Jj. Liepnieks et al., SYSTEMIC IMMUNOGLOBULIN (AL) AMYLOIDOSIS IN A CAT - COMPLETE PRIMARY STRUCTURE OF A FELINE LAMBDA-LIGHT CHAIN, AMYLOID-INTERNATIONAL JOURNAL OF EXPERIMENTAL AND CLINICAL INVESTIGATION, 3(3), 1996, pp. 177-182
A tarsal mass removed from a ten year old cat proved to be an extramed
ullary plasmacytoma largely composed of amyloid. Systemic amyloidosis
was indicated when histological examination at necropsy identified amy
loid also in the lymph nodes, spleen and liver. The amyloid subunit pr
otein was isolated by molecular sieve chromatography of reduced and al
kylated fibrils extracted from the mass, and its amino acid sequence w
as determined by sequence analysis of peptides isolated after digestio
n with trypsin or Stapylococcus protease. The sequence of the C-termin
al half of the protein was homologous to the constant region of immuno
globulin lambda light chains of other species establishing the immunog
lobulin origin of the amyloid. The N-terminal half of the protein was
homologous to the variable region of human lambda light chains and con
tained several rare residues in the framework regions. To our knowledg
e, this is the first complete sequence determination of a feline immun
oglobulin light chain, and the first complete sequence determination o
f an amyloid immunoglobulin light chain from a species other than man.