Human histidine‐rich glycoprotein expressed in SF9 insect cells inhibits apatite formation

FEBS Letters

Schinke, Thorsten¹  Koide, Takehiko²  Jahnen-Dechent, Willi¹ 

[1] Institute for Physiological Chemistry and Pathobiochemistry, Johannes Gutenberg-University at Mainz, Duesbergweg 6, D-55099 Mainz, Germany;Himeji Institute of Technology, Hyogo 678-12, Japan

关键词: Serum protein;    Calcium homeostasis;    Histidine-rich glycoprotein;    α2-HS-glycoprotein;    HRG;    histidine-rich glycoprotein;    α2-HS;    α2-HS–glycoprotein;    SDS-PAGE;    sodium dodecyl-sulfate polyacrylamide gel electrophoresis;    DIG;    digoxigenin;    Tris;    tris-(hydroxymethyl)aminomethane;    HEPES;    N-(2-hydroxyethyl)piperazine-N′-(2-ethanesulfonic acid);   

DOI  :  10.1016/S0014-5793(97)00827-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Histidine-rich glycoprotein (HRG) is structurally related to the α₂-HS glycoprotein/fetuin family of mammalian plasma proteins; both belong to the cystatin superfamily of proteins. We expressed recombinant human HRG and α₂-HS in Sf9 insect cells for functional analysis. Recombinant HRG bound heparin and fibrinogen while α₂-HS did not. Both proteins inhibited the formation of apatite, recombinant HRG (IC₅₀ ∼1 μM) with 2-fold lower molar activity than α₂-HS (IC₅₀ ∼0.5 μM). The inhibition in vitro of apatite formation suggests a new function for plasma HRG protein, inhibition of phase separation in blood vessels.

【 授权许可】

Unknown