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  Galectin 11USPTO Application #: 20080015149Title: Galectin 11 Abstract: The present invention relates to novel galectin 11 proteins which are members of the galectin superfamily. In particular, isolated nucleic acid molecules are provided encoding the human galectin 11 proteins. Galectin 11 polypeptides are also provided as are vectors, host cells and recombinant methods for producing the same. The invention further relates to screening methods for identifying agonists and antagonists of galectin 11 activity. Also provided are diagnostic and therapeutic methods. (end of abstract)
Agent: Human Genome Sciences Inc. Intellectual Property Dept. - Rockville, MD, US Inventors: Jian Ni, Reiner L Gentz, Craig A. Rosen, Fu-Tong Lui USPTO Applicaton #: 20080015149 - Class: 514012000 (USPTO) Related Patent Categories: Drug, Bio-affecting And Body Treating Compositions, Designated Organic Active Ingredient Containing (doai), Peptide Containing (e.g., Protein, Peptones, Fibrinogen, Etc.) Doai, Cyclopeptides, 25 Or More Peptide Repeating Units In Known Peptide Chain Structure The Patent Description & Claims data below is from USPTO Patent Application 20080015149. Brief Patent Description - Full Patent Description - Patent Application Claims
CROSS-REFERENCE TO RELATED APPLICATIONS [0001] This application is a continuation of U.S. application Ser. No. 11/246,980, filed Oct. 11, 2005, which is a divisional of U.S. application Ser. No. 10/455,366, filed Jun. 6, 2003, which is a divisional of U.S. application Ser. No. 09/557,170, filed Apr. 21, 2000, which is a continuation-in-part of U.S. application Ser. No. 09/109,864 (abandoned), filed Jul. 6, 1998, which is a continuation-in-part of U.S. application Ser. No. 09/010,146 (abandoned), filed Jan. 21, 1998, which claims benefit under 35 U.S.C. .sctn. 119(e) of U.S. Provisional Application No. 60/034,205, filed Jan. 21, 1997 and of U.S. Provisional Application No. 60/034,204, filed Jan. 21, 1997; and said U.S. application Ser. No. 09/557,170 also claims benefit under 35 U.S.C. .sctn. 119(e) of U.S. Provisional Application No. 60/169,932, filed Dec. 10, 1999 and of U.S. Provisional Application No. 60/130,390, filed Apr. 21, 1999. Each of the aforementioned non-provisional and provisional applications is hereby incorporated by reference in its entirety. STATEMENT UNDER 37 C.F.R. .sctn. 1.77(b)(4) [0002] This application refers to a "Sequence Listing" listed below, which is provided as a text document. The document is entitled "PF354P2D2C1_SeqListing.txt" (26,553 bytes, created Jul. 2, 2007), and is hereby incorporated by reference in its entirety herein. FIELD OF THE INVENTION [0003] The present invention relates to a novel galectin. More specifically, isolated nucleic acid molecules are provided encoding human galectin 11. Galectin 11 polypeptides are also provided, as are vectors, host cells, recombinant methods for producing the same, and antibodies to galectin 11 polypeptides. The invention further relates to screening methods for identifying agonists and antagonists of galectin 11 activity. Also provided are diagnostic methods for detecting cell growth disorders and therapeutic methods for cell growth disorders, including autoimmune diseases, cancer, and inflammatory diseases. BACKGROUND OF THE INVENTION [0004] Lectins are proteins that bind to specific carbohydrate structures and can thus recognize particular glycoconjugates. Barondes et al., J. Biol. Chem. 269(33):20807-20810 (1994). Galectins are members of a family of .beta.-galactoside-binding lectins with related amino acid sequences (For review see, Barondes et al., Cell 76:597-598 (1994); Barondes et al., J. Biol. Chem. 269(33):20807-20810 (1994)). Although a large number of glycoproteins containing .beta.-galactoside sugars are produced by the cell, only a few will bind to known galectins in vitro. Such apparent binding specificity suggests a highly specific functional role for the galectins. [0005] Galectin 1 (conventionally termed LGALS1 for lectin, galactoside-binding, soluble-1, but which is also known as: L-14-1, L-14, RL-14.5, galaptin, MGBP, GBP, BBL, CHA, HBP, HPL, HLBP 14, rIML-1) is a homodimer with a subunit molecular mass of 14,500 Daltons. Galectin 1 is expressed abundantly in smooth and skeletal muscle, and to a lesser extent in many other cell types (Couraud et al., J. Biol. Chem. 264:1310-1316 (1989). Galectin 1 is thought to specifically bind laminin, a highly polylactosaminated cellular glycoprotein, as well as the highly polylactosaminated lysosome-associated membrane proteins (LAMPs). Galectin 1 has also been shown to bind specifically to a lactosamine-containing glycolipid found on olfactory neurons and to integrin a.sub.7b.sub.1 on skeletal muscle cells. [0006] Other members of the Galectin family have also been reported. Galectin 2 was originally found in hepatoma and is a homodimer with a subunit molecular mass of 14,650 Daltons (Gitt et al., J. Biol. Chem. 267:10601-10606 (1992)). Galectin 3 (a.k.a., Mac-2, EPB, CBP-35, CBP-30, and L-29) is abundant in activated macrophages and epithelial cells and is a monomer with an apparent molecular mass between 26,320 and 30,300 Daltons (Cherayil et al., Proc. Natl. Acad. Sci. USA 87: 7324-7326 (1990)). Galectin 3 has been observed to bind specifically to laminin, immunoglobulin E and its receptor, and bacterial lipopolysaccharides. Galectin 4 has a molecular mass of 36,300 Daltons and contains two carbohydrate-binding domains within a single polypeptide chain (Oda et al., J. Biol. Chem. 268:5929-5939 (1993)). Galectins 5 and 6 are discussed in Barondes et al., Cell 76:597-598 (1994). Human Galectin 7 has a molecular mass of 15,073 Daltons and is found mainly in stratified squamous epithelium (Madsen et al., J. Biol. Chem. 270(11):5823-5829 (1995)). [0007] Animal lectins, in general, often function in modulating cell-cell and cell-matrix interactions. Galectin 1 has been shown to either promote or inhibit cell adhesion depending upon the cell type in which it is present. Galectin 1 inhibits cell-matrix interactions in skeletal muscle presumably, by galectin 1-mediated disruption of laminin-integrin a.sub.7b.sub.1 interactions (Cooper et al., J. Cell Biol. 115:1437-1448 (1991)). In several non-skeletal muscle cell types, Galectin 1 promotes cell-matrix adhesion possibly by cross-linking cell surface and substrate glycoconjugates (Zhou et al., Arch. Bioch. Biophys. 300:6-17 (1993); Skrincosky et al., Cancer Res. 53:2667-2675 (1993)). [0008] Galectin 1 also participates in regulating cell proliferation (Wells et al., Cell 64:91-97 (1991)) and some immune functions (Offner et al., J. Neuroimmunol. 28:177-184 (1990)). Galectin 1 induces the release of tumor necrosis factor from macrophages (Kajikawa et al., Life Sci. 39:1177-1181 (1986). Galectin 1 has also been demonstrated to have therapeutic activity against autoimmune diseases in animal models for experimental myasthenia gravis, and experimental autoimmune encephalomyelitis (Levi et al., Eur. J. Immunol. 13:500-507 (1983); and Offner et al., J. Neuroimmunol. 28:177-184 (1990), respectively). Additionally, galectin 1 has been shown to regulate immune response by mediating apoptosis of T cells (Perillo et al., Nature 378:736-739 (1995)). [0009] Galectin 3 promotes the growth of cells cultured under restrictive culture conditions (Yang et al., Proc. Natl. Acad. Sci. USA 93:6737-6742 (June 1996)). Galectin 3 expression in cells confers resistance to apoptosis which indicates that galectin 3 could be a cell death suppresser which interferes in a common pathway of apoptosis. Id. Galectin 3 has also been observed to function in modulating cell-adhesion, as well as in the activation of certain immune cells by cross-linking IgE and IgE receptors. [0010] Recently, a galectin-like antigen designated HOM-HD-21 was found to be highly expressed in a Hodgkin's Disease cDNA library and another galectin, termed PCTA-1, was identified as a specific cell surface marker on human prostate cancer cell lines and patient-derived carcinomas. [0011] Thus, galectins have been observed to be involved in the regulation of immune cell activity, as well as in such diverse processes as cell adhesion, proliferation, inflammation, autoimmunity, and metastasis of tumor cells. Accordingly, there is a need in the art for the identification of novel galectins which can serve as useful tools in the development of therapeutics and diagnostics for regulating immune response, inflammatory disease and cancer. SUMMARY OF THE INVENTION [0012] The present invention provides isolated nucleic acid molecules comprising, or alternatively consisting of, a polynucleotide encoding the galectin 11 polypeptide having the amino acid sequence shown in FIG. 1 (SEQ ID NO:2), the amino acid sequence encoded by the cDNA clone deposited in a bacterial host as ATCC Deposit Number 209053, on May 16, 1997, and fragments, variants, derivatives, and analogs thereof. [0013] The present invention also provides isolated nucleic acid molecules comprising a polynucleotide encoding the galectin 11 polypeptide having the amino acid sequence shown in FIGS. 6A-B (SEQ ID NO:14), referred to herein sometimes as "Galectin-11.alpha." and fragments, variants, derivatives, and analogs thereof. [0014] The present invention also provides isolated nucleic acid molecules comprising a polynucleotide encoding the galectin 11 polypeptide having the amino acid sequence shown in FIGS. 6A-B and 8 (SEQ ID NO:16), referred to herein sometimes as "Galectin-11.beta.", and fragments, variants, derivatives, and analogs thereof. [0015] The galectin 11 of FIG. 1 (SEQ ID NOS:1 and 2), the galectin 11.alpha. of FIGS. 6A-B (SEQ ID NOS:24 and 25), and the galectin 11.beta. of FIGS. 7-8 (SEQ ID NOS:26 and 27) are often referred to herein collectively as, e.g., "galectin 11." [0016] The galectin 11 polynucleotide of FIG. 1 (SEQ ID NO:1), the galectin 11.alpha. polynucleotide of FIGS. 6A-B (SEQ ID NO:24), and the galectin 11.beta. polynucleotide of FIG. 7 (SEQ ID NO:26) are often referred to herein collectively as, e.g., "galectin 11 polynucleotides." [0017] The present invention also relates to recombinant vectors which include the isolated nucleic acid molecules of the invention, and to host cells containing the recombinant vectors, as well as to methods of making such vectors and host cells and for using them for production of galectin 11 polypeptides by recombinant techniques. [0018] The invention further provides isolated galectin 11 polypeptides, including galectin 11 of SEQ ID NO:2 and galectin 11.alpha. and .beta., having an amino acid sequence encoded by a polynucleotide described herein and antibodies which bind these polypeptides. The galectin 11 polypeptide of FIG. 1 (SEQ ID NO:2), the galectin 11.alpha. polypeptide of FIGS. 6A-B (SEQ ID NO:25), and the galectin 11.beta. polypeptide of FIG. 7 (SEQ ID NO:27) are often referred to herein collectively as, e.g., "galectin 11 polypeptides." [0019] The present invention also provides screening methods for identifying compounds capable of enhancing or inhibiting a cellular response, such as, for example, apoptosis, induced by galectin 11. Generally, these methods involve contacting galectin 11, the candidate compound, and a cell which expresses a galectin 11 ligand, assaying a cellular response resulting from the binding of galectin 11 with the ligand, and comparing the cellular response to a standard, the standard being assayed when contact of galectin 11 and the galectin 11 ligand is made in the absence of the candidate compound; whereby, an increased cellular response over the standard indicates that the compound is an agonist and a decreased cellular response over the standard indicates that the compound is an antagonist. Continue reading... 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