Cathepsin C homolog

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving nucleic acid

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536 221, 536 231, 536 243, 536 2431, C12Q 168, C12P 1934, C07H 2102, C07H 2104

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active

056374623

ABSTRACT:
The present invention provides nucleotide and amino acid sequences that identify and encode a new cathepsin C homolog (RCP) expressed in THP-1 cells. The present invention also provides for antisense molecules to the nucleotide sequences which encode RCP, expression vectors for the production of purified RCP, antibodies capable of binding specifically to RCP, hybridization probes or oligonucleotides for the detection of RCP-encoding nucleotide sequences, genetically engineered host cells for the expression of RCP, diagnostic tests for activation of monocyte/macrophages based on RCP-encoding nucleic acid molecules, and use of the protein to produce antibodies capable of binding specifically to the protein and use of the protein to screen for inhibitors.

REFERENCES:
Ishidoh et al, "Molecular Cloning of cDNA for Rat Cathepsin C", J. Biol. Chem. 266(25):16312-16317) Sep. 1991.
Tezuka et al, "Molecular cloning of a possible cysteine proteinase predominantly expressed in osteoclasts", J. Biol. Chem. 269(2):1106-1109. Jan. 1994.
Paris et al, "Molecular cloning and sequence analysis of human preprocathepsin C", FEBS Lett. 369:326-330. 1995.
Dolenc et al, "Oligomeric structure and substrate induced inhibition of human cathepsin C", J. Biol. Chem. 270(37):21626-21631. Sep. 1995.
Tsuchiya et al., "Establishment and Characterization of a Human Acute Monocytic Leukemia Cell Line (THP-1)," Int J Cancer 26:171-176 (1980).
Auwerx, J., "The human leukemia cell line, THP-1: A multifacetted model for the study of monocyte-macrophage differentiation," Experientia 47:22-28 (1991).
Cochran et al., "Regulation of interleukin-1.beta. and tumor necrosis factor secretion by the human monocytic leukemia cell line, THP-1," Agents and Actions 27:271-273 (1989).
Kominami et al, "The Primary Structure and Tissue Distribution of Cathepsin C," Biol Chem 373:367-373 (1992).
Kuribayashi et al., "Endopeptidase Activity of Cathepsin C, Dipeptidyl Aminopeptidase I, from Bovine Spleen," J. Biochem 113:441-449 (1993).
Muno et al., "Processing and Transport of the Precursor of Cathepsin C during Its Transfer into Lysosomes," Arch Biochem Biophy 396:103-110 (1993).
Tezuka et al., "Molecular cloning of possible cysteine proteinase predominantly expressed in osteoclasts," Abstract available only, J Biol Chem 269(2):1106-1109 (1994).

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