Methods for treating herpes virus infections

Details Methods for treating herpes virus infections Methods for treating herpes virus infections

1998-04-01

2001-01-16

Moezie, F. T. (Department: 1653)

Drug, bio-affecting and body treating compositions

Designated organic active ingredient containing

Heavy metal containing doai

C514S492000, C514S934000

Reexamination Certificate

active

06174916

ABSTRACT:

FIELD OF THE INVENTION
The present invention relates to methods and materials for the treatment of diseases involving plaque formation including arteriosclerotic diseases and hypertension and more specifically to materials and methods for the treatment of atherosclerosis. As a further aspect of the present invention, materials and methods are provided for the treatment of herpes virus infections including but not limited to Herpes simples types 1 and 2, Epstein-Bair virus, cytomegalovirus, Herpes zoster and further for treatment of chronic fatigue syndrome
BACKGROUND OF THE INVENTION
Cellular skeletal systems have three distinct ultrastructural features, microtubules, intermediate filaments, and microfilaments, all of which are fibrous macromolecules associated with the central nervous system (CNS). Neuronal intermediate filaments, defined as neurofilaments (containing amyloid beta protein constructs), are distinct from other intermediate filaments found in the cells of the central nervous system. R. D. Goldman, A. Milstead, J. A. Schloss and M. J. Yerna,
Annu. Rev. Physiol
., 41, p. 703-722 (1979); R. J. Lasak,
Neurosci. Res. Program Bull
., 19, p. 7-32 1981); R. J. Lasek and M. L. Shelanski,
Neurosci. Res. Program Bull
., 19, p 3-153 (1981); C. A. Maretta, ed.,
Neurofilaments
(1983); M. L. Shelanski and R. K. H. Liem,
J. Neurochem
., 33, p. 5-13 (1979). Neurofilaments are composed of three proteins with molecular weights of 200,000, 150,000 and 70,000 daltons. B. H. Toh, L. J. Gibbs, Jr., D. C. Gajdusek, J. Goudsmit and D. Dahl,
Proc. Natl. Acad. Sci
. USA. An additional 62,000 dalton protein is also affiliated with the above-mentioned proteins. Such proteins are associated with slow axoplasmic transport. P. N. Hoffman and R. J. Lasek,
J. Cell Biology
, 66, p. 351-366 (1975).
Alzheimer's Disease, and other amyloid associated maladies including senile dementia, Down's syndrome, Pick's disease, progressive supranuclear palsy, multiple sclerosis and others, are characterized by the presence of one or more fused fibrils of repetitive amyloid beta proteins or other similar amyloid residues such as paired helical filaments, neurofibrillary tangles, neuritic plaques, amyloid plaques and cerebrovascular amyloidosis. B. H. Anderson, D. Breinberg and M. J. Downes,
Nature
, 298, p. 84-86 (1982). These paired helical filaments are indistinguishable immunologically and chemically from normal neurofilaments and share many of the same proteinaceous epitopes. B. H. Anderson, D. Breinberg and M. J. Downes,
Nature
, 298, p. 84-86 (1982); B. H. Toh, L. J. Gibbs, D. C. Gajdusek, J. Goudsmit and D. Dahl,
Proc. Natl. Acad. Sci
. USA; K. Iqbal, I. Grundke-Iqbal, H. M. Wisnieski and R. D. Terry,
Brain Res
., 142, p. 321-332 (1975). It has been suggested that they interfere with axonal transport. P. N. Hoffman and R. J. Lasek,
J. Cell. Biol
., 66, p. 351-366 (1975); J. W. Griffin, P. N. Hoffman, A. W. Clark, P. T. Carroll and D. L. Price,
Science
, 202, p. 633-665 (1978).
Using a cDNA clone of the gene encoding amyloid beta protein as a genetic probe, it was shown that the gene is located on chromosome twenty-one and is expressed in many tissues of the body. D. Goldjaber, M. I. Lerman, O. W. McBridge, U. Suffiotti and D. C. Gaidusak,
Science
, 235, p. 77-780 (1987); R. E. Tanzi, J. F. Gusella, P. C. Watkins, G. A. P. Bruns, P. St.George, M. L. Vankeuren, D. Patterson, S. Pagan, D. M. Kurnit and R. L. Neve,
Science
, 235, p. 880-884 (1987). Quantitation of amyloid beta protein expression, as seen by its mRNA levels using the cDNA probe, has revealed that its level of expression in brain tissue of Alzheimer's patients was not above that seen for other tissues outside the central nervous system. Such a finding was of interest to researchers when noting that amyloid plaque formation only occurs in the brain. R. E. Tanzi, J. F. Gusella, P. C. Watldns, G. A. P. Bruns, P. St.George, M. L. Vankeuren, D. Patterson, S. Pagan, D. M. Kurnit and R. L. Neve,
Science
, 235, p. 880-884 (1987).
Amyloid beta protein is obtained through conventional means known in the art and has been characterized in various reports. A. S. Cohen and E. Calkins,
Nature
, 183, p. 1202 (1959); A. S. Cohen and E. Calkins,
J. Cell Biology
, 21, p. 481 (1964); A. S. Cohen, E. Calkins and C. Levens,
Am. J. Pathol
., 35, p. 979 (1959). More recent work is manifested by D. Caspi, M. C. Baltz and M. K. Pepys,
Mol. Biol. Med
., 3, pp. 387-407 (1986); and D. Caspi, M. C. Baltz and M. K. Pepys,
Mol. Biol. Med
., 3, pp. 409-424 (1986). Amyloid beta protein exists in various structural forms. The amyloid beta protein that has been experimentally used and as referred to herein in terms of any specific embodiments constitutes a mixture of such forms. It is to be understood that within the scope of the present invention, it is contemplated that any of the various forms of amyloid beta protein may be used.
Amyloid beta protein from the brain has been cDNA cloned and shown to contain a unique twenty amino acid NH
2
-terminal sequence. Glenner, G. G. and Wong, W.,
Biochem. Biophys. Res. Comm
., 122, No. 3, pp. 1131-35 (1984); D. Caspi, M. C. Baltz and M. K. Pepys,
Mol. Biol. Med
., 3, pp. 409-424 (1986); Goldgaber, D., Lerman, M. I., McBridge, O. W., Saffiotti, U. and Gaidusak, D. C.,
Science,
235, pp. 777-80 (1987).
It has been observed that a buildup of abnormally organized amyloid beta protein in brain tissue is manifested in Alzheimer's Disease. See Dennis J. Selkoe and Carmela R. Abraham, “Isolation of Paired Helical filaments and Amyloid Fibers from Human Brain,” 134
, Methods in Immunology
, 388-404 (1986). The fact that there is an accumulation of beta amyloid protein in the brain in Alzheimer patients has been demonstrated by post mortem analysis of brain tissue that manifest a concentration of amyloid beta protein as part of an accumulation of parallel filaments or neural fibrillatory tangles in the brain that appear characteristic of Alzheimer victims, along with neuritic plaque and cerebral vasculatory amyloidosis.
The presence of amyloid beta protein in fibrils and plaques in Alzheimer's Disease, as well as other CNS disorders, has been suggested to be a result of a degradation product of the normal neurofilaments, D. Goldjaber, M. I. Lerman, O. W. McBridge, U. Suffiotti and D. C. Gaidusak,
Science
, 235, p. 77-780 (1987); R. E. Tanzi, J. F. Gusella, P. C. Watkins, G. A. P. Bruns, P. St.George, M. L. Vankeuren, D. Patterson, S. Pagan, D. M. Kumnit and R. L. Neve,
Science
, 235, p. 880-884 (1987); M. Baudry, B. R. Dubrin, L. Beasley, M. Leon and G. Lynch,
Neurobiol. Aging
, 7, p. 255-260 (1986); G. G. Glenner,
Arch. Path. Lab. Med
., 107, p. 218-282 (1983); or possibly due to improper metabolism of byproducts. Further breakdown products of amyloid beta proteins from neurofilaments have also been observed in amyloid plaques along meningeal vascular walls and intracortical blood vessels. S. Bahmanyar, E. J. Williams, F. B. Johnson, S. Young and D. C. Gaidusak,
J. Comp. Path
, 95, p. 1-5 (1985); M. E. Bruce and H. Fraser,
Neuropathol Appl. Neurobiol
, 1, p. 189-207 (1981); M. E. Bruce and H. Fraser,
NeurophathoL Appl Neurobiol
, 7, p. 289-298 (1981); G. G. Glenner and W. Wong, J. Quaranta and G. G. Glenner,
Proc. Natl. Acad. Sci
., 82, p. 8729 (1985); D. J. Selkoe, C. R. Abraham, M. B. Podlisky and L. K. Duffy,
J. Neurochem
., 46, p. 1820 (1986).
During the mid-1960's, Solomon & Moos speculated that there was a close integration between immunological function, the central nervous system, psychophysiological factors (emotions), and disease, both physical and mental. G. F. Solomon and R. H. Moos,
Arch. Gen. Psychiatry
, 11, p. 657-674 (1964). The integration of those systems was initially suggested through observation of the presence of abnormal immunoglobulins in schizophrenic patients. G. F. Solomon and R. H. Moos,
Arch. Gen. Psychiatry
, 11, p. 657-674 (1964); J. G. Knight,
Lancet
, 82, p. 1073-1076 (1982); W. J . Fessel and M. Hirata-Hibi,
Arch. Gen. Psychiatry
, 9, p. 6

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