Abstract
Amino acid sequences and three dimensional structural analysis of serine proteases show sequence homology in a group of compounds, which include thrombin, Cl’ esterase, urokinase, trypsin, plasminogen, snake venom, kallikrein, and the γ subunit of mouse submandibular gland nerve growth factor. Common to the structure of these enzymes are active sites consisting of aspartic acid, histidine and serine. The similarities between the various serine proteases are striking in a number of details, including cellular location, chemical structure, molecular weight and function.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Perris, A.D., and J.F. Whitfield. 1969. The mitogenic action of bradykinin on thymic lymphocytes and its dependence on calcium. Proc Soc. Exp. Biol. Med. 130: 1198–1201.
Rixon, R.H., J.F. Whitfield, and J. Bayliss. 1971. The stimulation of mitotic activity in the thymus and bone marrow of rats by kallikrein. Horm. Metab. Res. 3: 279–284.
Schapira, M., C.F. Scott, L.A. Boxer, and R.W. Colman. 1983. Activation of human polymorphonuclear leukocytes by human plasma kallikrein. Adv. Exp. Med. Biol. 156: 747–753.
Mandel, P., J. Rodesch, and J.M. Mantz. 1973. The treatment of experimental radiation lesions by kallikrein. In: Kininogenases 1, ed. by G.L. Haberland and J.W. Rohen, pp. 171–188, Schattauer, Stuttgart, New York.
Kraut, J. 1977. Serine proteases: structure and mechanism of catalysis. Ann. Rev. Biochem. 46: 331–358.
Stroud, R.M. 1974. A family of protein-cutting proteins. Sci Am 231: 74–88.
Pisano, J.J. 1975. Chemistry and biology of the kallikrein-kinin system. In: Proteases and Biological Control, ed. Pisano, J.J, pp. 199–222, Cold Spring Harbor Laboratory.
Neurath, H., and K.A. Walsh. 1976. Role of proteolytic enzymes in biological regulation (a review). Proc. Natl. Acad. Sci. USA 73: 3825–3832.
Levi-Montalcini, R., R.H. Angeletti, and P.U. Angelietti. 1972. The nerve growth factor. In: The Structure and Function of Nervous Tissue, ed. by G.H. Bourne, pp. 1–38, Academic Press, New York, London.
Bothwell, M.A., W.H. Wilson, and E.M. Shooter. 1979. The relationship between glandular kallikrein and growth factor-processing proteases of mouse submaxillary gland. J. Biol. Chem. 254: 7287–7294.
Habener, J.F., H.T. Change, and J.T. Potts. 1977. Enzymic processing Schacter, M., B. Maranda, and C. Moriwaki. 1978. Localization of kallikrein in the coagulation and submandibular glands of the guinea-pig. J. Histochem Cytochem 26: 318–321.
Metealf, D. 1981. In: Tissue Growth Factors, ed. by R. Baserga, pp. 343–384, Springer, New York.
Nicola, N.A., D. Metealf, M. Matsumoto, and G.R. Hohnson. 1983. Purification of a factor inducing differentiation in murine myelo- monocytic leukemia cells. Identification as granulocyte colony — stimulating factors. J. Biol. Chem. 258: 9017–9021.
Stanley, E.R., and P.M. Heard. 1977. Factors regulating macrophage production and growth. Purification and some properties of colony stimulating factors from medium conditioned by mouse L Cells. J. Biol. Chem. 252: 4305–4312.
Burgess, A.W., J. Camakaris, and D. Metcalf. 1977. Purification and properties of colony stimulating factors from mouse lung- conditioned medium. J. Biol. Chem. 252: 1998–2003.
Wokota, T., F. Lee, D. Rennich, et al. 1984. Isolation and characterization of a mouse cDNA clone that expresses mast-cell growth factor activity in monkey cells. Proc. Natl. Acad. Sci. USA. 81: 1070–1074.
Fung, M.C., A.J. Hapel, S. Ymer, et al. 1984. Molecular cloning of CDNA for murine interleukin-3. Nature 307: 233–237.
Iscove, N.N., C.A. Roitsch, N. Williams, and L.J. Guilbert. 1982. Molecules stimulating early red cell, granulocyte, macrophage and megakaryocyte precursors in culture: Similarity in size, hydrophobicity, and charge. J. Cell Physiol. Suppl 1: 65–78.
Bazill, C.W., M. Haynes, J. Garland, and T.M. Dexter. 1983. Qhar- acterization and partial purification of a hematopoietic growth factor in WEHI-3 cell conditioned medium. J. Biochem. 210: 747–759.
Wong, G.G., J.S. Witek, P.A. Temple, et al. 1985. Molecular cloning of the complimentary DNA and purification of the natural and recombinant proteins. Science 228: 810–815.
Gough, N.M., J. Gough, D. Metcalf, et al. 1984. Molecular cloning of cDNA encoding a murine hematopoietic growth regulator, granulocyte-macrophage colony stimulating factor. Nature 303: 763–767.
Kawasaki, E.S., M.B. Ladner, A.M. Wang, et al. 1985. Molecular cloning of a complimentary DNA encoding human macrophage-specific colony-stimulating factor (CSF-1). Science 230: 291–296.
Iscove, N.N., J.S. Senn, J.E. Till, and E.A. McCulloch. 1971. Colony formation by normal and leukemic marrow cells in culture: Effects of conditioned medium from normal leukocytes. Blood 37: 1–5.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1988 Plenum Press, New York
About this chapter
Cite this chapter
Gross, S., Worthington-White, D.A., Smith, C.M. (1988). Serine Proteases Promote Human CFU-GM in Methylcellulose Culture Systems. In: Tavassoli, M., Zanjani, E.D., Ascensao, J.L., Abraham, N.G., Levine, A.S. (eds) Molecular Biology of Hemopoiesis. Advances in Experimental Medicine and Biology, vol 34. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5571-7_31
Download citation
DOI: https://doi.org/10.1007/978-1-4684-5571-7_31
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-5573-1
Online ISBN: 978-1-4684-5571-7
eBook Packages: Springer Book Archive