Τόμος 11 (1997) – Τεύχος 2 & 3 – Άρθρο 3 – Επιθεώρηση Κλινικής Φαρμακολογίας και Φαρμακοκινητικής-Διεθνής Έκδοση – Volume 11 (1997) – Issue 2 & 3 – Article 3 – Epitheorese Klinikes Farmakologias και Farmakokinetikes-International Edition

Title Myelin basic protein peptides: induction and inhibition of experimental allergic encephalomyelitis
Authors T. Tselios1, S. Deraos1, E. Matsoukas1, D. Panagiotopoulos1, J. Matsoukas1, G. J. Moore2, L. Probert3, G. Kollias3, B. Hilliard4, A. Rostami4 and D. Monos51. Department of Chemistry, University of Patras, 265 00 Patra, Greece2. Pharmacology and Therapeutics, University of Calgary, Alberta Canada

3. Department of Molecular Genetics, Hellenic Pasteur Institute, Athens, Greece

4. Department of Neurology, University of Pennsylvania, Medical Center, Philadelphia, PA U.S.A.

5. Department of Pathology and Laboratory Medicine, University of Pennsylvania, Medical Center, Philadelphia, PA U.S.A.

Citation Tselios, T., Deraos, S., Matsoukas, E. Panagiotopoulos, D., Matsoukas, J. et al.: Myelin basic protein peptides: induction and inhibition of experimental allergic encephalomyelitis, Epitheorese Klin. Farmakol. Farmakokinet. 11(2-3): 60-64 (1997)
Publication Date 1997
Full Text Language English
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Keywords Myelin Basic Protein (MBP), analogs, synthesis,  peptide-mimetics.
Other Terms review article
Summary Experimental Allergic Encephalomyelitis (EAE) is induced in susceptible animals by immunodominant determinants of Myelin Basic Protein (MBP). Analogs of these disease-associated peptides have been identified with disease progression upon coimmunization. Usage of peptides, with disease-specific immunomodulatory capacity in vivo is limited, however, due to their sensitivity to proteolytic enzymes. Alternative approaches include the development of mimetic molecules which maintain the biological function of an original peptide, yet are stable and able to elicit their response in pharmacological quantities. A novel technique was employed to design a series of peptides-mimetics, based on the guinea pig MBP74-85 peptide used to induce EAE in Lewis rats. One semi-mimetic peptide (SMP II) was shown to have the disease-inducing effect of the original peptide but with significantly reduced signs. Another semi-mimetic peptide, upon coimmunization with the disease inducing peptide MBP74-85, induced EAE earlier than the MBP74-85 peptide. These findings suggest that the design and synthesis of semi-mimetic peptide molecules with immunomodulatory potential is possible and that eventually these molecules may form the basis for the development of novel and more effective disease-specific therapeutic agents.
References 1.         Chou Y.K., Vandenbark A.A., Jones R., Hashim G., Offner N.: Selection of encephalitogenic rat T lymphocyte clones recognizing an immunodominant epitope on myelin basic protein. J. Neurosci. Res, 22: 181 (1989)2.        Zamvil S.S., Steinman L.: The T lymphocyte in exper-mental allergic encephalomyelitis. Ann. Rev. Immunol. 8: 579-621 (1990)3.        Wucherpiennig, K.W., Sette A., Southwood S., Oseroff C., Matsui M., Strominger J.L., Hafler D.A.: Structural requirements for binding of an immunodominant myelin basic protein peptide to DR2 isotypes and for its recognition by human T cell clones. J. Exp. Med. 179: 279-290 (1994)

4.        Moore G.J., Smith J.R., Baylis B., Matsoukas J.M.: Design and Pharmacology of Peptide Mimetics. Adv. Pharmacol. 35: 91-141 (1995)

5.        Matsoukas J.M., Hondrelis J., Keramida M., Mavromoustakos T., Makrijannis A., Hamdagni R., Wu Q., Moore G.J.: Role of the NH2 .-terminal donai of Angiotensin II and [Sari] Angiotensin II on conformation and activity: NMR evidence for aromatic ring clusing and peptide backbone folding compared to [Des 1,2,3] Angiotensin II: J. Biol. Chem. 269: 5303-5312 (1994)

6.        Matsoukas J.M., Hondrelis J., Agelis G., Barlos K., Gatos D.,  Ganter R.C., Moore D., Moore G.J.: Novel synthesis of cyclic amide-linked analogues of Angiotensin II and III. J. Med. Chem. 37: 2958-2669 (1994)

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