Recombinant carboxyl-terminal fibrin-binding domain of human fibronectin expressed in mouse L cells

This research was originally published in the Journal of Biological Chemistry. K Ichihara-Tanaka, K Titani and K Sekiguchi. Recombinant carboxyl-terminal fibrin-binding domain of human fibronectin expressed in mouse L cells. J. Biol. Chem. 1990; 265: 401-407 © the American Society for Biochemistry and Molecular Biolog

Deregulation of alternative splicing of fibronectin pre-mRNA in malignant human liver tumors

This research was originally published in the Journal of Biological Chemistry. F Oyama, S Hirohashi, Y Shimosato, K Titani and K Sekiguchi. Deregulation of alternative splicing of fibronectin pre-mRNA in malignant human liver tumors. J. Biol. Chem. 1989; 264: 10331-10334 © the American Society for Biochemistry and Molecular Biolog

Snake venom proteases a¡ecting hemostasis and thrombosis

Abstract The structure and function of snake venom proteases are briefly reviewed by putting the focus on their effects on hemostasis and thrombosis and comparing with their mammalian counterparts. Up to date, more than 150 different proteases have been isolated and about one third of them structurally characterized. Those proteases are classified into serine proteases and metalloproteinases. A number of the serine proteases show fibrin(ogen)olytic (thrombin-like) activities, which are not susceptible to hirudin or heparin and perhaps to most endogenous serine protease inhibitors, and form abnormal fibrin clots. Some of them have kininogenase (kallikrein-like) activity releasing hypotensive bradykinin. A few venom serine proteases specifically activate coagulation factor V, protein C, plasminogen or platelets. The venom metalloproteinases, belonging to the metzincin family, generally show fibrin(ogen)olytic and extracellular matrix-degrading (hemorrhagic) activities. A few venom metalloproteinases show a unique substrate specificity toward coagulation factor X, platelet membrane receptors or von Willebrand factor. A number of the metalloproteinases have chimeric structures composed of several domains such as proteinase, disintegrin-like, Cys-rich and lectin-like domains. The disintegrin-like domain seems to facilitate the action of those metalloproteinases by interacting with platelet receptors. A more detailed analysis of snake venom proteases should find their usefulness for the medical and pharmacological applications in the field of thrombosis and hemostasis.

A novel cell adhesive protein engineered by insertion of the Arg-Gly-Asp-Ser tetrapeptide

This research was originally published in the Journal of Biological Chemistry. T Maeda, R Oyama, K Ichihara-Tanaka, F Kimizuka, I Kato, K Titani and K Sekiguchi. A novel cell adhesive protein engineered by insertion of the Arg-Gly-Asp-Ser tetrapeptide. J. Biol. Chem. 1989; 264: 15165-15168 © the American Society for Biochemistry and Molecular Biolog

Structural and functional analyses of the Arg-Gly-Asp sequence introduced into human lysozyme

This research was originally published in the Journal of Biological Chemistry. T Yamada, M Matsushima, K Inaka, T Ohkubo, A Uyeda, T Maeda, K Titani, K Sekiguchi and M Kikuchi. Structural and functional analyses of the Arg-Gly-Asp sequence introduced into human lysozyme. J. Biol. Chem. 1993; 268: 10588-10592 © the American Society for Biochemistry and Molecular Biolog

Role of type III homology repeats in cell adhesive function within the cell-binding domain of fibronectin

This research was originally published in the Journal of Biological Chemistry. F Kimizuka, Y Ohdate, Y Kawase, T Shimojo, Y Taguchi, K Hashino, S Goto, H Hashi, I Kato, K Sekiguchi and K Titani. Role of type III homology repeats in cell adhesive function within the cell-binding domain of fibronectin. J. Biol. Chem. 1991; 266: 3045-3051 © the American Society for Biochemistry and Molecular Biolog

Amino acid sequence of rubredoxin from Desulfovibrio desulfuricans strain 27774

AbstractThe amino acid sequence of a rubredoxin from Desulfovibrio desulfuricans (strain 27774) has been determined. Comparison with rubredoxins from other species reveals pervasive homology, including the regions known to provide the cysteine ligands to the iron atom in several rubredoxins. Neither an extra cysteinyl residue nor a unique histidyl residue in the new sequence is located in the sequence in such a way that, by homology, a functional role in the structure is suggested