P2U2 receptor antibodies

Details P2U2 receptor antibodies P2U2 receptor antibodies

2001-09-07

2004-01-20

Spector, Lorraine (Department: 1647)

Chemistry: natural resins or derivatives; peptides or proteins;

Proteins, i.e., more than 100 amino acid residues

Blood proteins or globulins, e.g., proteoglycans, platelet...

C435S331000, C435S334000, C435S336000, C435S007100, C530S351000, C530S387100, C530S388200, C424S139100, C424S143100

Reexamination Certificate

active

06680373

ABSTRACT:

FIELD OF THE INVENTION
The present invention relates to a new subtype of the P
2
-purnergic receptors, which is abundantly expressed in kidney and in many cell lines of megakaryocytic or erythroleukemic origin. Referred to herein as the P
2U2
receptor, this receptor is activated by ATP, ADP, UTP and UDP. The P
2U2
receptor can be used as a tool to screen for agonists and antagonists that can either stimulate or block receptor activation. Such compounds have therapeutic utility in treating (1) diseases that are caused by aberrant activation of this receptor, for example over stimulation or under stimulation of the receptor and (2) diseases whose symptoms can be ameliorated by stimulating or inhibiting the activity of the P
2U2
receptor.
The present invention also relates to the isolated entire human gene encoding the P
2U2
receptor, methods for the recombinant production of purified P
2U2
receptor proteins and the proteins made by these methods, antibodies against the whole P
2U2
receptor or regions thereof, vectors, nucleotide probes, and host cells transformed by genes encoding polypeptides having the P
2U2
receptor activity, along with diagnostic and therapeutic uses for these various reagents.
BACKGROUND OF THE INVENTION
Purinergic receptors are cell surface receptors that interact with extracellular adenine or uridine nucleotides and nucleosides. These receptors are present throughout the central nervous system and peripheral tissues and play a role in numerous physiological responses.
The purinergic receptors are broadly divided into two major receptor types, P
1
and P
2
, which are defined by their level of interaction with the adenine nucleotides and nucleosides. Where P
1
receptors are activated by adenosine and exhibit a potency order of adenosine>AMP>ADP>ATP, P
2
receptors are activated by ATP, UTP, ADP or UDP and exhibit a potency order of ATP≧ADP>AMP>adenosine. As more has become known about the purinergic receptors and the wide range of physiological responses in which they play a role, the P
1
- and P
2
-type classifications were no longer sufficient to accurately portray this complex family of receptors. Therefore, receptor subtype categories have been developed. For example, the P
2
-type purinergic receptors are now classified as P
2y
-, P
2U
- , P
2T
-, P
2X
- and P
2Z
-subtypes. A review of the P
2
-type purinergic receptors can be found in Harden, et al.,
Ann. Rev. Pharmacol. Toxicol.
35:541-579 (1995).
Classification of the P
2
-type purinergic receptors has been difficult because there are no published selective P
2
-receptor antagonists and there are few ATP or ADP receptor-subtype specific agonists. In addition, it has been difficult to compare the relative order of potency of P
2
-purinergic receptor agonists. Hence, this subtype has presented numerous challenges in the identification and characterization of its members.
SUMMARY OF THE PRESENT INVENTION
One aspect of the invention is an isolated and purified polypeptide comprising the amino acid sequence of
FIG. 1
(SEQ ID NO:2).
Another aspect of the invention is an isolated and purified nucleic acid sequence encoding for the P
2U2
receptor.
Yet another aspect of the invention is an isolated and purified nucleic acid sequence comprising the nucleotide sequence of
FIG. 1
(SEQ ID NO:1).


REFERENCES:
patent: 5441883 (1995-08-01), Civelli et al.
patent: 5596088 (1997-01-01), Boucher et al.
Chang et al., “Molecular cloning and functional analysis of a novel P2 nucleotide receptor,”J Biol Chem270:26152-26158, 1995.
Conley et al., “Cloning of a Novel Purinoreceptor from a Human Megacaryocytic Cell Line,”Blood, p. 361a (Abstract 1433), 1995.
Harden et al., “P2purinergic receptors: sub-type associated signaling responses and structure,”Am Rev Pharmacol Toxicol35:541-579, 1995.
Henderson et al., “Cloning and characterization of a bovine P2Yreceptor,”Biochemical and Biophysical Research Comm212(2):648-656, 1995.
Kim et al., “Characterization of the Purinergic P. Receptors in PC12 Cells,”Journal of Biological Chemistry269(9):6471-6477, 1994.
Lustig, et al., “Expression cloning of an ATP receptor from mouse neuroblastoma cells,”Proc Natl Acad Sci USA90:5113-5117, 1993.
Mohammed et al., “Identification of two calcium-signaling P2U purinergic receptors in human erythro leukemia cells,”Experimental Biology, Part 1, p. A117 (Abstract 684), 1995.
Parr et al., “Cloning and expression of a human P2U nucleotide receptor, a target for cystic fibrosis pharmacotherapy,”Proc Natl Acad Sci USA91:3275-3279, 1994.
Rice, et al., “Cloning and Expression of the Alveolar Type II Cell P2uPurinergic Receptor,”Am J Respir Cell Mol Biol12:27-32, 1995.
Tokuyama, Y., et al., “Cloning of Rat and Mouse P2y Purinoreceptor,”Biochemical and Biophysical Research Communications211(1):211-218, 1995.
Webb, et al., “Cloning and functional expression of a brain G-protein-coupled ATP receptor,”FEBS324(2):219-225, 1993.
International Search Report in PCT Application No. PCT/US96/18175, May 20, 1997.

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