Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...
Reexamination Certificate
1999-11-04
2002-08-27
Caputa, Anthony C. (Department: 1642)
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Recombinant dna technique included in method of making a...
C435S325000, C536S018700, C536S022100, C536S023100, C536S023500, C536S024300, C536S024310, C536S024330
Reexamination Certificate
active
06440697
ABSTRACT:
BACKGROUND OF THE INVENTION
Proper control of the opposing processes of cell proliferation versus terminal differentiation and apoptotic programmed cell death is an important aspect of normal development and homeostasis (Raff, M. C.,
Cell
86:173-175, 1996), and has been found to be altered in many human diseases. See, for example, Sawyers, C. L. et al.,
Cell
64:337-350, 1991; Meyaard, L. et al.,
Science
257:217-219, 1992; Guo, Q. et al.,
Nature Med.
4:957-962, 1998; Barinaga, M.,
Science,
273:735-737, 1996; Solary, E. et al.,
Eur. Respir. J.,
9:1293-1305, 1996; Hamet, P. et al.,
J. Hypertension,
14:S65-S70, 1996; Roy, N. et al.,
Cell,
80:167-178, 1995; and Ambrosini, G.,
Nature Med.,
8:917-921, 1997. Much progress has been made towards understanding the regulation of this balance. For example, signaling cascades have been elucidated through which extracellular stimuli, such as growth factors, peptide hormones, and cell-cell interactions, control the commitment of precursor cells to specific cell lineages and their subsequent proliferative expansion (Morrison, S. J. et al.,
Cell
88:287-298, 1997). Further, it has been found that cell cycle exit and terminal differentiation are coupled in most cell types. See, for example, Coppola, J. A. et al.,
Nature
320:760-763, 1986; Freytag, S. O,
Mol. Cell. Biol.
8:1614-1624, 1988; Lee, E. Y. et al.,
Genes Dev.
8:2008-2021, 1994; Morgenbesser, S. D. et al.,
Nature
371:72-74, 1994; Casaccia-Bonnefil, P. et al.,
Genes Dev.
11:2335-2346, 1996; Zacksenhaus, E. et al.,
Genes Dev.
10:3051-3064, 1996; and Zhang, P. et al.,
Nature
387:151-158, 1997. Apoptosis also plays an important role in many developmental and homeostatic processes (Raff, M. C.,
Nature
356:397-400, 1992; Raff, M. C., supra.), and is often coordinately regulated with terminal differentiation (Jacobsen, K. A. et al.,
Blood
84:2784-2794, 1994; Morgenbesser et al., supra.; Yan, Y. et al.,
Genes Dev.
11:973-983, 1997; Zacksenhaus et al., supra.). Hence, it appears that the development of individual lineages, tissues, organs, or even entire multicellular organisms is the result of a finely tuned balance between increased cell production due to proliferation, and decreased numbers of cells resulting from terminal differentiation and apoptosis. This balance is most likely regulated coordinately by the convergence of multiple regulatory pathways. The identification of novel members of such networks can provide important insights into both normal cellular processes, as well as the etiology and treatment of human disease states.
Thus, there is a continuing need to discover new proteins that regulate proliferation, differentiation, and apoptotic pathways. The in vivo activities of inducers and inhibitors of these pathways illustrates the enormous clinical potential of, and need for, novel proliferation, differentiation, and apoptotic proteins, their agonists and antagonists. The present invention addresses this need by providing such polypeptides for these and other uses that should be apparent to those skilled in the art from the teachings herein.
SUMMARY OF THE INVENTION
The present invention addresses this need by providing a novel polypeptide and related compositions and methods.
Within one aspect, the present invention provides an isolated polynucleotide that encodes a polypeptide comprising a sequence of amino acid residues that is at least 90% identical to an amino acid sequence as shown in SEQ ID NO:2 from amino acid number 1 (Met), to amino acid number 723 (Ser), wherein the amino acid percent identity is determined using a FASTA program with ktup=1, gap opening penalty=10, gap extension penalty=1, and substitution matrix=BLOSUM62, with other parameters set as default. Within one embodiment the isolated polynucleotide disclosed above, wherein the polynucleotide is selected from the group consisting of: (a) polynucleotide molecules comprising a nucleotide sequence as shown in SEQ ID NO:1 from nucleotide 367 to nucleotide 2535; and (b) polynucleotide molecules complementary to (a). Within another embodiment the isolated polynucleotide disclosed above comprises nucleotide 1 to nucleotide 2169 of SEQ ID NO:3. Within another embodiment the isolated polynucleotide disclosed above comprises a sequence of amino acid residues having an amino acid sequence as shown in SEQ ID NO:2 from amino acid number 1 (Met), to amino acid number 723 (Ser). Within another embodiment the isolated polynucleotide disclosed above consists of an amino acid sequence as shown in SEQ ID NO:2 from amino acid number 1 (Met), to amino acid number 723 (Ser). Within another embodiment the isolated polynucleotide disclosed above further encodes a polypeptide that contains a RING finger domain or at least one LRR motif. Within another embodiment the isolated polynucleotide disclosed above further encodes a polypeptide that contains a RING finger domain and at least one LRR motif.
Within a second aspect, the present invention provides an expression vector comprising the following operably linked elements: a transcription promoter; a DNA segment encoding a zapop3 polypeptide having an amino acid sequence as shown in SEQ ID NO:2 from amino acid number 1 (Met), to amino acid number 723 (Ser); and a transcription terminator, wherein the promoter is operably linked to the DNA segment, and the DNA segment is operably linked to the transcription terminator. Within one embodiment the expression vector disclosed above further comprises a secretory signal sequence operably linked to the DNA segment.
Within a third aspect, the present invention provides a cultured cell into which has been introduced an expression vector as disclosed above, wherein the cell expresses the polypeptide encoded by the DNA segment.
Within a fourth aspect, the present invention provides an isolated polypeptide comprising a sequence of amino acid residues that is at least 90% identical to an amino acid sequence selected from the group consisting of: (a) polypeptide molecules comprising an amino acid sequence as shown in SEQ ID NO:2 from amino acid number 1 (Met), to amino acid number 723 (Ser), wherein the amino acid percent identity is determined using a FASTA program with ktup=1, gap opening penalty=10, gap extension penalty=1, and substitution matrix=BLOSUM62, with other parameters set as default. Within one embodiment, the isolated polypeptide disclosed above comprises a sequence of amino acid residues having an amino acid sequence as shown in SEQ ID NO:2 from amino acid number 1 (Met), to amino acid number 723 (Ser). Within another embodiment, the isolated polypeptide disclosed above consists of amino acid number 1 (Met), to amino acid number 723 (Ser) of SEQ ID NO:2. Within another embodiment, the isolated polypeptide disclosed above further contains a RING finger domain or at least one LRR motif; Within another embodiment, the isolated polypeptide disclosed above further contains a RING finger domain and at least one LRR motif. Within another aspect, the present invention provides a method of producing a zapop3 polypeptide comprising: culturing a cell as disclosed above; and isolating the zapop3 polypeptide produced by the cell.
Within another aspect, the present invention provides a method of producing an antibody to zapop3 polypeptide comprising: inoculating an animal with a polypeptide selected from the group consisting of: (a) a polypeptide consisting of 9 to 723 amino acids, wherein the polypeptide consists of a contiguous sequence of amino acids in SEQ ID NO:2 from amino acid number 1 (Met), to amino acid number 723 (Ser); (b) a polypeptide as disclosed above; (c) a polypeptide consisting of the amino acid sequence of SEQ ID NO:2 from amino acid residue 1 (Met) to amino acid residue 223 (Leu); (d) a polypeptide consisting of the amino acid sequence of SEQ ID NO:2 from amino acid residue 224 (Glu) to amino acid residue 348 (Arg); (e) a polypeptide consisting of the amino acid sequence of SEQ ID NO:2 from amino acid residues 520 (Lys) to amino acid r
Grossmann Angelika
Venezia Domenick
Caputa Anthony C.
Harris Alana M.
Johnson Jennifer K.
ZymoGenetics Inc.
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