Expression and Functional Analysis of a Novel Isoform of Gicerin, an Immunoglobulin Superfamily Cell Adhesion Molecule (*)
Expression and Functional Analysis of a Novel Isoform of Gicerin, an Immunoglobulin Superfamily Cell Adhesion Molecule (*)
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免疫球蛋白超家族细胞粘附分子 Gicerin 的新型异构体的表达和功能分析 (*)
DOI:
10.1074/jbc.270.48.28681
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发表时间:
1995
期刊:
影响因子:
--
通讯作者:
N. Miki
中科院分区:
文献类型:
--
作者:
E. Taira;T. Nagino;H. Taniura;N. Takaha;Cheol‐Hee Kim;C. Kuo;Bing;Hiroshi Higuchi;N. Miki
We have cloned a novel cDNA of gicerin, a cell adhesion molecule belonging to the immunoglobulin superfamily. Both gicerin isoforms share the same extracellular domain, which has five immunoglobulin-like loop structures and a transmembrane domain as s-gicerin, but differ in the cytoplasmic tail domain. As the newly identified form has a larger cytoplasmic domain than the previously reported form, we refer to them as l-gicerin and s-gicerin, respectively. l-gicerin is transcribed from a distinct mRNA containing an inserted sequence not found in s-gicerin mRNA which caused a frameshift for the coding region for a cytoplasmic domain. Previous studies demonstrated that gicerin showed a doublet band of 82 and 90 kDa in chicken gizzard smooth muscle. We report that the 82-kDa protein corresponds to s-gicerin and the 90-kDa protein to l-gicerin. We also found that the two gicerin isoforms are expressed differentially in the developing nervous system. Functional analysis of these gicerin isoforms in stable transfectants revealed that they had differ in their homophilic adhesion properties, as well as in heterophilic cell adhesion assayed with neurite outgrowth factor. In addition, these isoforms have neurite-promoting activity by their homophilic adhesion, but differ in their ability to promote neurite outgrowth.