Molecular and Pathological Analysis of Anticoagulant Heparan Sulfate Proteoglycan from Endothelial Cell

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We have isolated a cDNA of the human ryudocan core protein encoding a 2,610 bp transcript, which potentially codes for a 198 amino acid protein. Comparison of the deduced core proteina between the human and the rat ryudocan revealed that they have high structural conservation, particularly in the NH_2 and COOH terminus regions of the putative mature core protein, which might serve important roles for biological function of ryudocan. A major 2.7kb transcript was detected in all tissues tested, with relatively high levels of expression observed in mRNA from lung, liver, skeletal muscle and kidney. A minor 1.9 kbtranscript was also observed in some of tissues, which would be caused by alternative polyadenylation. Human ryudocan gene has localized on the chromosome 20q12 by fluorescence in situ hybridization. Immuno-histochemical analysis using a specific polyclonal antibody against human ryudocan core protein revealed that ryudocan was expressed in trophoblasts of placental villi and in endothlial cells of neovesseles, but not in those of normal vesseles. Isolation of the human ryudocan core protein cDNA will allow us to study for the regulation of ryudocan expression and the role of this molecule in human endothelial cell function