Drug – bio-affecting and body treating compositions – Dentifrices – Ferment containing
Reexamination Certificate
1999-06-24
2001-06-05
Rose, Shep K. (Department: 1614)
Drug, bio-affecting and body treating compositions
Dentifrices
Ferment containing
C424S049000
Reexamination Certificate
active
06241973
ABSTRACT:
This application is a 371 of PCT FI98/00001 filed Jan. 1, 1998
The object of the invention is a method and a product for cleaning and/or whitening of teeth based on the use of a cysteine proteinase.
PRIOR ART
Cysteine proteinases and their inhibitors
Cysteine proteinases are proteolytic enzymes which possess a cysteine residue in their active site. For the existence in an active reduced form these enzymes need an external sulfhydryl reagent. The mammalian cysteine proteinases belong to the cathepsin family and among them at least cathepsins B, H, L, S, O, U, and N have been purified and classified. The first mammalian cysteine proteinase to be characterized was cathepsin B (Suominen, J. & Hopsu-Havu, V. K.: Cathepsin B in the thyroid gland. Acta chem. Scand. 1971:25:2531). These are distributed throughout the body but they are found especially in the kidneys, liver, and macrophages (Rinne, A., Järvinen, M., Kirschke, H., Wiederanders, B., Hopsu-Havu, V. K.: demonstration of cathepsins H and L in rat tissues. Biomed Biochim Acta 1986:45:11-12:1465-1476). A part of them are active in acidic pH values but a part are active in physiological pH values, such as cathepsin s. (Kirschke, H., Wiederanders, B., Brömme, D., Rinne, A.: Cathepsin S from bovine spleen. Purification, distribution, intra cellular localization and action on proteins. Biochem J 1989:264:467-473, and Kirschke, H., Rawlings, N. D. , Barrett, A. J.: Lysosomal cysteine proteinases. Academic Press, London 1995.
In the plant kingdom, there are found cysteine proteinases such as ficin, bromelain and papain (Jävinen, M., Rinne, A.: Human spleen cysteine proteinase inhibitor. Purification, fractionation into isoelectric variants and some properties of the variants. Biochim Biophys Acta 1982: 708: 210-217).
The cysteine proteinases in the plant kingdom and those found in mammalians are closely related to each other. Papain is classically used in research work as a cysteine proteinase employed routinely in tests and as a proteinase for comparative research work concerning mammalian cysteine proteinases and their inhibitors. (the reference books, the inventor's own unpublished and published results (Ari Rinne and Mikko Järvinen 1976-1997)).
The most numerous and best known mammalian cysteine proteinases are considered to belong to the cathepsin family. However, the mammalian cysteine proteinase inhibitors are divided into several families by their structure and mode of action.
Among the mammalian cysteine proteinases are further known calcium-activated cysteine proteinases, which are considered to belong to the calpain family. Their inhibitors are called calpastatins (M. Nakamura, s. Imajoh-Ohmi, K, Suzuki and S. Kawashima: An endogenous inhibitor of calcium-activated neutral proteinase in UMX 7.1 Hamster Dystrophy. Muscle & Nerve 14: 701-708, 1991). They are also inhibited by the cathepsin inhibitor kininogen.
Cysteine proteinases have the property of dissoluting biological material, which properties can be inhibited by using inhibitors (toothpastes Rembrant ® and Yotuel®, Kirschke, H., Rawlings, N. B., Barrett, A. J.: Kysosomal cysteine proteinases, Academic Press, London 1995 and the inventor's own unpublished results.)
The following are the most important and best known so called “classical” natural (originating form the body) families of cysteine proteinase inhibitors:
1. Epdiermal-SH-proteinase inhibitor or acid cysteine proteinase inhibitor (ACPI) or stefin A. This inhibitor was simultaneously discovered in the beginning of the 1970'ies by Hayashi and Järvinen (Hayashi, H. (1975): The intra cellular neutral SH-dependent protease associated with inflammatory reactions. Int. Rev. Cytol., 40:101-151; Jävinen, M. and Hopsu-Havu, V. K. (1975): &agr;-N-Benzoly-arginine-2-naphthylamide hdyrolase (Cathepsin B1?) from rate skin. II. Purification of the enzyme and demonstration of two inhibitors in the skin. Acta Chem Scand B, 29: 772-780). It is aimed to have this inhibitor named internationally as cystatin A. (Type I) (Rinne, A: Cystatin A. Human protein data [A. Haeberli, editor, VCH Verlag, Weinheim], 3. Installment 1995; Green, G. D. J., Kembhavi. A. A. , Davies, M. L., Barrett, A. J. : Cystatin-like cysteine proteinase inhibitors from human liver. Biochem J 1984: 218: 939-946; Rinne, A.: epidermal SH-protease Inhibitor. Occurrence in human and rat tissues and in human neoplasms Thesis. Acta Univ Ouluensis, Ser D. Medica No. 41, Oulu 1979).
2. Another small-molecular cysteine proteinase inhibitor, which was electroneutral at pH-values 6.0-65., was discovered at the end of the 1970'ies (A. Rinne, M. Järvinen, J. Martikainen, M. Alavaikko und O. Räsänen: Über das Vorkommen des epidermalen SH-Protease-Inhibitors im lymphatischen Gewebe. Verh. anat. Ges. 75, S. 573-574 (1981): Järvinen, J., Rinne, A.: Human spleen cysteine proteinase inhibitor. Purification, fractionation into isoelectric variants and some properties of the variants. Biochim Biophys Acta 1982: 708: 210-217). Neutral cysteine proteinase inhibitor (NCPI) or cystatin B or stefin B. (Type I) (Rinne, A., Rinne, R., Jävinen, M.: Cystatin B. Human protein data [A. Haeberli, editor, VCH Verlag, Weinheim], 3. Installment 1995).
3. &ggr;-trace, which is called cystatin C. (Type II) (Abrahamson, M.: Human cysteine proteinase inhibitors. Isolation, physiological importance, inhibitory mechanism, gene structure and relation to hereditary cerebral hemorrhage. Scand J Clin Lab Invest 1988: 48: suppl 191: 21-31).
4. Cystatin S. (Type II) (Isemura, S., Saitoh, E., Sanada, K.: Characterization and amino acid sequence of a new acidic cysteine proteinase inhibitor (Cystatin SA) structurally closely related to cystatin S, from human whole saliva. J. Biochem 1987: 102:693-704).
5. Kininogen. (Type III). (Järvinene, M., Hopsu-Havu, V.-K.: &agr;-N-benzoylarginine-2-naphyhylamide hydrolase (cathepsin B1?) form rat skin. II. Purification of the enzyme and demonstration of tow inhibitors in the skin. Acta Chem Scand 1975: B:29:772-780).
6. “Psoriasis inhibitor”, for which we have recently proposed the name squamin. (Type ? (not classified so far) (Järvinen, M., Rinne, A., Hopsu-Havu, V. K. : Partial purification and some properties of a new papain inhibitor from psoriatic scales, J Invest Dermatil 1984:82473-476).
The type I lacks sulfur birdges. The type II has two sulfur bridges. The type III has three structures of the type II and a chain responsible for kininogen activity. Cysteine proteinase inhibitors are found particularly in cellular structures which have a role in the defense mechanism, such as in granulocytes, stratified squamous epithelia, dendrites as well as in histiocytic reticular cells and in the reserve cells in prostata. (Davies, M. E. and Barrett, A. J.. Immunolocalization of human cysteins in neutrophils and lymphocytes. Histochemistry, 80: 373-377, 1984). In addition to the natural cysteine proteinase inhibitors, also synthetic peptide cysteine proteinase inhibitors have been made. (Brömme, D., Rinne, R., Kirschke, H.: Tight-binding inhibition of cathepsin S by cystatins. Biomed Biochim Acta 1991: 150:631-635). cysteine proteinase inhibitors are also found in the skin of poikilothermic animals, such as salmon and river lamprey (for example the recently found so called troms family; the inventor's own unpublished results). Cysteine proteinase inhibitors are known to inhibit the reproduction of microbes (bacteria and viruses) and/or the associated destruction of tissues (Rinne, A.: Cystatin A. Human protein data [A. Haeberli, editor, VCH Verlag, Weinheim], 3. Installment 1995; Björck, L., Grubb, A. and Kjellen, L. (1990) Cystatin C, a human proteinase inhibitor, blocks replication of Herpes simplex virus. J Virol 64, 941-943Björck, L., Akesson, P., Bohus, M., Trojnar, J., Abrahamson, M., Olafson, I., and Grubb, A. (1989) Bacterial growth blocked by a synthetic peptide based on the structure of a human proteinase inhibitor. Nature 337, 385-386Björklund, H. V., Johansson, T. R., and Rinne, A. Rha
Lydon James C.
Rose Shep K.
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