1-palmitoyl-2-linoleoylphosphatidylcholine and Amyloidosis

In AL-amyloidosis the cause of amyloid fibril formation in beta-pleated sheets from the precursor protein immunoglobulin light chain is not established, but studies of AL-proteins indicate that amino acid substitutions are important in the pathogenesis. Amyloid material was extracted from a subcutaneous fat tissue biopsy and submitted to extended protein separation, typing and amino acid sequence analyses. The AL-protein belonged to the rare immunoglobulin light chain kappa, subtype kappa IV and contained unique amino acid substitutions, mostly in the highly preserved framework regions. The study shows that subcutaneous fat biopsies are useful sources of amyloid material for biochemical studies.

Topics: Abdomen; Adipose Tissue; Amino Acid Sequence; Amino Acid Substitution; Amyloid; Amyloidosis; Biopsy; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Humans; Immunoglobulin kappa-Chains; Immunoglobulin Light Chains; Molecular Sequence Data; Molecular Weight; Phosphatidylcholines