Human ADAMTS-1 protein and pharmaceutical composition

Drug – bio-affecting and body treating compositions – Nonspecific immunoeffector – per se ; or nonspecific...

Reexamination Certificate

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C530S350000, C530S400000

Reexamination Certificate

active

06565858

ABSTRACT:

TECHNICAL FIELD
The present invention relates to a human ADAMTS-1 protein, a gene encoding the same, a pharmaceutical composition, and a method for immunologically analyzing the human ADAMTS-1 protein.
BACKGROUND ART
A mouse ADAMTS (A disintegrin and metalloproteinase with thrombospondin motifs)-1 gene has been cloned as a cDNA from a mouse colon cancer cell which induces cancer cachexia when transplanted to a mouse. The mouse ADAMTS-1 protein encoded by the gene is a unique protein containing a matrix metalloproteinase domain, a disintegrin domain, and three thrombospondin domains [J. Biol. Chem., 272, 556-562 (1997)]. The physiological functions of the mouse ADAMTS-1 protein has not been reported, but there have been reports of each individual functional domain contained therein.
For example, a snake venom disintegrin belongs to a family of proteins which are rich in cystein, and exhibit an anticoagulant activity [Semin. Hematol., 31, 289-300 (1994)].
Further, for example, an ADAM (A disintegrin and metalloproteinase) family is known as a protein family containing a matrix metalloproteinase domain and a disintegrin domain [Nature, 377, 652-656 (1995); Nature Genet., 5, 151-157 (1993); Nature, 356, 248-252 (1992)]. Examples of known ADAM family proteins are fertilin, epidermal apical protein, cyritestin, MDC (metalloprotease-like, disintegrin-like and cystein-rich protein), meltrin, MS2, and metargidin [Nature, 377, 652-656 (1995); Nature Genet. 5, 151-157 (1993); Nature, 356, 248-252 (1992); Biochem. J., 286, 671-675 (1992); Dev. Growth. Differ., 36, 49-58 (1994); Int. Immunol., 2, 585-591 (1990); J. Biol. Chem., 271, 4593-4596 (1996)].
It was reported that fertilin is involved in an integrin-mediated sperm-egg binding [Nature, 356, 248-252 (1992)], and meltrin is involved in a myotube formation [Nature, 377, 652-656 (1995)]. MDC expressed mainly in a central nervous system is a candidate as a suppresser against a human breast cancer [Nature Genet. 5, 151-157 (1993)], and MS2 serves as a macrophage antigen [Int. Immunol., 2, 585-591 (1990)]. However, little have been known about the physiological roles of these ADAM family proteins.
The mouse ADAMTS-1 protein contains a matrix metalloproteinase domain and a disintegrin domain, and therefore belongs to the ADAM family. However, the mouse ADAMTS-1 protein is different from other known ADAM family proteins in that it further contains thrombospondin domains.
As mentioned, the ADAM family proteins have various kinds of activities such as the involvement of bone or muscle metabolism, suppression of cancer growth, or fertilization, and the thrombospondin exhibits an action to inhibit vascularization and suppresses cancer. Therefore, it is expected that the mouse ADAMTS-1 protein will exhibit unique physiological functions.
The inventors of the present invention attempted to isolate the corresponding human ADAMTS-1 protein. Accordingly, the present inventors designed and prepared various probes on the basis of the base sequence of the known mouse ADAMTS-1 gene, and carried out plaque hybridizations with a human kidney cDNA library so as to obtain a human ADAMTS-1 gene, but a desired gene was not obtained. Then, the present inventors designed and prepared various primers on the basis of the base sequence of the known mouse ADAMTS-1 gene, and carried out PCRs, using the human kidney cDNA library as templates under ordinary conditions, so as to obtain the desired gene, but did not succeed.
Thereafter, the present inventors carried out a PCR of the human kidney cDNA library, using the same primers, but under conditions milder than those ordinarily used, more particularly, an annealing temperature is set lower than an ordinary temperature, and the inventors successfully obtained a novel human ADAMTS-1 gene. The resulting gene was then, expressed in
E. coli
, and the biological activities of the recombinant human ADAMTS-1 protein were examined. Surprisingly, it was found that the novel human ADAMTS-1 protein can decrease the numbers of leukocytes and platelets, and at the same time, increase the number of erythrocytes. Such activities in influencing hematopoietic functions cannot be expected from the structure of the mouse ADAMTS-1 gene which was used as the basis in designing the primers, or from the functions of domains contained in the human ADAMTS-1 protein. The present invention is based on the above findings.
DISCLOSURE OF INVENTION
The present invention relates to a protein characterized by containing an amino acid sequence of SEQ ID NO: 1:
Met Asp Ile Cys Arg Ile Arg Leu Arg Lys Lys Arg Phe Val Ser Ser

Pro Arg Tyr Val Glu Thr Met Leu Val Ala Asp Gln Ser Met Ala Glu

Phe His Gly Ser Gly Leu Lys His Tyr Leu Leu Thr Leu Phe Ser Val

Ala Ala Arg Leu Tyr Lys His Pro Ser Ile Arg Asn Ser Val Ser Leu

Val Val Val Lys Ile Leu Val Ile His Asp Glu Gln Lys Gly Pro Glu

Val Thr Ser Asn Ala Ala Leu Thr Leu Arg Asn Phe Cys Asn Trp Gln

Lys Gln His Asn Pro Pro Ser Asp Arg Asp Ala Glu His Tyr Asp Thr

Ala Ile Leu Phe Thr Arg Gln Asp Leu Cys Gly Ser Gln Thr Cys Asp

Thr Leu Gly Met Ala Asp Val Gly Thr Val Cys Asp Pro Ser Arg Ser

Cys Ser Val Ile Glu Asp Asp Gly Leu Gln Ala Ala Phe Thr Thr Ala

His Glu Leu Gly His Val Phe Asn Met Pro His Asp Asp Ala Lys Gln

Cys Ala Ser Leu Asn Gly Val Asn Gln Asp Ser His Met Met Ala Ser

Met Leu Ser Asn Leu Asp His Ser Gln Pro Trp Ser Pro Cys Ser Ala

Tyr Met Ile Thr Ser Phe Leu Asp Asn Gly His Gly Glu Cys Leu Met

Asp Lys Pro Gln Asn Pro Ile Gln Leu Pro Gly Asp Leu Pro Gly Thr

Leu Tyr Asp Ala Asn Arg Gln Cys Gln Phe Thr Phe Gly Glu Asp Ser

Lys His Cys Pro Asp Ala Ala Ser Thr Cys Ser Thr Leu Trp Cys Thr

Gly Thr Ser Gly Gly Val Leu Val Cys Gln Thr Lys His Phe Pro Trp

Ala Asp Gly Thr Ser Cys Gly Glu Gly Lys Trp Cys Ile Asn Gly Lys

Cys Val Asn Lys Thr Asp Arg Lys His Phe Asp Thr Pro Phe His Gly

Ser Trp Gly Pro Trp Gly Pro Trp Gly Asp Cys Ser Arg Thr Cys Gly

Gly Gly Val Gln Tyr Thr Met Arg Glu Cys Asp Asn Pro Val Pro Lys

Asn Gly Gly Lys Tyr Cys Glu Gly Lys Arg Val Arg Tyr Arg Ser Cys

Asn Leu Glu Asp Cys Pro Asp Asn Asn Gly Lys Thr Phe Arg Glu Glu

Gln Cys Glu Ala His Asn Glu Phe Ser Lys Ala Ser Phe Gly Ser Gly

Pro Ala Val Glu Trp Ile Pro Lys Tyr Ala Gly Val Ser Pro Lys Asp

Arg Cys Lys Leu Ile Cys Gln Ala Lys Gly Ile Gly Tyr Phe Phe Val

Leu Gln Pro Lys Val Val Asp Gly Thr Pro Cys Ser Pro Asp Ser Thr

Ser Val Cys Val Gln Gly Gln Cys Val Lys Ala Gly Cys Asp Arg Ile

Ile Asp Ser Lys Lys Lys Phe Asp Lys Cys Gly Val Cys Gly Gly Asn

Gly Ser Thr Cys Lys Lys Ile Ser Gly Ser Val Thr Ser Ala Lys Pro

Gly Tyr His Asp Ile Val Thr Ile Pro Thr Gly Ala Thr Asn Ile Glu

Val Lys Gln Arg Asn Gln Arg Gly Ser Arg Asn Asn Gly Ser Phe Leu

Ala Ile Lys Ala Ala Asp Gly Thr Tyr Ile Leu Asn Gly Asp Tyr Thr

Leu Ser Thr Leu Glu Gln Asp Ile Met Tyr Lys Gly Val Val Leu Arg

Tyr Ser Gly Ser Ser Ala Ala Leu Glu Arg Ile Arg Ser Phe Ser Pro

Leu Lys Glu Pro Leu Thr Ile Gln Val Leu Thr Val Gly Asn Ala Leu

Arg Pro Lys Ile Lys Tyr Thr Tyr Phe Val Lys Lys Lys Lys Glu Ser

Phe Asn Ala Ile Pro Thr Phe Ser Ala Trp Val Ile Glu Glu Trp Gly

Glu Cys Ser Lys Ser Cys Glu Leu Gly Trp Gln Arg Arg Leu Val Glu

Cys Arg Asp Ile Asn Gly Gln Pro Ala Ser Glu Cys Ala Lys Glu Val

Lys Pro Ala Ser Thr Arg Pro Cys Ala Asp His Pro Cys Pro Gln Trp

Gln Leu Gly Glu Trp Ser Ser Cys Ser Lys Thr Cys Gly Lys Gly Tyr

Lys Lys Arg Ser Leu Lys Cys Leu Ser His Asp Gly Gly Val Leu Ser

His Glu Ser Cys Asp Pro Leu Lys Lys Pro Lys His Phe Ile Asp Phe

Cys Thr Leu Thr Gln Cys Ser.
Further, the present invention relates to the variation of proteins which are equivalent to the protein containing the amino acid sequence of SEQ ID NO: 1.
Further, the present invention relates to a protein characterized by containing a matrix metalloproteinase domain, a disintegrin domain, and a thrombospondin domain, except for a mouse ADAMTS-1 protein.
Further, the present invention relates to a gene characterized by encoding the above novel proteins.
Further, the presen

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