BASIGIN, A NEW MEMBER OF THE IMMUNOGLOBULIN SUPERFAMILY - GENES IN DIFFERENT MAMMALIAN-SPECIES, GLYCOSYLATION CHANGES IN THE MOLECULE FROM ADULT ORGANS AND POSSIBLE VARIATION IN THE N-TERMINAL SEQUENCES
BASIGIN, A NEW MEMBER OF THE IMMUNOGLOBULIN SUPERFAMILY - GENES IN DIFFERENT MAMMALIAN-SPECIES, GLYCOSYLATION CHANGES IN THE MOLECULE FROM ADULT ORGANS AND POSSIBLE VARIATION IN THE N-TERMINAL SEQUENCES
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DOI：
10.1247/csf.16.23
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发表时间：
1991-02-01
影响因子：
1.5
通讯作者：
MURAMATSU, T
中科院分区：
文献类型：
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作者：
KANEKURA, T;MIYAUCHI, T;MURAMATSU, T
Basigin是免疫球蛋白超家族的新成员，与免疫球蛋白V结构域和主要组织相容性复合物II类抗原β链具有同源性。Southern印迹分析表明，basigin基因是作为一个单一的拷贝或作为几个拷贝每个小鼠基因组。虽然在仓鼠和人类中检测到同源基因，但Southern和北方印迹实验表明basigin结构具有相当大的种属特异性。N-聚糖酶处理后的胚胎癌细胞basigin的分子量约为32，000，与cDNA序列推测的basigin多肽值接近，证实了basigin的开放阅读框架。在Western印迹法中，在小鼠肾脏中检测到大量的basigin作为与蓖麻凝集素（RCA）-I结合的糖蛋白和作为与伴刀豆球蛋白A结合的糖蛋白;前者的分子量为38，000 - 43，000，后者为30，000。在肝、小肠和脾的RCA-I结合糖蛋白中检测到分子量为48，000的Basigin。因此，不同形式的basigin可以通过不同的糖基化模式产生。basigin异质性的另一个来源可能是N-末端序列的差异，因为鉴定了具有不同5'编码序列的cDNA克隆。
Basigin is a new member of the immunoglobulin superfamily with homology to both the immunoglobulin V domain and major histocompatibility complex class II antigen beta-chain. Southern blot analysis indicated that the basigin gene was present as a single copy or as a few copies per mouse genome. Although a homologous gene was detected in the hamster and human, Southern and Northern blotting experiments indicated considerable species specificity in the basigin structure. The molecular weight of N-glycanase-treated basigin from embryonal carcinoma cells was about 32,000 and was close to the value of basigin polypeptide inferred from the cDNA sequence; the result confirmed the open reading frame of basigin. Upon Western blotting, large amounts of basigin were detected in the mouse kidney as a glycoprotein bound to Ricinus communis agglutinin (RCA)-I and as a glycoprotein bound to concanavalin A; the molecular weight of the former was 38,000-43,000, and of the latter was 30,000. Basigin of the molecular weight of 48,000 was detected in RCA-I-binding glycoproteins of the liver, small intestine and spleen. Thus, different forms of basigin can be produced by different modes of glycosylation. Another source of heterogeneity of basigin may be differences in N-terminal sequences, since cDNA clones with different 5' coding sequences were identified.