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  1. Oweity T, West AB, Stokes MB
    Int. J. Surg. Pathol., 2001 Apr;9(2):149-54.
    PMID: 11484503
    A 71-year-old man with intestinal pseudo-obstruction was found to have a diffusely thickened adynamic small bowel with AA-amyloid in submucosal vessels and muscularis propria, foreign body giant cell reaction to amyloid, and necrotizing angiitis. The mucosa was unremarkable. Immunostains demonstrated numerous CD68+ monocyte/macrophages and CD8+ T cells associated with the amyloid deposits. The patient had no evidence of systemic vasculitis and no underlying cause for AA-amyloidosis was identified. Necrotizing angiitis coexistent with amyloid angiopathy has been reported in brain and temporal arteries, but not in the gastrointestinal tract and not with AA-amyloid. The inflammatory cell infiltrates in this case are consistent with a foreign-body and/or cell-mediated immunologic reaction to AA-amyloid, although a role for these cells in amyloid formation cannot be excluded.
    Matched MeSH terms: Serum Amyloid A Protein/analysis*
  2. Looi LM
    Australas J Dermatol, 1991;32(1):39-44.
    PMID: 1930004
    A review of consecutive biopsies from 85 Malaysian patients with primary localised cutaneous amyloidosis (PLCA) revealed 63 with papular amyloidosis (PA) and 22 with macular amyloidosis (MA). PLCA appeared to affect the Chinese more frequently than the other major ethnic groups but MA was more common than expected among the Indians. Of patients with PA, one had systemic lupus erythematosus, one scleroderma and in another, connective tissue disease was suspected. MA was not found to be associated with any other disease. Histologically, PA differed from MA by the larger size of amyloid deposits in the papillary dermis. There was no difference in their tinctorial and immunohistochemical characteristics. Deposits were permanganate-resistant and negative for AA protein, immunoglobulin light chains and keratin. A few cases exhibited positively for cytokeratin. Strong immunoreactivity for AP protein was observed. PA and MA appear chemically similar and are likely to be of epidermal origin.
    Matched MeSH terms: Serum Amyloid A Protein/analysis
  3. Looi LM, Jayalakshim P, Lim KJ, Rajagopalan K
    Ann Acad Med Singap, 1988 Oct;17(4):573-8.
    PMID: 3223746
    Congo red screening of tissue blocks from 37 consecutive autopsies on leprosy patients revealed 7 cases of systemic amyloidosis, indicating a prevalence rate of 19%. 5 were males and 2 females. All were ethnic Chinese. Their ages ranged from 52 to 85 years with a mean of 69 years. Six had lepromatous leprosy while the remaining 1 had tuberculoid leprosy. In all 7 cases, the amyloid was AA in type, being permanganate-sensitive and immunoreactive with anti-human AA protein antiserum. Hepatic deposition was limited to blood vessels, a pattern typical of AA (secondary) amyloidosis. With regard to renal involvement, 4 showed a predominantly vascular pattern of infiltration while 3 exhibited the more ominous glomerular pattern. Three died of chronic renal failure and 2 of congestive cardiac failure attributable to renal and cardiac amyloidosis respectively. One patient succumbed to septicaemia and the remaining 1 to acute myocardial infarction. AA amyloidosis remains a serious and significant complication of leprosy among Malaysians.
    Matched MeSH terms: Serum Amyloid A Protein/analysis
  4. Odhah MN, Jesse FFA, Lawan A, Idris UH, Marza AD, Mahmood ZK, et al.
    Microb Pathog, 2018 Apr;117:243-246.
    PMID: 29481974 DOI: 10.1016/j.micpath.2018.02.038
    Haptoglobin (Hp) and Serum Amyloid A (SAA) are a group of blood proteins whose concentrations in animals can be influenced by infection, inflammation, surgical trauma or stress. Corynebacterium pseudotuberculosis is the causative agent of caseous lymphadenitis (CLA), and Mycolic acid is a virulent factor extracted from C. pseudotuberculosis. There is a dearth of sufficient evidence on the clinical implication of MAs on the responses of Hp and SAA in goats. Therefore, this study was conducted to evaluate the potential effects of Mycolic acid (MAs) and C. pseudotuberculosis on the responses of Hp and SAA in female goats. A total of 12 healthy female goats was divided into three groups; A, B and C each comprising of 4 goats and managed for a period of three months. Group (A) was inoculated with 2 mL of sterile phosphate buffered saline (as a negative control group) intradermally, while group (B) and (C) were inoculated intradermally with 2 ml each of mycolic acid and 1‏ × 109 cfu of active C. pseudotuberculosis respectively. The result of the study showed that the Hp concentration in goats inoculated with C. pseudotuberculosis was significantly increased up to 7-fold (1.17 ± 0.17 ng/L) while MAs showed a 3-fold increased (0.83 ± 0.01 ng/L) compared with the control. Whereas SAA concentration in C. pseudotuberculosis and MAs groups showed a significant 3-fold (17.85 ± 0.91 pg/mL) and 2-fold (10.97 ± 0.71 pg/mL) increased compared with the control. This study concludes that inoculation of C. pseudotuberculosis and MAs have significant effects on Hp and SAA levels, which indicates that MAs could have a role in the pathogenesis of caseous lymphadenitis.
    Matched MeSH terms: Serum Amyloid A Protein/analysis
  5. Fish-Low CY, Than LTL, Ling KH, Sekawi Z
    J Proteome Res, 2024 Sep 06;23(9):4027-4042.
    PMID: 39150348 DOI: 10.1021/acs.jproteome.4c00376
    Leptospirosis, a notifiable endemic disease in Malaysia, has higher mortality rates than regional dengue fever. Diverse clinical symptoms and limited diagnostic methods complicate leptospirosis diagnosis. The demand for accurate biomarker-based diagnostics is increasing. This study investigated the plasma proteome of leptospirosis patients with leptospiraemia and seroconversion compared with dengue patients and healthy subjects using isobaric tags for relative and absolute quantitation (iTRAQ)-mass spectrometry (MS). The iTRAQ analysis identified a total of 450 proteins, which were refined to a list of 290 proteins through a series of exclusion criteria. Differential expression in the plasma proteome of leptospirosis patients compared to the control groups identified 11 proteins, which are apolipoprotein A-II (APOA2), C-reactive protein (CRP), fermitin family homolog 3 (FERMT3), leucine-rich alpha-2-glycoprotein 1 (LRG1), lipopolysaccharide-binding protein (LBP), myosin-9 (MYH9), platelet basic protein (PPBP), platelet factor 4 (PF4), profilin-1 (PFN1), serum amyloid A-1 protein (SAA1), and thrombospondin-1 (THBS1). Following a study on a verification cohort, a panel of eight plasma protein biomarkers was identified for potential leptospirosis diagnosis: CRP, LRG1, LBP, MYH9, PPBP, PF4, SAA1, and THBS1. In conclusion, a panel of eight protein biomarkers offers a promising approach for leptospirosis diagnosis, addressing the limitations of the "one disease, one biomarker" concept.
    Matched MeSH terms: Serum Amyloid A Protein/analysis
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