ENDO16, A LARGE MULTIDOMAIN PROTEIN FOUND ON THE SURFACE AND ECM OF ENDODERMAL CELLS DURING SEA-URCHIN GASTRULATION, BINDS CALCIUM

ENDO16, A LARGE MULTIDOMAIN PROTEIN FOUND ON THE SURFACE AND ECM OF ENDODERMAL CELLS DURING SEA-URCHIN GASTRULATION, BINDS CALCIUM
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DOI:
10.1006/dbio.1994.1235
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发表时间:
1994-09-01
影响因子:
2.7
通讯作者:
ERNST, SG
ERNST, SG
中科院分区:
生物学3区
文献类型:
--
作者:
SOLTYSIKESPANOLA, M;KLINZING, DC;ERNST, SG

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在海胆原肠形成过程中,Endo16编码一种受发育调节的蛋白质,这种蛋白质被限制在参与肠原肠形成的细胞和海胆胃中。Endo16基因的4680-nt编码区已经从重叠的cdna中测序。序列分析表明,Endo16是一个大的多结构域蛋白,从其氨基端推定的信号序列开始,随后是一个富含半胱氨酸的区域,两个潜在的肝素结合区域,一个由5个聚集重复序列组成的酸性结构域,一个RGD细胞结合基序,以及一组12个额外的酸性重复序列。共聚焦和电镜免疫定位表明,Endo16蛋白存在于细胞外基质中,并与中肠和后肠的内胚层细胞表面相关。这两个不同的酸性重复区域与已知的钙结合序列相似。含有两个假定的钙结合重复区域的重组Endo16蛋白已被证明可以结合放射性钙。在存在和不存在钙的情况下,原肠期蛋白质提取物的胰蛋白酶消化已经证实,钙可以稳定Endo16蛋白,防止蛋白水解降解。(C) 1994学术出版社,Inc.
Endo16 encodes a developmentally regulated protein restricted to cells participating in the formation of the archenteron during sea urchin gastrulation and to the stomach of the pluteus. The 4680-nt coding region of the Endo16 gene has been sequenced from overlapping cDNAs. Sequence analysis revealed that Endo16 is a large multidomain protein starting with a putative signal sequence at its amino terminus which is followed by a cysteine-rich region, two potential heparin-binding regions, an acidic domain of 5 clustered repeats, an RGD cell binding motif, and a group of 12 additional acidic repeats. Immunolocalization by confocal and electron microscopy demonstrate that the Endo16 protein is in the extracellular matrix and associated with the surface of endodermal cells in the mid and hindgut of the archenteron. The two distinct acidic repeat regions are similar to known calcium-binding sequences. A recombinant Endo16 protein containing both putative calcium-binding repeat regions has been shown to bind radioactive calcium. Tryptic digests of gastrula stage protein extracts in the presence and the absence of calcium have established that calcium stabilizes Endo16 protein against proteolytic degradation. (C) 1994 Academic Press, Inc.