We describe as nomenclature, classification, statistics, clinicopathology, histology, histochemistory, and ultrastructure of amyloid and amyloidosis. Amyloidosis is a disease caused by deposition of amyloid proteins in various tissues and organs. Amyloid is morphologically characterized by its birefringence and dichroism after Congo red stain, and its ultrastructure. The classification of amyloid and amyloidosis is based on the amyloid fibril proteins, followed by a designation of the fibril protein precursor. To date, 15 proteins have been identified as constituents of amyloid fibrils in clinically diverse conditions. Amyloid proteins derived from serum amyloid A(AA) in secondary amyloidosis, immunoglobulin light chain (AL) in primary amyloidosis, transthyretin (ATTR) in familial amyloidotic polyneuropathy FAP) and systemic senile amyloidosis, β2-microglobulin (Aβ2M) in hemodialysis associated amyloidosis, and rarely immunoglobulin heavy chain (AH), apolipoprotein A l(AApoA 1) in FAP typeIII, gelsolin (AGel) in FAP typeIV. Deposition of Aβ amyloid derived from β protein are common findings in the brain of patients with Alzheimer's disease and cortical hemorrhage, AIAPP from amylin in islets of Langerhans of patients with diabetes typeII , and AANF from atrail natriuretic factor in the atrium of advanced age in human. The pathogenesis of amyloidosis is also discussed. Amyloid enhancing factor (AEF) is associated with several forms of amyloidosis and play an important role for the pathogenesis in experimental amyloidosis. Amyloid fibres are seen mainely in the interstitia of the various organs. Aggregates of amyloid fibrils have been observed in proximity to cells, oriented perpendicularly to. and merging with, the cell membrane. Inrracyoplasmic amyloid fibrils are noted in several cases, mainely in localized amyloidosis.