Novel genes encoding proteins having prognostic, diagnostic preventive, therapeutic, and other uses

This application is a divisional application of U.S. patent application Ser. No. 11/491,318, filed Jul. 21, 2006, pending, which is a divisional application of U.S. patent application Ser. No. 09/766,511, filed Jan. 19, 2001, now U.S. Pat. No. 7,160,694.

U.S. patent application Ser. No. 09/766,511 is a continuation-in-part of U.S. patent application Ser. No. 09/578,063, filed on May 24, 2000, now U.S. Pat. No. 6,764,677, which is a continuation-in-part of U.S. patent application Ser. No. 09/333,159, filed on Jun. 14, 1999, now U.S. Pat. No. 7,033,780.

U.S. patent application Ser. No. 09/766,511 is also a continuation-in-part of U.S. patent application Ser. No. 09/596,194, filed on Jun. 16, 2000, now abandoned, which is a continuation-in-part of U.S. patent application Ser. No. 09/342,364, filed on Jun. 29, 1999, now abandoned.

U.S. patent application Ser. No. 09/766,511 is also a continuation-in-part of U.S. patent application Ser. No. 09/608,452, filed on Jun. 30, 2000, now abandoned, which is a continuation-in-part of U.S. patent application Ser. No. 09/393,996, filed on Sep. 10, 1999, now abandoned.

U.S. patent application Ser. No. 09/766,511 is also a continuation-in-part of U.S. patent application Ser. No. 09/345,680, filed on Jun. 30, 1999, now abandoned.

The contents of each of the applications cross-referenced in this section are incorporated into this disclosure by reference.

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The molecular bases underlying many human and animal physiological states (e.g., diseased and homeostatic states of various tissues) remain unknown. Nonetheless, it is well understood that these states result from interactions among the proteins and nucleic acids present in the cells of the relevant tissues. In the past, the complexity of biological systems overwhelmed the ability of practitioners to understand the molecular interactions giving rise to normal and abnormal physiological states. More recently, though, the techniques of molecular biology, transgenic and null mutant animal production, computational biology, and pharmacogenomics have enabled practitioners to discern the role and importance of individual genes and proteins in particular physiological states.

Knowledge of the sequences and other properties of genes (particularly including the portions of genes encoding proteins) and the proteins encoded thereby enables the practitioner to design and screen agents which will affect, prospectively or retrospectively, the physiological state of an animal tissue in a favorable way. Such knowledge also enables the practitioner, by detecting the levels of gene expression and protein production, to diagnose the current physiological state of a tissue or animal and to predict such physiological states in the future. This knowledge furthermore enables the practitioner to identify and design molecules which bind with the polynucleotides and proteins, in vitro, in vivo, or both.

Many secreted proteins, for example, cytokines and cytokine receptors, play a vital role in the regulation of cell growth, cell differentiation, and a variety of specific cellular responses. A number of medically useful proteins, including erythropoietin, granulocyte-macrophage colony stimulating factor, human growth hormone, and various interleukins, are secreted proteins. Thus, an important goal in the design and development of new therapies is the identification and characterization of secreted and transmembrane proteins and the genes which encode them.

Many secreted proteins are receptors which bind a ligand and transduce an intracellular signal, leading to a variety of cellular responses. The identification and characterization of such a receptor enables one to identify both the ligands which bind to the receptor and the intracellular molecules and signal transduction pathways associated with the receptor, permitting one to identify or design modulators of receptor activity, e.g., receptor agonists or antagonists and modulators of signal transduction.

The present invention is based, at least in part, on the discovery of human cDNA molecules which encode proteins which are herein designated TANGO 273, TANGO 325, TANGO 364, TANGO 405, and M019 (M019 is synonymous with TANGO 533). These proteins, fragments thereof, derivatives thereof, and variants thereof are collectively referred to herein as the polypeptides of the invention or the proteins of the invention. Nucleic acid molecules encoding polypeptides of the invention are collectively referred to as nucleic acids of the invention.

The nucleic acids and polypeptides of the present invention are useful as modulating agents for regulating a variety of cellular processes. Accordingly, in one aspect, the present invention provides isolated nucleic acid molecules encoding a polypeptide of the invention or a biologically active portion thereof. The present invention also provides nucleic acid molecules which are suitable as primers or hybridization probes for the detection of nucleic acids encoding a polypeptide of the invention.

The invention also includes fragments of any of the nucleic acids described herein wherein the fragment retains a biological or structural function by which the full-length nucleic acid is characterized (e.g., an activity, an encoded protein, or a binding capacity). The invention furthermore includes fragments of any of the nucleic acids described herein wherein the fragment has a nucleotide sequence sufficiently (e.g., 50%, 60%, 70%, 80%, 85%, 90%, 95%, 98%, or 99% or greater) identical to the nucleotide sequence of the corresponding full-length nucleic acid that it retains a biological or structural function by which the full-length nucleic acid is characterized (e.g., an activity, an encoded protein, or a binding capacity).

The invention also includes fragments of any of the polypeptides described herein wherein the fragment retains a biological or structural function by which the full-length polypeptide is characterized (e.g., an activity or a binding capacity). The invention furthermore includes fragments of any of the polypeptides described herein wherein the fragment has an amino acid sequence sufficiently (e.g., 50%, 60%, 70%, 80%, 85%, 90%, 95%, 98%, or 99% or greater) identical to the amino acid sequence of the corresponding full-length polypeptide that it retains a biological or structural function by which the full-length polypeptide is characterized (e.g., an activity or a binding capacity).