Useful polyclonal antibodies against synthetic peptides corresponding to immunoglobulin light chain constant region for immunohistochemical detectionof immunoglobulin light chain amyloidosis
Y. Hoshii et al., Useful polyclonal antibodies against synthetic peptides corresponding to immunoglobulin light chain constant region for immunohistochemical detectionof immunoglobulin light chain amyloidosis, PATHOL INT, 51(4), 2001, pp. 264-270
For the immunohistochemical detection of immunoglobulin (lg) light chain am
yloidosis on formalin-fixed, paraffin-embedded tissue sections, we prepared
polyclonal antibodies against synthetic peptides corresponding to position
s 118-134 of Ig lambda light chain and positions 116-133 of Ig kappa light
chain. Nineteen cases of systemic Ig lambda light chain amyloidosis (A lamb
da amyloldosis), 10 cases of systemic lg kappa light chain amyloidosis (A k
appa amyloidosis), one case of immunohistochemically unclassified systemic
amyloidosis and five cases of localized A lambda amyloidosis were tested wi
th these antibodies, Anti-lambda (118-134) antiserum and the affinity-purif
ied antibody both reacted with 18 of the 19 cases of systemic A lambda amyl
oidosis and all cases of localized A lambda amyloidosis, although the immun
oexpression was somewhat variable in intensity in different areas within th
e same specimen in both systemic and localized amyloidosis. The signal inte
nsities in plasma cells and serum reacted for anti-lambda (118-134) antiser
um were weaker than signals obtained with commercially available anti-lg la
mbda light chain antibodies, Anti-kappa (116-133) antiserum and the affinit
y-purified antibody reacted with nine of the 10 cases of systemic A kappa a
myloidosis, We conclude that these antibodies against synthetic peptides co
rresponding to the lg light chain constant region are useful for the classi
fication of amyloidosis on formalin-fixed, paraffin-embedded tissue section
s.