MONOCLONAL-ANTIBODY TO A HIGHLY GLYCOSYLATED PROTEIN REACTS IN FIXED TISSUE WITH MELANOMA AND OTHER TUMORS
MONOCLONAL-ANTIBODY TO A HIGHLY GLYCOSYLATED PROTEIN REACTS IN FIXED TISSUE WITH MELANOMA AND OTHER TUMORS
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DOI：
10.1089/hyb.1985.4.243
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发表时间：
1985-01-01
期刊：
影响因子：
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通讯作者：
KOPROWSKI, H
中科院分区：
文献类型：
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作者：
ATKINSON, B;ERNST, CS;KOPROWSKI, H
抗黑色素瘤单克隆抗体已鉴定出分子量为30，000至60，000且蛋白质核心为20，000道尔顿的高度糖基化蛋白质。这种黑色素瘤相关糖蛋白（MAG）的抗原性在固定石蜡包埋的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（31/33）和一半的转移性黑色素瘤（5/10）中。正常黑素细胞不表达该抗原。发育不良痣与抗MAG抗体的强反应性与放射状生长期黑色素瘤中观察到的反应性相当。复合痣的抗原表达要弱得多，其反应范围从交界处和真皮上部的中度到痣基底部的缺失。
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.