OSTEOBLAST-SPECIFIC FACTOR-II - CLONING OF A PUTATIVE BONE ADHESION PROTEIN WITH HOMOLOGY WITH THE INSECT PROTEIN FASCICLIN-I
OSTEOBLAST-SPECIFIC FACTOR-II - CLONING OF A PUTATIVE BONE ADHESION PROTEIN WITH HOMOLOGY WITH THE INSECT PROTEIN FASCICLIN-I
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DOI：
10.1042/bj2940271
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发表时间：
1993-08-15
影响因子：
4.1
通讯作者：
AMANN, E
中科院分区：
文献类型：
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作者：
TAKESHITA, S;KIKUNO, R;AMANN, E
从小鼠成骨细胞系MC 3 T3-E1制备的cDNA文库中筛选特异性表达的基因的存在下，通过采用组合消减杂交/差异筛选方法。鉴定并测序了编码命名为成骨细胞特异性因子2（OSF-2）的蛋白质的cDNA，所述蛋白质包含811个氨基酸。OSF-2具有典型的信号序列，随后是富含半胱氨酸的结构域、四重重复结构域和C端结构域。该蛋白缺乏典型的跨膜区。OSF-2的四重重复结构域显示与昆虫蛋白fasciclin I同源。RNA分析显示，OSF-2在骨中表达，在肺中表达程度较低，但在其他组织中不表达。小鼠OSF-2 cDNA随后用作探针以克隆人对应物。小鼠和人OSF-2显示出高氨基酸序列保守性，除了信号序列和C-末端结构域中的两个区域，其中观察到“框内”插入或缺失，这意味着选择性剪接事件。在与成束蛋白1的氨基酸序列同源性的基础上，我们认为OSF-2在骨形成中起着嗜同性粘附分子的作用。
A cDNA library prepared from the mouse osteoblastic cell line MC3T3-E1 was screened for the presence of specifically expressed genes by employing a combined subtraction hybridization/differential screening approach. A cDNA was identified and sequenced which encodes a protein designated osteoblast-specific factor 2 (OSF-2) comprising 811 amino acids. OSF-2 has a typical signal sequence, followed by a cysteine-rich domain, a fourfold repeated domain and a C-terminal domain. The protein lacks a typical transmembrane region. The fourfold repeated domain of OSF-2 shows homology with the insect protein fasciclin I. RNA analyses revealed that OSF-2 is expressed in bone and to a lesser extent in lung, but not in other tissues. Mouse OSF-2 cDNA was subsequently used as a probe to clone the human counterpart. Mouse and human OSF-2 show a high amino acid sequence conservation except for the signal sequence and two regions in the C-terminal domain in which 'in-frame' insertions or deletions are observed, implying alternative splicing events. On the basis of the amino acid sequence homology with fasciclin 1, we suggest that OSF-2 functions as a homophilic adhesion molecule in bone formation.