Comparative proteomics analysis of primary cutaneous amyloidosis
Daxing Cai1, Yang Li2, Chunlei Zhou1
1Department of Dermatology, Qilu Hospital, Shandong University, Jinan, Shandong 250012, P.R. China.
Experimental and Therapeutic Medicine
|September 16, 2017
Summary
Primary cutaneous amyloidosis (PCA) involves abnormal amyloid deposits in skin. This study identified upregulated extracellular proteins in PCA lesions, linked to epidermal development, collagen organization, and wound healing, offering insights into PCA pathogenesis.
Area of Science:
- Dermatology
- Proteomics
- Molecular Biology
Background:
- Primary cutaneous amyloidosis (PCA) is a skin disorder with unknown pathogenesis.
- Amyloid deposition in the dermal extracellular matrix (ECM) characterizes PCA.
Purpose of the Study:
- To investigate proteome alterations in PCA lesions.
- To elucidate the molecular basis and pathogenesis of PCA.
Main Methods:
- Proteomic analysis using isobaric tags for relative and absolute quantitation (iTRAQ).
- Bioinformatic analysis including Gene Ontology (GO), KEGG pathway, and protein-protein interaction analysis.
- Immunohistochemistry for validating upregulated proteins.
Main Results:
- Identified 1,032 proteins, with 51 differentially expressed in PCA lesions (27 upregulated).
- Upregulated proteins were predominantly extracellular and enriched in epidermal development, collagen organization, and wound response pathways.
- Key upregulated proteins included calcium-binding proteins like S100A7 and S100A8/A9.
Conclusions:
- PCA pathogenesis is associated with increased focal adhesion, differentiation, and wound healing processes.
- Proteomic insights reveal novel molecular pathways involved in PCA development.
- Targeting these pathways may offer therapeutic strategies for PCA.
