Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
1998-07-22
2002-03-19
Spector, Lorraine (Department: 1646)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C530S351000, C530S399000, C536S023500
Reexamination Certificate
active
06358916
ABSTRACT:
BACKGROUND OF THE INVENTION
Insulin-like growth factors (IGFs) are members of the highly diverse insulin gene family that includes insulin, IGF-I, IGF-II, relaxin, prothoraciotropic hormone (PTTH), and molluscan insulin-related peptide (Blundell, T. L. and Humbel, R. E.,
Nature
287:781-787 (1980); Ebberink, R. H. M. et al.,
Biol. Bull
177:176-182 (1989); Smit, A. B. et al.,
Nature
331:535-538 (1989)). IGFs comprise, from amino to carboxy termini, a prepeptide leader followed by a B domain, a C domain, an A domain, a D domain and a carboxy-terminal E domain. The IGFs are circulating, mitogenic peptide hormones that have an important role in stimulating growth, differentiation, metabolism and regeneration both in vitro and in vivo (Froesh, E. R., in
Insulin-like Growth
Factors/Somatomediams, de Gruyter, S. M. (ed.), New York, pp. 18-29 (1983); Lowe, M. W. Jr., in
Insulin
-
like Growth Factors:Molecular and Cellular Aspects
, LeRoith, D. (ed.), Boca Raton, Fla., CRC Press, pp. 49-80 (1991)). IGF-I and IGF-II are produced as prepropeptides; upon post-translation processing, the prepeptide leader sequence and the E domain peptide are cleaved from the prepropeptide to form the mature, bioactive molecule. In trout, four distinct forms of IGF-I mRNA exist (IGF Ea-1, Ea-2, Ea-3 and Ea-4), differing in the lengths of the E domain peptides (Shamblott, M. J. and Chen, T. T.,
Mol. Mar. Biol. Biotechnol
. 2(6):351-361 (1993)). These four mRNA forms have different temporal expression patterns (Greene, M. W. and Chen, T. T., Mol.
Mar. Biol. Biotechnol
. 6(2):144-151 (1997)).
SUMMARY OF THE INVENTION
As described herein, the E domain peptides of rainbow trout insulin-like growth factor I (rtIGF-I) have several biological activities, including mitogenic activity, cell attachment activity, and induction of morphological changes in malignant or oncogenically-transformed cells. The present invention thus pertains to use of an E domain peptide agent, such as an E domain peptide of a trout, an E domain peptide homolog, an E domain peptide fusion protein, or a nucleic acid encoding an E domain peptide, E domain peptide homolog, or E domain peptide fusion protein. In one embodiment, the invention is drawn to methods of increasing mitosis in cells, by administering to the cells at least one E domain peptide agent, particularly Ea-2 domain peptide, Ea-3 domain peptide or Ea-4 domain peptide. In another embodiment, the invention is drawn to methods of increasing cell attachment in culture (e.g., cell culture or tissue culture), by providing to the cells an E domain peptide agent, particularly Ea-2 domain peptide and/or Ea-4 domain peptide, in the cell culture medium. The invention also provides a culture medium containing one or more E domain peptide agents (e.g., to supplement or replace fetal bovine serum). In yet another embodiment, the invention is drawn to methods of enhancing wound healing, by administering to the wound one or more E domain peptide agents. In a further embodiment, the invention is drawn to methods of inhibiting proliferation of malignant cells, either in vitro or in vivo, by administering one or more E domain peptide agents to the malignant cells.
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Zheng, J.L et al., “Induction of Cell Proliferation by Fibroblast and Insulin-Like Growth Factors in Pure Rat Inner Ear Epithelial Cell Cultures,”J. Neurosci.17(1): 216-226 (Jan. 1, 1997) (XP-002060020).
Cambrey, A.D. et al., “Insulin-like growth factor I is a major fibroblast mitogen produced by primary cultures of human airway epithelial cells,”Clincal Science 89:611617 (1995).
Duguay, S.J. et al., “Mutational Analysis of the Insulin-like Growth Factor I Prohormone Processing Site,”J. of Biol. Chem. 270(29):17566-17574 (1995).
Duguay, S.J. et al., “Nucleotide Sequence and Tissue Distribution of Three Insulin-Like Growth Factor I Prohormones i Salmon,”Molecular Endocrinology, 6(8):1202-1210 (1992).
Greene, M.W. and Chen, T.T., Temporal expression pattern of insulin-like growth factor mRNA during embryonic development in a teleost, rainbow trout (Onchorynchus mykiss),Mol. Marine Biol. and Biotech. 6(2):144-151 (1997).
Hylka, V.W. and Straus, D.S., “The E-domain peptide of rat pro-insulin-like growth factor II (proIGF-II): properties of the peptide in serum and production by rat cell lines,”Biochimica et Biophysica Acta 1051:6-13 (1990).
Siegfried, J.M. et al., “A mitogenic peptide amide encoded within the E peptide domain of the insulin-like growth IB prohormone,”Proc. Natl. Acad. Sci. USA 89:8107-8111 (1992).
Shamblott M.J. and Chen, T.T., “Age-related and tissue-specific levels of five forms of insulin-like growth factor mRNA in a teleost,”Mol. Marine Biol. and Biotech. 2(6):351-361 (1993).
Wallis, A.E. and Devlin, R.H., “Duplicate Insulin-Like Growth Factor-I Genes in Salmon Display Alternative Splicing Pathways,”Mol. Endocrinology 7(3):409-422 (1993).
Chen Maria J. M.
Chen Thomas T.
Tian Xiuchun
Cummings & Lockwood
O'Hara Eileen B.
Spector Lorraine
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