Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Amyloidoses are characterized by the deposition of non soluble proteins in tissues. Clinical aspects of hereditary amyloidoses are very diverse, and they offer many diagnosis problems to the physician. Biochemical and genetic aspects are also various. Several proteins are implicated in these hereditary diseases mainly: transthyretin, apolipoprotein A1, gelsolin, fibrinogen alpha chain and lysozyme. Studies on structural changes induced by the mutations in the transthyretin should bring new data relevant to our understanding of the amyloidogenic process. Transgenic mice with mutated transthyretin are a good model and will allow new pathogenic approach and therapeutic intervention.
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PMID:[Hereditary amyloidosis]. 805 45

Clinical aspects of hereditary amyloidoses are very diverse, and they pose many diagnostic problems to the physician. Biochemical and genetic aspects are also various. Several proteins are implicated in these hereditary diseases: transthyretin, apolipoprotein A1, gelsolin, fibrinogen alpha chain and lysozyme. Studies on structural changes induced by the mutations in these proteins should bring new data relevant to our understanding of the amyloidogenic process. Familial mediterranean fever is a hereditary disease of the inflammatory reaction which is associated with AA amyloidosis.
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PMID:[Hereditary amyloidosis]. 945 3

Amyloidosis has traditionally been of a few defined varieties, most commonly including light-chain amyloidosis (AL amyloidosis) and secondary amyloidosis due to chronic inflammation (AA amyloidosis). Apolipoprotein A-I/A-II cystatin C, gelsolin, lysozyme, fibrinogen alpha chain, beta 2 microglobulin, and transthyretin familial amyloidosis represent rarer but reported varieties. Ten years ago, the first reports linked leukocyte chemotactic factor 2 (LECT2) amyloidosis as a pathological agent identified as a novel class of amyloid-generating protein. Epidemiology suggested that this was a new cause of amyloidosis that is especially common in Hispanic patients and somewhat common among patients from the Middle East-North Africa (MENA) region. We report a case of splenic and renal LECT 2 amyloidosis in a 62-year- old Hispanic male with diabetes mellitus. After an unremarkable serological workup, LECT 2 amyloidosis was diagnosed on renal biopsy. The case presentation is reviewed as a typical presentation, and the literature is reviewed regarding this newly reported entity, resulting in infiltrative renal amyloidosis and chronic renal disease.
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PMID:A case of renal and splenic LECT 2 amyloidosis: A recently recognized cause of renal and systemic amyloidosis. 3239 25

Amyloidosis is a diverse group of protein conformational disorder which is caused by accumulation and deposition of insoluble protein fibrils in vital tissues or organs, instigating organ dysfunction. Renal amyloidosis is characterized by the acellular Congo red-positive pathologic deposition of amyloid fibrils within glomeruli and/or the interstitium. It is generally composed of serum amyloid A-related protein or an immunoglobulin light chain; other rare forms lysozyme, gelsolin, fibrinogen alpha chain, transthyretin, apolipoproteins AI/AII/AIV/CII/CIII; and the recently identified form ALECT2. This disease typically manifests with heavy proteinuria, nephrotic syndrome, and finally progression to end-stage renal failure. Early diagnosis of renal amyloidosis is arduous as its symptoms appear in later stages with prominent amyloid deposition. The identification of the correct type of amyloidosis is quite troublesome as it can be confused with another related form. Therefore, the exact typing of amyloid is essential for prognosis, treatment, and correct management of renal amyloidosis. The emanation of new techniques of proteomic analysis, for instance, mass spectroscopy/laser microdissection, has provided greater accuracy in amyloid typing. This in-depth review emphasizes on the clinical features, renal pathological findings, and diagnosis of the AL and non-AL forms of renal amyloidosis.
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PMID:Renal amyloidosis: an update on diagnosis and pathogenesis. 3244 67

To clarify the significance of quantitative analyses of amyloid proteins in clinical practice and in research relating to systemic amyloidoses, we applied mass spectrometry-based quantification by isotope-labeled cell-free products (MS-QBIC) to formalin-fixed, paraffin-embedded (FFPE) tissues. The technique was applied to amyloid tissues collected by laser microdissection of Congo red-stained lesions of FFPE specimens. Twelve of 13 amyloid precursor proteins were successfully quantified, including serum amyloid A (SAA), transthyretin (TTR), immunoglobulin kappa light chain (IGK), immunoglobulin lambda light chain (IGL), beta-2-microglobulin (B2M), apolipoprotein (Apo) A1, Apo A4, Apo E, lysozyme, Apo A2, gelsolin, and fibrinogen alpha chain; leukocyte cell-derived chemotaxin-2 was not detected. The quantification of SAA, TTR, IGK, IGL, and B2M confirmed the responsible proteins, even when the immunohistochemical results were not decisive. Considerable amounts of Apo A1, Apo A4, and Apo E were deposited in parallel amounts with the responsible proteins. Quantification of amyloid protein by MS-QBIC is feasible and useful for the classification of and research on systemic amyloidoses.
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PMID:Mass spectrometry-based absolute quantification of amyloid proteins in pathology tissue specimens: Merits and limitations. 3260 50