Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0031099 (periodontitis)
 12,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An 18-year-old Caucasian woman has been followed since age 12 years for Ehlers-Danlos syndrome (EDS) with easy bruisability and "cigarette paper scars." Her chief complaint at age 17 years was tooth mobility, especially in the anterior mandible, necessitating the removal of the four incisors. Initial biochemical analysis of cultured skin fibroblasts indicated the presence of pepsin-sensitive type III collagen. Subsequent analysis of cultured skin fibroblasts by the same laboratory and another laboratory found no abnormality in the type III collagen with or without protease treatment. This is in distinction to the finding of abnormal type III collagen in the only two reported patients with EDS and early-onset periodontitis who have had collagen analyses. One of them was diagnosed as EDS type IV and the other as EDS type VIII, although the defects of type III collagen were consistent with EDS type IV. The defect in type III collagen in some patients with early periodontitis and the considerable overlap of the clinical manifestations of EDS types IV and VIII point out the need for further studies of collagen formation and maturation in any patient who has early periodontitis and who has been classified with EDS type IV or VIII.
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PMID:Phenotypic overlap of Ehlers-Danlos syndrome types IV and VIII. 226 May 89

Biochemical alterations in the connective tissue matrix are a common feature of many diseases, and they account in major part for their functional impairment. Such alterations are especially important in acute and chronic inflammatory diseases where they may take the form of degradation of matrix components or their excessive accumulation leading to fibrosis. Although a wealth of morphologic information is available, very little is known about these changes at the biochemical level. Using human gingival tissue as a model, we have carried out studies aimed at assessing the effects of chronic inflammation on the collagen isotypes comprising the connective tissue matrix. Tissue obtained from patients undergoing surgical treatment for periodontitis was separated on the basis of clinical features into healthy and inflamed portions. After confirming the inflammatory status of each specimen histologically, each set of tissue pairs was extracted at 4 degrees C in 0.5 M acetic acid containing 1 mg/ml of pepsin, and the extracted collagens were fractionated with NaCl. Alpha chains were separated by polyacrylamide slab gel electrophoresis, and methods devised for their quantitation. The results showed that the proportions of type I and III collagens present in normal and inflamed tissues did not differ significantly. In contrast, the type V collagen, which accounted for 0.1 to 1.3% of the total collagens present in normal tissue, was increased by 2- to 9-fold in the chronically inflamed tissue. Because of the unique binding and connecting role type V collagen is thought to play, this alteration may have major pathologic and functional significance.
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PMID:The effect of chronic inflammation on the composition of collagen types in human connective tissue. 641 24