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Gene Review

F10  -  coagulation factor X

Bos taurus

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Disease relevance of F10

  • Rabbit morulae and blastocysts were cultured in conventional culture media [Ham's F10 or BSM II supplemented with bovine serum albumin (BSA) or serum] or in Ham's medium supplemented with synchronous or asynchronous uterine flushings, mostly for 2 days, and afterwards investigated by light and electron microscopy and by autoradiography [1].

High impact information on F10


Biological context of F10


Anatomical context of F10

  • However, when a modified Brackett's medium was used instead of modified Ham's F10 for the initial 4-hour period after mixing gametes, more oocytes were fertilized (52% versus 28%, P less than 0.01) [11].
  • In this experiment 158 morulae were bisected and both portions were cultured for 24-44 h either in vivo after transfer to sheep oviducts (n = 80 morulae) or in vitro (n = 78 morulae) in Ham's F10 medium with 20% fetal calf serum, with bovine oviduct cells or in medium collected from oviduct cultures (conditioned medium) [12].
  • Whitten's medium supported more (P<0.05) intact and demi-embryos to grow to expanded blastocysts (92.9 and 73.1%, respectively) compared with Ham's F10 (43.8 and 26.3%, respectively) and PBS (53.8 and 12.5%, respectively) [13].
  • Compared to TALP (77.8%), more (P less than .05) embryos in Ham's F10 (95.0%) developed to the morula stage; development of mKRB embryos (88.9%) was intermediate and not different (P greater than .05) [14].
  • Interaction of bovine coagulation factor X and its glutamic-acid-containing fragments with phospholipid membranes. A surface plasmon resonance study [15].

Associations of F10 with chemical compounds


Other interactions of F10

  • Activation of prekallikrein was also observed with bovine plasmin [EC], but not with bovine clotting factors Xa (Stuart factor) [EC] and IXa (Christmas factor) or thrombin [EC] [19].
  • The lectin jacalin immobilized on agarose was found to bind a variety of glycoproteins known to contain typical O-linked oligosaccharides, including human IgA, C1 inhibitor, chorionic gonadotropin, plasminogen, bovine protein Z, bovine coagulation factor X, and fetuin [20].


  1. Ultrastructural and autoradiographic study of preimplantation rabbit embryos grown in conventional or uterine flushing-supplemented culture media. Fischer, B., Lambertz, M., Hegele-Hartung, C. In Vitro Cell. Dev. Biol. (1992) [Pubmed]
  2. Activation of coagulation releases endothelial cell mitogens. Gajdusek, C., Carbon, S., Ross, R., Nawroth, P., Stern, D. J. Cell Biol. (1986) [Pubmed]
  3. Bovine factor X1 (Stuart factor): amino-acid sequence of heavey chain. Titani, K., Fujikawa, K., Enfield, D.L., Ericsson, L.H., Walsh, K.A., Neurath, H. Proc. Natl. Acad. Sci. U.S.A. (1975) [Pubmed]
  4. How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in coagulation factor X. Selander-Sunnerhagen, M., Ullner, M., Persson, E., Teleman, O., Stenflo, J., Drakenberg, T. J. Biol. Chem. (1992) [Pubmed]
  5. Protein structural requirements for Ca2+ binding to the light chain of factor X. Studies using isolated intact fragments containing the gamma-carboxyglutamic acid region and/or the epidermal growth factor-like domains. Persson, E., Björk, I., Stenflo, J. J. Biol. Chem. (1991) [Pubmed]
  6. Tissue factor (coagulation factor III) inhibition by apolipoprotein A-II. Carson, S.D. J. Biol. Chem. (1987) [Pubmed]
  7. Five regional localizations to the sheep genome: first assignments to chromosomes 5 and 12. Pearce, P.D., Ansari, H.A., Maher, D.W., Broad, T.E. Anim. Genet. (1995) [Pubmed]
  8. Effects of serum-free culture media on in vitro development of domestic cat embryos following in vitro maturation and fertilization. Murakami, M., Otoi, T., Karja, N.W., Ooka, A., Suzuki, T. Reprod. Domest. Anim. (2002) [Pubmed]
  9. Kinetics of the activation of bovine coagulation factor X by components of the extrinsic pathway. Kinetic behavior of two-chain factor VII in the presence and absence of tissue factor. Silverberg, S.A., Nemerson, Y., Zur, M. J. Biol. Chem. (1977) [Pubmed]
  10. Binding of anticoagulation factor II from the venom of Agkistrodon acutus with activated coagulation factor X. Xu, X., Liu, Q. Toxicon (2001) [Pubmed]
  11. In vitro fertilization, culture, and transfer of rabbit ova. Seidel, G.E., Bowen, R.A., Kane, M.T. Fertil. Steril. (1976) [Pubmed]
  12. Sex-dependent loss of bisected bovine morulae after culture and freezing. King, W.A., Picard, L., Bousquet, D., Goff, A.K. J. Reprod. Fertil. (1992) [Pubmed]
  13. In vitro survival of fresh and frozen/thawed bovine demi-embryos. Lucas-Hahn, A., Niemann, H. Theriogenology (1991) [Pubmed]
  14. Culture medium and protein supplementation influence in vitro fertilization and embryo development in the domestic cat. Johnston, L.A., Donoghue, A.M., O'Brien, S.J., Wildt, D.E. J. Exp. Zool. (1991) [Pubmed]
  15. Interaction of bovine coagulation factor X and its glutamic-acid-containing fragments with phospholipid membranes. A surface plasmon resonance study. Erb, E.M., Stenflo, J., Drakenberg, T. Eur. J. Biochem. (2002) [Pubmed]
  16. Effect of nutrients, hormones and serum on survival of rat islet beta cells in culture. Ling, Z., Hannaert, J.C., Pipeleers, D. Diabetologia (1994) [Pubmed]
  17. Monolayer culture of cells originating from a preimplantation bovine embryo. Stringfellow, D.A., Gray, B.W., Lauerman, L.H., Thomson, M.S., Rhodes, P.J., Bird, R.C. In Vitro Cell. Dev. Biol. (1987) [Pubmed]
  18. The structures of the carbohydrate moieties of bovine blood coagulation factor X. Mizuochi, T., Yamashita, K., Fujikawa, K., Titani, K., Kobata, A. J. Biol. Chem. (1980) [Pubmed]
  19. Studies on prekallikrein of bovine plasma. II. Activation of prekallikrein with proteinases and properties of kallikrein activated by bovine Hageman factor. Takahashi, H., Nagasawa, S., Suzuki, T. J. Biochem. (1980) [Pubmed]
  20. Lectin affinity chromatography of proteins bearing O-linked oligosaccharides: application of jacalin-agarose. Hortin, G.L., Trimpe, B.L. Anal. Biochem. (1990) [Pubmed]
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