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Abstrak :
The second edition of this text presents an overview of the most recent developments in this area including clinical presentation, etiology, pathogenesis, and differential diagnosis. The rationale for various therapies, including transplantation, is discussed and tissue diagnosis (its pitfalls and strategies for avoiding them) and laboratory support are included. The involvement of all major organ systems including renal/genitourinary, cardiac, gastrointestinal, pulmonary, peripheral nerve/central nervous system, soft tissue, skin, lymph node/spleen and bone marrow pathology is also covered.

Abstrak :
Amyloidosis is a rare disease, when diagnosed it's incurable and mostly affect over 40 years old male. Diagnostic is confirmed if histopathologic stained positive with Congo red and evidence of monoclonal protein. Survivals for untreated patients are 13 months in primary amyloidosis but if secondary to other chronic disease and systemic, survival could be 3-4 years. It can not be prevented but when affected, control of the underlying illness can prevent progression of amyloidosis. We report a rare case of a 67 year old male, who came with chronic diarrhea. The stool analysis, there were no negative gram microorganisme found, only food maldigestion and fungus infection. Stool analyze from parasitology department were found microspore, but the stool culture were sterile. The patient underwent colonoscopy which revealed hyperemis mucosa in rectum, sigmoid, descending & transverse colon. From the biopsy was concluded intestinal amyloidosis. We treated the patient symptomatically and couldn't find the underlying inflammatory disease which causes the problem.

Abstrak :
Amyloid-forming proteins are implicated in over 30 human diseases. The proteins involved in each disease have unrelated sequences and dissimilar native structures, but they all undergo conformational alterations to form fibrillar polymers. The fibrillar assemblies accumulate progressively into disease-specific lesions in vivo. Substantial evidence suggests these lesions are the end state of aberrant protein folding whereas the actual disease-causing culprits likely are soluble, non-fibrillar assemblies preceding the aggregates. The non-fibrillar protein assemblies range from small, low-order oligomers to spherical, annular, and protofibrillar species. Oligomeric species are believed to mediate various pathogenic mechanisms that lead to cellular dysfunction, cytotoxicity, and cell loss, eventuating in disease-specific degeneration and systemic morbidity. The particular pathologies thus are determined by the afflicted cell types, organs, systems, and the proteins involved. Evidence suggests that the oligomeric species may share structural features and possibly common mechanisms of action. In many cases, the structure–function interrelationships amongst the various protein assemblies described in vitro are still elusive. Deciphering these intricate structure–function correlations will help understanding a complex array of pathogenic mechanisms, some of which may be common across different diseases albeit affecting different cell types and systems.