Evidence for calmodulin binding to the cytoplasmic domains of two C‐CAM isoforms

FEBS Letters

Öbrink, Björn¹  Edlund, Magnus¹ 

[1] Department of Cell and Molecular Biology, Medical Nobel Institute, Karolinska Institutet, Box 60400, S-104 01 Stockholm, Sweden

关键词: Adhesion;    Calcium;    Calmodulin;    C-CAM;    Immunoglobulin super-family;    BGP;    biliary glycoprotein;    cDNA;    complementary DNA;    kDa;    kilodalton;    MBP;    maltose binding protein;    PAGE;    polyacrylamide gel electrophoresis;    PCR;    polymerase chain reaction;    RT;    reverse transcriptase;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/0014-5793(93)81046-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

C-CAM (cell-CAM 105) is a transmembrane cell adhesion molecule, belonging to the immunoglobulin superfamily. It is expressed in epithelia, vessel endothelia and leukocytes, and mediates intercellular adhesion in rat hepatocytes by homophilic binding. Two major isoforms (C-CAM1 and C-CAM2) that differ in their cytoplasmic domains occur. A previous study demonstrated that C-CAM can bind calmodulin in a Ca²⁺-dependent manner. In this study we have expressed the cytoplasmic domains of C-CAM1 and C-CAM2 in fusion proteins and measured calmodulin binding by a gel overlay assay, using ¹²⁵I-labelled calmodulin. Our results indicate that the cytoplasmic domains of both C-CAM1 and C-CAM2 can bind calmodulin.

【 授权许可】

Unknown