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Heat shock protein 27 expression in the epithelium of periapical lesions
- Source :
- Journal of endodontics. 27(2)
- Publication Year :
- 2001
-
Abstract
- Heat shock protein (HSP) 27 is a member of the small HSP family that plays a part in the regulation of epithelial cell growth and differentiation, wound healing, apoptosis and cell protection against inflammatory cytotoxicity mediators. Thus the expression of HSP27 was investigated immunohistochemically in periapical granulomas with epithelial rests of Malassez and in radicular cysts. Anti-HSP27 mouse monoclonal antibody and peroxidase-labeled streptavidin-biotin standard technique were used to study the expression of HSP27. Proliferating epithelial cell rests, and islands of epithelium and epithelial lining of microcysts strongly reacted throughout all layers, whereas radicular cysts epithelial lining presented mainly a moderate suprabasal staining pattern. However both the proliferating epithelial cell rests and the radicular cysts shared an over-expression of HSP27 immunostaining intensity in coincidence with the presence of local infiltration of immune cells. HSP27 may play several roles in periapical lesions that include contributing to the migration of epithelial cell rests and an increased resistance both to necrotic and apoptotic cell deaths.
- Subjects :
- Pathology
medicine.medical_specialty
Periodontal Ligament
Cell
Periapical Granuloma
Apoptosis
Immunoenzyme Techniques
Hsp27
Cell Movement
Heat shock protein
medicine
Leukocytes
Humans
Coloring Agents
General Dentistry
Heat-Shock Proteins
Radicular Cyst
Wound Healing
biology
Antibodies, Monoclonal
Cell Differentiation
Epithelial Cells
Epithelial cell rests of Malassez
Immunohistochemistry
Epithelium
medicine.anatomical_structure
Gene Expression Regulation
Connective Tissue
biology.protein
Inflammation Mediators
Immunostaining
Cell Division
Subjects
Details
- ISSN :
- 00992399
- Volume :
- 27
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Journal of endodontics
- Accession number :
- edsair.doi.dedup.....d5b723ae813fbc228d541ecd92b85f26