Bouvet J P, Hocini H, Iscaki S
Unité d'Immunologie Microbienne, Institut Pasteur, Paris, France.
Scand J Immunol. 1992 Jan;35(1):79-83. doi: 10.1111/j.1365-3083.1992.tb02836.x.
Secretory immunoglobulins A (SIgA) and M (SIgM) were investigated in 20 sera containing high levels of monoclonal polymeric IgM or IgA. In the sera of patients suffering from Waldenström's macroglobulinemia (WM), the level of SIgA was found to be low, whereas that of SIgM was extremely high. Reciprocally, in the multiple myeloma (MM) patients, SIgA were increased and SIgM were dramatically decreased. Electrophoretic analysis showed these SIgA and SIgM to have the same monoclonal pattern as the corresponding paraprotein. Hence these molecules must originate from the malignant clone. The most likely mechanism involved is an intravascular formation of the secretory-like immunoglobulins. Free secretory component (SC) could diffuse passively from the digestive lumen and bind the circulating myeloma polymeric immunoglobulins. Such a possibility of in vivo binding of free SC to IgM and IgA polymers leads to a reconsideration of the secretory origin of SIgM and SIgA in normal human serum.
对20份含有高水平单克隆聚合免疫球蛋白M或免疫球蛋白A的血清中的分泌型免疫球蛋白A（SIgA）和免疫球蛋白M（SIgM）进行了研究。在患有华氏巨球蛋白血症（WM）的患者血清中，发现SIgA水平较低，而SIgM水平极高。相反，在多发性骨髓瘤（MM）患者中，SIgA升高而SIgM显著降低。电泳分析表明，这些SIgA和SIgM与相应的副蛋白具有相同的单克隆模式。因此，这些分子必定源自恶性克隆。最可能涉及的机制是分泌型免疫球蛋白在血管内形成。游离分泌成分（SC）可从消化管腔被动扩散并结合循环中的骨髓瘤聚合免疫球蛋白。游离SC在体内与IgM和IgA聚合物结合的这种可能性导致对正常人血清中SIgM和SIgA的分泌起源的重新思考。
