Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving antigen-antibody binding – specific binding protein...
Patent
1995-07-14
1998-12-01
Scheiner, Toni R.
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving antigen-antibody binding, specific binding protein...
435 721, 435 723, 4351722, 435331, 435332, 435338, 5303882, 53038826, 5303888, 53038885, A61K 39395, C12N 512, G01N 3353, G01N 33573
Patent
active
058436740
DESCRIPTION:
BRIEF SUMMARY
TECHNICAL FIELD
The present invention relates to an anti-human tyrosinase monoclonal antibody, a method for producing the same, and a method for detecting human tyrosinase by using the monoclonal antibody.
BACKGROUND ART
Tyrosinase is the most important enzyme for in vivo biosynthesis of melanin pigment. It is acknowledged that tyrosinase is produced in ribosome of rough endoplasmic reticulum, then concentrated and activated in Golgi organ-related endoplasmic reticulum, and selectively transferred to premelanosome generated by Golgi organ.
Serious dermal disorders are known to occur when biosynthesis of tyrosinase is inhibited. For example, dyschromatosis is known to occur due to mutation of a structure of tyrosinase itself or due to abnormality in its biosynthesis process, while the selective transfer of tyrosinase to premelanosome has a possibility of contribution thereto. In recent years, increase in ozone holes results in increase in amount of ultraviolet light arriving at the surface of the earth. Associating increase in dermal cancers is worried worldwide. Among them, malignant melanoma is one type of dermal cancers, in which melanocyte cancerates while maintaining its function, especially tyrosinase productivity, which is known to have extremely strong malignancy, and metastasize to lymph node at a high frequency. If in an early stage, it can be cured by surgical excision over a wide region. In such a case, however, in order to decrease the load of a patient as small as possible, it is necessary to certainly remove lesions while minimizing the excision. However, no diagnostic agent which can completely judge the lesions has been known until present.
A knowledge of behavior of tyrosinase in a living body or cells has been believed to be extremely beneficial for diagnosis or elucidation of causes of such diseases. From such a viewpoint, efforts have been hitherto made to know behavior of tyrosinase. Especially, various investigations have been made for methods to use antigen-antibody reactions because of their high sensitivity, and polyclonal antibodies against tyrosinase have been prepared since the early days (for example, Jimenez, M. et al., (1991) J. Biol. Chem., 266 (2), 1147-1156; Bouchard, B. et al., (1994) J. Invest. Dermatol., 102 (3), 291-295).
However, polyclonal antibodies have a serious drawback in that the antibody titer largely disperses depending on lots, and the reproducibility is poor because they are prepared by immunizing an animal one by one and recovering them from its blood. Thus they are not practical, and have not been commercially produced. For this reason, trials have been made, in which an animal is immunized by using tyrosinase as an antibody, and then lymphocyte of the animal is fused with cultured cells such as myeloma to prepare hybridoma which is used to produce an anti-tyrosinase monoclonal antibody (Margherita Cuo-mo et al., J. Invest. Dermatol., 96 (4), 446-451 (1991); Yasushi Tomita et al., J. Invest. Dermatol., 85 (5), 426-430 (1985)).
However, it has been revealed afterward that those regarded as the anti-tyrosinase monoclonal antibody in the foregoing reports are monoclonal antibodies against tyrosinase-related proteins (Yasushi Tomita et al., J. Invest. Dermato., 96 (4), 500-504 (1991)). This is due to the fact that the proteins called "tyrosinase-related proteins" (hereinafter referred to as "TRP") exist in a living body, as having extremely similar amino acid sequence and molecular weight to those of tyrosinase. Thus complete separation of tyrosinase from TRP is extremely difficult. Accordingly, contaminating TRP acts as an antigen, and an anti-TRP antibody is generated in the case of the conventional techniques in which an animal is immunized by using an antigen of tyrosinase purified from cells or tissues. Therefore, it is difficult to correctly detect tyrosinase by using such a monoclonal antibody.
McEwan et al. has reported an anti-human tyrosinase monoclonal antibody (McEwan, M. et al., Pigment Cell Res., 2, 1-7 (1989)). However, a molecular weight (
REFERENCES:
Jimenez, J. Biol. Chem 266:1147-1156, 1991.
Kwon, Biochem Biophys Res Comm 153:1301-1309, 1988.
Bouchard, J. Exp. Med. 169:2029-2042, 1989.
Coump J. Inv. Dermatol 96:446-451, 1991.
M. McEwan et al., "Monoclonal Antibody against Human Tyrosinase and Reactive with Melanotic and Amelanotic Melanoma Cells", pp. 515-519, Journal of Investigative Dermatology, vol. 90, No. 4 (1988).
M. McEwan et al., "Monoclonal Antibody against a Melanosomal Protein in Melanotic and Amelanotic Human Melanoma Cells", pp. 1-7, Pigment Cell Research, vol. 2, No. 1 (1989).
B. Bouchard et al., "Production and Characterization of Antibodies against Human Tyrosinase", pp. 291-295, Journal of Investigative Dermatology, vol. 102, No. 3 (1994).
Masui Shigeki
Shibata Koushi
Suzuki Satoshi
Takimoto Hiroyuki
Johnson Nancy A.
Pola Chemical Industries Inc.
Scheiner Toni R.
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