Cytoplasmic domain is not essential for the cell adhesion activities of gicerin, an Ig-superfamily molecule.
Cytoplasmic domain is not essential for the cell adhesion activities of gicerin, an Ig-superfamily molecule.
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细胞质结构域对于 Ig 超家族分子 gicerin 的细胞粘附活性不是必需的。
作者：
E. Taira;T. Nagino;Y. Tsukamoto;S. Okumura;O. Muraoka;F. Sakuma;N. Miki
Gicerin是免疫球蛋白（IG）超家族中的细胞粘附分子，并且在神经系统发育期间大量表达。它具有嗜同性细胞粘附活性，也具有与NOF（神经突生长因子）的嗜异性结合活性，并介导神经突延伸。存在两种gicerin同种型，一种具有短的（s-gicerin），另一种具有较长的胞质结构域（l-gicerin）。我们已经报道，s-gicerin具有更强的活动比l-gicerin在细胞聚集，在NOF结合，并在神经突起的延伸。在这项研究中，我们建立了细胞系，表达的muclida-gicerin的胞质结构域被删除，我们比较了上述三个生物活性的muclida-gicerin的s-和l-gicerin。我们发现，muclid-gicerin保留了所有这些活动，但活动弱于s-gicerin和几乎相同的l-gicerin。我们的结论是，gicerin的胞质结构域是不是必不可少的最佳粘附活动的gicerin，但可能参与其活动的调节。
Gicerin is a cell adhesion molecule in the immunoglobulin (Ig) superfamily and is expressed abundantly during development in the nervous system. It has homophilic cell adhesion activity and also has heterophilic binding activity with NOF (neurite outgrowth factor) and mediates neurite extension. There are two isoforms of gicerin, one with a short (s-gicerin) and the other with a longer cytoplasmic domain (l-gicerin). We have reported that s-gicerin possesses stronger activities than l-gicerin during cell aggregation, in NOF-binding, and in neurite extension. In this study, we established cell lines which expressed a mutant-gicerin whose cytoplasmic domain was deleted and we compared the above three biological activities of the mutant-gicerin with those of s- and l-gicerin. We found that the mutant-gicerin retained all these activities, but the activities were weaker than those of s-gicerin and almost the same as those of l-gicerin. We concluded that the cytoplasmic domain of gicerin is not essential for optimal adhesive activities of gicerin, but might be involved in the regulation of its activities.
影响因子：
56.9
作者：
RUTISHAUSER, U;ACHESON, A;SUNSHINE, J
通讯作者：
SUNSHINE, J