Useful polyclonal antibodies against synthetic peptides corresponding to immunoglobulin light chain constant region for immunohistochemical detection of immunoglobulin light chain amyloidosis
Useful polyclonal antibodies against synthetic peptides corresponding to immunoglobulin light chain constant region for immunohistochemical detection of immunoglobulin light chain amyloidosis
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DOI：
10.1046/j.1440-1827.2001.01198.x
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发表时间：
2001-04-01
影响因子：
2.2
通讯作者：
Ishihara, T
中科院分区：
文献类型：
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作者：
Hoshii, Y;Setoguchi, M;Ishihara, T
为了对福尔马林固定、石蜡包埋的组织切片上的免疫球蛋白 (lg) 轻链淀粉样变性进行免疫组织化学检测，我们制备了针对对应于 Ig lambda 轻链第 118-134 位和 Ig kappa 轻链第 116-133 位的合成肽的多克隆抗体。用这些抗体检测了19例系统性Ig lambda轻链淀粉样变性（A lambda淀粉样变性）、10例系统性lg kappa轻链淀粉样变性（A kappa淀粉样变性）、1例免疫组化未分类的系统性淀粉样变性和5例局限性A lambda淀粉样变性，抗-lambda（118-134）抗血清和亲和纯化的抗体均与19例系统性A lambda淀粉样变性病例中的18例和所有局限性A lambda淀粉样变性病例，尽管在系统性和局限性淀粉样变性中同一标本的不同区域的免疫表达强度有所不同。与抗 lambda (118-134) 抗血清反应的浆细胞和血清中的信号强度弱于用市售抗 lg lambda 轻链抗体、抗 κ (116-133) 抗血清和与 10 例系统性 A κ 淀粉样变性病例中的 9 例反应的亲和纯化抗体获得的信号。我们得出结论，这些针对对应于 lg 轻链恒定区的合成肽的抗体可用于分类福尔马林固定、石蜡包埋的组织切片上的淀粉样变性。
For the immunohistochemical detection of immunoglobulin (lg) light chain amyloidosis on formalin-fixed, paraffin-embedded tissue sections, we prepared polyclonal antibodies against synthetic peptides corresponding to positions 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 lambda amyloldosis), 10 cases of systemic lg kappa light chain amyloidosis (A kappa amyloidosis), one case of immunohistochemically unclassified systemic amyloidosis and five cases of localized A lambda amyloidosis were tested with these antibodies, Anti-lambda (118-134) antiserum and the affinity-purified antibody both reacted with 18 of the 19 cases of systemic A lambda amyloidosis and all cases of localized A lambda amyloidosis, although the immunoexpression was somewhat variable in intensity in different areas within the same specimen in both systemic and localized amyloidosis. The signal intensities in plasma cells and serum reacted for anti-lambda (118-134) antiserum were weaker than signals obtained with commercially available anti-lg lambda light chain antibodies, Anti-kappa (116-133) antiserum and the affinity-purified antibody reacted with nine of the 10 cases of systemic A kappa amyloidosis, We conclude that these antibodies against synthetic peptides corresponding to the lg light chain constant region are useful for the classification of amyloidosis on formalin-fixed, paraffin-embedded tissue sections.