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S100 protein subcellular localization during epidermal differentiation and psoriasis
Ann-Marie Broome1, David Ryan, Richard L Eckert
1Department of Physiology, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106, USA.
Summary
S100 proteins are key in skin cell signaling. Their altered expression in psoriasis suggests a role in the disease, with some S100 proteins forming complexes in differentiated skin cells.
Area of Science:
- Biochemistry
- Cell Biology
- Dermatology
Background:
- S100 proteins are calcium-binding signaling molecules involved in various cellular processes.
- Their specific roles and expression patterns in normal versus diseased skin require further elucidation.
Purpose of the Study:
- To compare the expression levels and cellular localization of specific S100 proteins (S100A7, S100A8, S100A9, S100A10, S100A11) in normal and psoriatic epidermis.
- To investigate the potential in vivo modifications of these S100 proteins.
Main Methods:
- Immunohistochemical analysis of normal and psoriatic skin tissue.
- Assessment of protein expression and subcellular localization.
- Biochemical assays to detect protein multimerization.
Main Results:
- S100A7 and S100A11 are found in basal and spinous layers of normal epidermis, localizing to nucleus, cytoplasm, and plasma membrane.
- S100A10 is present in cytoplasm and associated with the plasma membrane in normal epidermis.
- S100A8 and S100A9 are minimally expressed in normal epidermis but markedly overexpressed in psoriatic epidermis.
- S100A7, S100A10, and S100A11 form resistant multimers, indicating transglutaminase activity, while S100A8 and S100A9 do not.
Conclusions:
- S100 proteins are found at the plasma membrane of differentiated keratinocytes, suggesting roles in calcium-dependent, membrane-associated events.
- Altered expression of S100A7, S100A8, and S100A9 in psoriasis indicates their involvement in the pathogenesis of the disease.