Atkinson B, Ernst C S, Ghrist B F, Ross A H, Clark W H, Herlyn M, Herlyn D, Maul G, Steplewski Z, Koprowski H
Hybridoma. 1985 Fall;4(3):243-55. doi: 10.1089/hyb.1985.4.243.
A highly glycosylated protein with a molecular weight of 30,000 to 60,000 and a protein core of 20,000 daltons has been identified by antimelanoma monoclonal antibodies. The antigenicity of this melanoma-associated glycoprotein (MAG) was not destroyed in fixed paraffin-embedded melanoma tissue, and was present in malignant cells of cutaneous superficial spreading melanomas in skin (31/33) and in half of all metastatic melanomas examined (5/10). The antigen was not expressed by normal melanocytes. The strong reactivity of dysplastic nevi with the anti-MAG antibodies was comparable to that seen in radial growth phase melanoma. Antigen expression was much weaker in compound nevi where reactivity ranged from moderate in the junctional component and the upper dermis to absent at the base of the nevus.
抗黑色素瘤单克隆抗体已识别出一种高度糖基化的蛋白质，其分子量为30,000至60,000，蛋白质核心为20,000道尔顿。这种黑色素瘤相关糖蛋白（MAG）的抗原性在固定的石蜡包埋黑色素瘤组织中未被破坏，并且存在于皮肤浅表扩散性黑色素瘤的恶性细胞中（31/33）以及所检查的所有转移性黑色素瘤的一半中（5/10）。正常黑素细胞不表达该抗原。发育异常痣与抗MAG抗体的强反应性与在放射状生长期黑色素瘤中所见相当。在复合痣中抗原表达要弱得多，其反应性在交界成分和真皮上层为中度，在痣底部则不存在。
