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Proprotein convertase expression and localization in epidermis: evidence for multiple roles and substrates
D J Pearton1, W Nirunsuksiri, A Rehemtulla
1Department of Oral Biology, University of Washington, Seattle, WA 98195, USA.
Experimental Dermatology
|May 31, 2001
Summary
Proprotein convertases (PCs) are key serine proteases in skin cell differentiation. This study reveals PCs like furin and PACE4 cleave essential proteins such as profilaggrin, impacting epidermal development.
Area of Science:
- Biochemistry
- Cell Biology
- Dermatology
Background:
- Specific proteolysis is crucial for keratinocyte differentiation in the epidermis.
- Proprotein convertases (PCs) are Ca2+-dependent serine proteases involved in substrate processing and activation.
Purpose of the Study:
- To investigate the expression and substrates of PCs in the epidermis.
- To understand the role of PCs in keratinocyte differentiation.
Main Methods:
- Detection of four PCs (furin, PACE4, PC5/6, PC7/8) in epidermal keratinocytes.
- Analysis of furin's differential accessibility and forms.
- In vitro cleavage assays using a PC inhibitor and profilaggrin.
Main Results:
- Furin, PACE4, PC5/6, and PC7/8 are expressed in the epidermis.
- Furin exhibits differential active site accessibility and exists in soluble and transmembrane forms.
- Furin and PACE4 specifically cleave profilaggrin in vitro; PC inhibitors affect Notch-1 cleavage.
Conclusions:
- PCs play multifaceted roles in epidermal differentiation.
- Furin and PACE4 are key proteases involved in profilaggrin processing.
- PCs regulate keratinocyte differentiation through cleavage of specific substrates like Notch-1 and profilaggrin.