Jianhong Geng

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The minimal region of the gamma-carboxyglutamic acid (Gla) domain of human factor (f) IX that interacted with its putative bovine aortic endothelial cell (BAEC) receptor was examined by chemical synthesis of peptides with sequence counterparts in this region of the protein, and assessment of their relative abilities to compete with fIX for receptor binding.(More)
Variant proteins containing charge-to-alanine mutations of single amino acid residues and clusters of such groups contained in the epidermal growth factor 1 (EGF1) homology unit of human protein C (PC) have been accomplished, resulting in the following recombinant (r) mutant proteins: r-[E56A/H57A]PC; r-[H66A]PC; r-[D71A]PC; r-[D79A/R81A]PC;(More)
The role of the helical stack (HS) in defining the properties of human recombinant (r) protein C (PC) and activated protein C (APC) was assessed. To do so, several mutations were made in this region of the molecule and their effects on the proteins examined. Substitution of the entire HS of PC (residues 38-46) by that of human coagulation factor (f) IX(More)
The cDNA encoding murine coagulation factor VII (mfVII) was isolated and reconstructed from a lambda Zap cDNA library generated from murine liver mRNA. The cDNA contains 1903 nucleotides spanning 15 bases upstream of the 5'-translation initiation codon, an open reading frame of 1338 nucleotides, 550 nucleotides downstream of the first stop codon and a 3'(More)
Parkinson's disease (PD) is the second most common neurodegenerative disease in the world. L166P mutant DJ-1 has been linked with a genetic form of the disease. Preventing neurotoxicity of DJ-1 familial mutations has become a new therapeutic target for PD. Adiponectin, the most abundantly secreted adipokine, has displayed its protective roles in pathologies(More)
Charge-to-alanine mutations of three amino acid residues, viz, D46, D48, and D/Hya71, which are known to be important in stabilizing Ca2+ binding to epidermal growth factor (EGF) domains of vitamin K-dependent blood coagulation proteins, have been engineered into recombinant human protein C (r-PC). The resulting variants were then employed to assess the(More)
The specificity of the propeptide sequence in directing vitamin K-dependent post-translational gamma-carboxylation has been assessed by examination of the extent of processing of chimeric constructs of blood coagulation factor VII (fVII), factor IX (fIX) and protein C (PC). One chimera consisted of a protein in which the gamma-carboxyglutamic acid(More)
A chimeric cDNA, encoding residues 1-46 (the gamma-carboxyglutamic acid module and its trailing helical stack) of human coagulant factor (f) VII, bound to residues 47-419 of human anticoagulant protein C (PC), was constructed and expressed. The resulting protein, r-[delta GD-HSPC/[symbol: see text] GD-HSfVII]PC, was properly processed with regard to(More)