[HTML][HTML] Human histidine-rich glycoprotein expressed in SF9 insect cells inhibits apatite formation
T Schinke, T Koide, W Jahnen-Dechent - FEBS letters, 1997 - Elsevier
T Schinke, T Koide, W Jahnen-Dechent
FEBS letters, 1997•ElsevierHistidine-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 …
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 …
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.
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