Association of amyloid P protein with pathology in periodontal tissues
| Autor: | Neil Hunter, Hans Zoellner, L. L. Short |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Adult
Cancer Research Pathology medicine.medical_specialty Amyloid Plasma Cells Connective tissue Integrin alphaXbeta2 Biology Epithelium Pathology and Forensic Medicine Extracellular matrix Gingivitis Nerve Fibers medicine Humans Periodontal Pocket Periodontitis Complement C4 medicine.disease Elastic Tissue Chronic periodontitis Immunohistochemistry Extracellular Matrix Fibronectins Serum Amyloid P-Component medicine.anatomical_structure Otorhinolaryngology Connective tissue metabolism Connective Tissue Chronic Disease Periodontics Blood Vessels Oral Surgery medicine.symptom Carrier Proteins |
| Zdroj: | Journal of oral pathologymedicine : official publication of the International Association of Oral Pathologists and the American Academy of Oral Pathology. 23(8) |
| ISSN: | 0904-2512 |
| Popis: | The lesion of chronic periodontitis is characterized by the persistence of perivascular collections of degenerate plasma cells. In this study, immunohistochemical demonstration of amyloid P (AP) component was used to define the distribution of this protein in established periodontitis lesions and in biopsies of non-destructive marginal gingivitis. Quantitative assessment of AP indicated significantly higher levels in periodontitis than in gingivitis for all regions of the tissue. This was associated with pathology as determined by the intensity of plasma cell accumulation and the extent of connective tissue matrix degradation. AP was concentrated in the deep connective tissue areas but perivascular accumulation was also noted, as was deposition associated with nerve bundles and, occasionally, in the extracellular matrix of the lining epithelium. These findings have potential significance in relation to the pathology of chronic periodontitis as AP has been shown to interact in a calcium-dependent manner with a number of ligands including fibronectin, elastic fibres, C-4 binding protein and amyloid fibrils. |
| Databáze: | OpenAIRE |
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