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J. Biochem, 1990, Vol. 108, No. 2 297-302
© 1990 Japanese Biochemical Society


research-article

A Heparin Binding Protein Whose Expression Increases during Differentiation of Embryonal Carcinoma Cells to Parietal Endoderm Cells: cDNA Cloning and Sequence Analysis1

Tatsuhiko Furukawa, Masayuki Ozawa, Ruo-Pan Huang and Takashi Muramatsu

Department of Biochemistry, Faculty of Medicine, Kagoshisna University Kagoshirno, Kagoshkna 890

A cDNA clone isolated from a {lambda}gtll expression library of teratocarcinoma OTTBO5O specifies for a glycoprotein with a molecular weight of about 44,000. The new glycoprotein was termed heparin binding protien -44 (HIBP-44), since It was absorbed to a heparin agarose column and was eluted from it by a buffer containIng 1.5 M NaC1. HLBP-44 mRNA was intensely expressed in PYS-2 parietal endoderm cells and in the kidney, and the RNA level Increased about 10-fold during differentiation of FL) embryonal carcinoma cells to parietal endoderm cells. From the eDNA sequence, IIBP-44 was concluded to be rich in charged amino acids, and large segments of the protein appeared to form {alpha}-helixes. The protein was considered to be anchored to the membrane by a cluster of hydrophobic amino acids present in the N-terminal region. Indeed, the N-terminal sequence of HBP-44 was homologous to asialoglycoprotein receptor, which Is anchored to the membrane by the N-terminal region. Furthermore, a portion of the N-terminal region of HIBP-44 was homologous to the leucine zipper domain. Except for the N-terminal region, HBP-44 had over-all homology with structural proteins such as myosin heavy chain. We propose that BIBP-44 is extruded from plasma membranes and interacts with heparin and related molecules and that It is Involved in the interactions of plasma membranes with basement membranes.

1This work was supported by Grants-in-Aid from the Ministry of Education, Science and Culture of Japan.


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