Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues
Reexamination Certificate
2001-11-29
2004-04-06
Carlson, Karen Cochrane (Department: 1653)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Reexamination Certificate
active
06716965
ABSTRACT:
BACKGROUND OF THE INVENTION
Cell-cell and cell-extracellular matrix interactions allow for exchange of information between, and coordination among, various cells of a multi-cellular organism and are fundamental for most biological processes. These interactions play a role in everything from fertilization to death. Such interactions are essential during development and differentiation and are critical for the function and protection of the organism. For example, interaction between the cell and its environment is necessary to initiate and mediate tissue remodeling. Tissue remodeling may be initiated, for example, in response to many factors including physical injury, cytotoxic injury, metabolic stress or developmental stimuli. Modulation between pathology and healing (or metabolic optimization) may be done, in part, by the interaction of stimulated cells with the extracellular matrix as well as the local solvent.
The adipocyte complement related protein family plays a role in the interaction of cells with their environment, and appear to act at the interface of the extracellular matrix and the cell. These proteins include, Acrp30 (Scherer et al.,
J. Biol. Chem.
270:26746-49, 1995), apM1 (Maeda et al.,
Biochem. Biophys. Res. Comm.
221:286-9, 1996), GBP28 (Nakano et al.,
J. Biochem.
120:803-12, 1996), zsig39 (Sheppard and Humes, WIPO Published Patent No: WO99/10492), zsig37 (Sheppard, WIPO Published Patent No: WO99/04000), ZCRP30R1 (Smith et al., WIPO Published Patent No. WO99/56619), ACRP30R1L (Hensley et al., WIPO Published Patent No: WO99/59618), ACRP30R2 (Hensley et al., WIPO Published Patent No: WO99/64629), PRO 353 and PRO 344 (Wood et al., WIPO Published Patent No. WO99/28462), zacrp2 (Piddington et al., WO 00/63376), zacrp3 (Piddington et al., WO 00/63377), zacrp4 (Piddington et al., WO 01/02565), zacrp5 (Piddington et al., WO 00/73444), zacrp6 (Piddington et al., WO 00/73466), zacrp11 (Piddington et al., WO 00/070704), and zacrp12 (Piddington et al., WO 00/44373).
These proteins all share a collagen-like domain comprising perfect Gly-Xaa-Pro and imperfect Gly-Xaa-Xaa collagen repeats, and a C1q domain. Complement factor C1q consists of six copies of three related polypeptides (A, B and C chains), with each polypeptide being about 225 amino acids long with a near amino-terminal collagen domain and a carboxy-terminal globular region. Six triple helical regions are formed by the collagen domains of the six A, six B and six C chains, forming a central region and six stalks. A globular head portion is formed by association of the globular carboxy terminal domain of an A, a B and a C chain. C1q is composed of six globular heads linked via six collagen-like stalks to a central fibril region. Sellar et al.,
Biochem. J.
274: 481-90, 1991. This configuration is often referred to as a bouquet of flowers. Acrp30 has a similar bouquet structure formed from a single type of polypeptide chain. The C1q globular domain of ACRP30 has been determined to have a 10 beta strand “jelly roll” topology (Shapiro and Scherer,
Curr. Biol.
8:335-8, 1998). The structural elements such as folding topologies, conserved residues and similar trimer interfaces and intron positions are homologous to the tumor necrosis factor family suggesting a link between the TNF and C1q families.
Proteins that play a role in cellular interaction, such as transcription factors and hormones are useful diagnostic and therapeutic agents. Proteins that mediate specific interactions, such a remodeling, would be particularly useful. The present invention provides such polypeptides for these and other uses that should be apparent to those skilled in the art from the teachings herein.
REFERENCES:
patent: WO 00/63376 (2000-10-01), None
patent: WO 00/63377 (2000-10-01), None
patent: WO 02/55694 (2002-07-01), None
Accession No.: Z82198. Human DNA sequence from clone RP1-302D9 on chromosome 22 Contains GSSs, complete sequence.*
Lee J, Choi SI, Jang JS, Jang K, Moon JW, Bae CS, Yang DS, Seong BL. Novel secretion system of recombinantSaccharomyces cerevisiaeusing an N-terminus residue of human IL-1 beta as secretion enhancer. Biotechnol Prog. Sep.-Oct. 1999;15(5):884-90.*
Maeda et al., “cDNA Cloning and Expression of a Novel Adipose Specific Collagen-like Factor, apM1 (Adipose Most Abundant Gene Transcript 1),”Biochem Biophys Res Commun. Apr. 16, 1996;221(2):286-9.
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, GenBank Locus TMSHP20A, Accession No. D12974, “Tamias asiaticus mRNA for HP-20, complete cds,” [online], Bethesda, MD [retrieved on Dec. 3, 2002]. Retrieved from the Internet:<http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=nucleotide&list_uids=287467&dopt=GenBank>, 2 pages.
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, GenBank Locus A48150, Accession No. A48150, “Hibernation-related protein HP-20 precursor—Siberian chipmunk,” [online], Bethesda, MD [retrieved on Dec. 3, 2002]. Retrieved from the Internet:<http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=nucleotide&list_uids=2302012&dopt=GenBank>, 2 pages.
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, GenBank Locus Q06575, Accession No. Q06575, “Hibernation-associated plasma protein HP-20 precursor (Hibernator-specific blood complex, 20 kDa subunit),” [online], Bethesda, MD [retrieved on Dec. 3, 2002]. Retrieved from the Internet:<http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=protein&list_uids=1170339&dopt=GenPept>, 2 pages.
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, GenBank Locus AK024120, Accession No. AK024120, “Homo sapiens cDNA FLJ14058 fis, clone HEMBB1000554,” [online], Bethesda, MD [retrieved on Dec. 3, 2002]. Retrieved from the Internet:<http://ww.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=nucleotide&list_uids=10436423&dopt=GenBank>, 2 pages.
Scherer et al., “A Novel Serum Protein Similar to C1q, Produced Exclusively in Adipocytes,” J Biol Chem. Nov. 10, 1995;270(45):26746-9.
Sellar et al., “ Characterization and organization of the genes encoding the A-, B- and C-chains of human complement subcomponent C1q. The complete derived amino acid sequence of human C1q,” Biochem J. Mar. 1, 1991;274 (Pt 2):481-90.
Shapiro et al., “The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor,” Curr Biol. Mar. 12, 1998;8(6):335-8.
Fox Brian A.
Holloway James L.
Carlson Karen Cochrane
Snedden Sheridan
Walsh Brian J.
ZymoGenetics Inc.
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