6533b86cfe1ef96bd12c8159
RESEARCH PRODUCT
Human histidine-rich glycoprotein expressed in SF9 insect cells inhibits apatite formation
Takehiko KoideThorsten SchinkeWilli Jahnen-dechentsubject
Histidine-rich glycoproteinHistidine-rich glycoproteinalpha-2-HS-GlycoproteinBiophysicsSerum proteinSf9SpodopteraFibrinogenBiochemistryα2-HS-glycoproteinBone and BonesCell Linelaw.inventionStructural BiologylawApatitesCalcium homeostasisGeneticsmedicineAnimalsHumansMolecular Biologychemistry.chemical_classificationHeparinChemistryProteinsBlood ProteinsCell BiologyFetuinBlood proteinsRecombinant ProteinsIn vitroBiochemistryProtein BiosynthesisRecombinant DNAGlycoproteinProtein Bindingmedicine.drugdescription
Histidine-rich glycoprotein (HRG) is structurally related to the alpha2-HS glycoprotein/fetuin family of mammalian plasma proteins; both belong to the cystatin superfamily of proteins. We expressed recombinant human HRG and alpha2-HS in Sf9 insect cells for functional analysis. Recombinant HRG bound heparin and fibrinogen while alpha2-HS did not. Both proteins inhibited the formation of apatite, recombinant HRG (IC50 approximately 1 microM) with 2-fold lower molar activity than alpha2-HS (IC50 approximately 0.5 microM). The inhibition in vitro of apatite formation suggests a new function for plasma HRG protein, inhibition of phase separation in blood vessels.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1997-08-04 | FEBS Letters |