyzing enzyme levels in different epidermal layers and disease lesions.
Main Results:
- A novel PLA2 enzyme with high activity against phospholipids in solution was identified in human epidermis.
- This enzyme's activity was unaffected by corticosteroid pretreatment or alkaline phosphatase treatment.
- Enzyme activity decreased in inflammatory disease lesions like psoriasis and was localized to differentiated keratinocytes.
Conclusions:
- The newly discovered PLA2 enzyme is distinct from the classic cutaneous enzyme.
- This enzyme is primarily found in terminally differentiated keratinocytes.
- The novel PLA2 is likely involved in phospholipid degradation during epidermal terminal keratinization.