Amyloidosis stained with Anti-Serum Amyloid A
Serum Amyloid A(SAA) is an acute-phase protein primarily synthesized in the liver. While it is typically found at low concentrations in healthy individuals, pro-inflammatory cytokines upregulates SAA productio to encourage recruitment of immune cells to inflammatory sites. Amyloidosis is a disease characterized by the abnormal build-up of amyloid, abnormal non-branching fibillary beta pleated sheet proteins thatare insoluble and highly resistant to proteolytic degradation that result into localized or systemic organ dysfunction. Amyloidosis are grouped as AL(primary), AA(secondary) and hereditary forms. Proper classification is important since treatment and prognosis of the disorders are vastly different. AA(secondary) amyloidosis is associated with a variety of chronic inflammatory conditions and infections, derived from SAA. Immunohistochemical staining using a panel of antibodies including kappa and lambda Ig light chains, amyloid A and transthyretin can aid in recognizing most forms of amyloid.
Serum Amyloid A(SAA) is an acute-phase protein primarily synthesized in the liver. While it is typically found at low concentrations in healthy individuals, pro-inflammatory cytokines upregulates SAA productio to encourage recruitment of immune cells to inflammatory sites. Amyloidosis is a disease characterized by the abnormal build-up of amyloid, abnormal non-branching fibillary beta pleated sheet proteins thatare insoluble and highly resistant to proteolytic degradation that result into localized or systemic organ dysfunction. Amyloidosis are grouped as AL(primary), AA(secondary) and hereditary forms. Proper classification is important since treatment and prognosis of the disorders are vastly different. AA(secondary) amyloidosis is associated with a variety of chronic inflammatory conditions and infections, derived from SAA. Immunohistochemical staining using a panel of antibodies including kappa and lambda Ig light chains, amyloid A and transthyretin can aid in recognizing most forms of amyloid.
