Wessel G M, Zhang W, Klein W H
Department of Biochemistry and Molecular Biology, University of Texas, M.D. Anderson Cancer Center, Houston 77030.
Dev Biol. 1990 Aug;140(2):447-54. doi: 10.1016/0012-1606(90)90093-x.
In this study, myosin heavy chain from sea urchin pluteus larvae was characterized by analysis of a 2.5-kb cDNA clone. DNA sequence of 1465 bp demonstrated a 71% similarity in the deduced amino acid sequence to the embryonic rat skeletal muscle sequence. Antibodies generated against a polypeptide encoded by the open reading frame of the cDNA clone specifically identified a 210-kDa myosin protein which accumulated in 8-12 muscle cells differentiating bilateral to the esophagus beginning at early larval stages. This same myosin also accumulated in cells of the endodermal epithelium that comprise the three sphincters of the larval gut. Thus, a gene encoding myosin heavy chain is expressed in dissimilar cell types of the macromere lineage, and the pattern of accumulation in the gut identifies functionally distinct cells of the endodermal epithelium.
在本研究中,通过对一个2.5kb cDNA克隆的分析,对海胆长腕幼虫的肌球蛋白重链进行了表征。1465bp的DNA序列显示,推导的氨基酸序列与胚胎大鼠骨骼肌序列有71%的相似性。针对该cDNA克隆开放阅读框编码的多肽产生的抗体特异性识别出一种210kDa的肌球蛋白蛋白,该蛋白从幼虫早期开始在食管两侧分化的8-12个肌肉细胞中积累。同样的肌球蛋白也在内胚层上皮细胞中积累,这些细胞构成了幼虫肠道的三个括约肌。因此,编码肌球蛋白重链的基因在大卵裂球谱系的不同细胞类型中表达,并且在肠道中的积累模式确定了内胚层上皮中功能不同的细胞。