WO2002061432A2 - Gpr22, recepteur couple aux proteines g (gpcr) et compositions et procedes associes a ce recepteur - Google Patents

Gpr22, recepteur couple aux proteines g (gpcr) et compositions et procedes associes a ce recepteur Download PDF

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Publication number
WO2002061432A2
WO2002061432A2 PCT/US2001/051388 US0151388W WO02061432A2 WO 2002061432 A2 WO2002061432 A2 WO 2002061432A2 US 0151388 W US0151388 W US 0151388W WO 02061432 A2 WO02061432 A2 WO 02061432A2
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WO
WIPO (PCT)
Prior art keywords
assay
gpr
patient
binding partner
sample
Prior art date
Application number
PCT/US2001/051388
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English (en)
Other versions
WO2002061432A3 (fr
Inventor
Glenna C. Burmer
Christina L. Roush
Joseph P. Brown
Madeline L. Woodward
Original Assignee
Lifespan Biosciences, Inc.
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Lifespan Biosciences, Inc. filed Critical Lifespan Biosciences, Inc.
Publication of WO2002061432A2 publication Critical patent/WO2002061432A2/fr
Publication of WO2002061432A3 publication Critical patent/WO2002061432A3/fr

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Classifications

    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/74—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving hormones or other non-cytokine intercellular protein regulatory factors such as growth factors, including receptors to hormones and growth factors
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
    • G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
    • G01N2333/705—Assays involving receptors, cell surface antigens or cell surface determinants
    • G01N2333/72—Assays involving receptors, cell surface antigens or cell surface determinants for hormones
    • G01N2333/726—G protein coupled receptor, e.g. TSHR-thyrotropin-receptor, LH/hCG receptor, FSH

Definitions

  • BIOLOGICAL ACTIVITY ASSAY SUPPLYING BIOLOGICAL ACTIVITY OR FUNCTIONALITY OF THE GPCR:
  • IMMUNOSTICK DIP-STICK
  • ASSAYS ⁇ VDVIUNOCHROMATOGRAPHIC
  • ASSAYS LMMUNOFILTRATION
  • BIOSENSOR ASSAYS BIOSENSOR ASSAYS: b. Assays Based On GPR 22 Polynucleotides
  • the activity or functionality of GPR 22 may be measured using any of a variety of functional assays in which activation of the receptor in question results in an observable change in the level of some second messenger system, including but not limited to adenylate cyclase, calcium mobilization, arachidonic acid release, ion channel activity, inositol phospholipid hydrolysis, or guanylyl cyclase.
  • adenylate cyclase calcium mobilization, arachidonic acid release, ion channel activity, inositol phospholipid hydrolysis, or guanylyl cyclase.
  • Heterologous expression systems utilizing appropriate host cells to express the nucleic acid of the subject invention are used to obtain the desired second messenger coupling. Receptor activity may also be assayed in an oocyte expression system.
  • GPR 22 biological activity may also be measured, for example, in whole cells transfected with a reporter gene whose expression is dependent upon the biological activity of GPR 22 or the biological activity of a substrate of GPR 22.
  • a reporter gene whose expression is dependent upon the biological activity of GPR 22 or the biological activity of a substrate of GPR 22.
  • polynucleotides encoding GPR 22 polypeptide and a substrate may be cotransfected into a cell. Following activation or modulation of GPR 22 activity, the substrate may then be immunoprecipitated, and its activity evaluated in an in vitro assay.
  • cells may be transfected with an ATF2-dependent promoter linked to a reporter gene such as luciferase.
  • Recognized immunoglobulin genes include the kappa, lambda, alpha, gamma, delta, epsilon, and mu constant region genes, as well as myriad immunoglobulin variable region genes.
  • Light chains are classified as either kappa or lambda.
  • Heavy chains are classified as gamma, mu, alpha, delta, or epsilon, which in turn define the immunoglobulin classes, IgG, IgM, IgA, IgD, and IgE, respectively.
  • An exemplary immunoglobulin (antibody) structural unit comprises a tetramer.
  • Animals can be immunized against the antigen, immunogenic conjugates, or derivatives by combining 1 mg or 1 ⁇ g of the peptide or conjugate (for rabbits or mice, respectively) with 3 volumes of Freund's complete adjuvant and injecting the solution intradermally at multiple sites.
  • 1 mg or 1 ⁇ g of the peptide or conjugate for rabbits or mice, respectively
  • 3 volumes of Freund's complete adjuvant for injecting the solution intradermally at multiple sites.
  • the animals are boosted with 1/5 to 1/10 the original amount of peptide or conjugate in Freund's complete adjuvant by subcutaneous injection at multiple sites.
  • Seven to 14 days later the animals are bled and the serum is assayed for antibody titer. Animals are boosted until the titer plateaus.
  • the animal is boosted with the conjugate of the same antigen, but conjugated to a different protein or through a different cross-linking reagent.
  • Conjugates also can be made in recombinant cell culture as protein fusions.
  • aggregating agents such as alum can be suitably used to enhance the immune response.
  • the clones may be subcloned by limiting dilution procedures and grown by standard methods (Goding, supra). Suitable culture media for this purpose include, for example, D-MEM or RPMI-1640 medium.
  • the hybridoma cells may be grown in vivo as ascites tumors in an animal.
  • the monoclonal antibodies secreted by the subclones are suitably separated from the culture medium, ascites fluid, or serum by conventional immunoglobulin purification procedures such as, for example, protein A-SEPHAROSETM, hydroxyapatite chromatography, gel electrophoresis, dialysis, or affinity chromatography.
  • DNA encoding the monoclonal antibodies can be readily isolated and sequenced using conventional procedures (e.g., by using oligonucleotide probes that are capable of binding specifically to genes encoding the heavy and light chains of murine antibodies).
  • the hybridoma cells serve as a preferred source of such DNA. Once isolated, the DNA may be placed into expression vectors, which can then be transfected into host cells such as E.
  • the bispecific antibodies are composed of a hybrid immunoglobulin heavy chain with a first binding specificity in one arm, and a hybrid immunoglobulin heavy chain-light chain pair (providing a second binding specificity) in the other arm.
  • This asymmetric structure may facilitate the separation of the desired bispecific compound from unwanted immunoglobulin chain combinations, as the presence of an immunoglobulin light chain in only one half of the bispecific molecule provides for a facile way of separation.
  • This approach is disclosed in WO 94/04690.
  • For further details of generating bispecific antibodies see, for example, Suresh et al., Methods in Enzymology, 121:210 (1986).
  • the GPCR agonists, antagonists, and other polypeptide-based therapeutic agents of this invention can be used therapeutically to stimulate or inhibit the activity of GPR 22, for example via the action of a specific or endogenous ligand for GPR 22, and thereby to treat medical conditions and situations caused by, mediated by, or otherwise related to the ligand, or otherwise to improve or enhance a medical condition by providing a desired biological activity.
  • the dosage regimen involved in a therapeutic application will be determined by the attending physician, considering various factors that may modify the action of the therapeutic substance, e.g., the condition, body weight, sex, and diet of the patient, the severity of any infection or other condition, including complicating conditions, time of administration, and other clinical factors.
  • Appropriate nucleic acid expression systems contain the necessary DNA sequences for expression in the patient (such as a suitable promoter and terminating signal). Such gene delivery vehicles (GDV) are also discussed elsewhere herein.
  • Viral vectors are typically non-pathogenic (defective), replication competent viruses, which require assistance in order to produce infectious vector particles.
  • This assistance can be provided, for example, by using helper cell lines that contain plasmids that encode all of the structural genes of the retrovirus under the control of regulatory sequences within the LTR, but that are missing a nucleotide sequence which enables the packaging mechanism to recognize an RNA transcript for encapsulation.
  • helper cell lines include (but are not limited to) ⁇ 2, PA317, and PA12.
  • a retroviral vector introduced into such cells can be packaged and vector virion produced.
  • the vector virions produced by this method can then be used to infect a tissue cell line, such as NTH 3T3 cells, to produce large quantities of chimeric retroviral virions .
  • EXAMPLE 6 PREPARATION OF AUTOSTAJNER SOLUTIONS [331] The purpose of this protocol was the preparation of concentrated solutions for use in a DAKO autostainer. Materials include DAKO ® TBST (Tris Buffered Saline Containing Tween-S3306), 10X Concentrate, DAKO ® Target Retrieval Solution, lOx Concentrate (SI 699), deionized H 2 O, 20L container, with lid, marked at the 10L level, DAKO ® TBS (Tris Buffered Saline-S1968), and DAKO Tween ® (SI 966).
  • DAKO ® TBST Tris Buffered Saline Containing Tween-S3306
  • 10X Concentrate DAKO ® Target Retrieval Solution
  • lOx Concentrate SI 699
  • deionized H 2 O 20L container, with lid, marked at the 10L level
  • DAKO ® TBS Tris Buffered Sa
  • Ovary A few theca cells and neutrophils were faintly positive. Macrophages were moderately positive. Focal blush staining was identified in granulosa cells, endothelium, vascular smooth muscle, and oocytes. Ovarian stroma, aside from theca cells, was largely negative.
  • Small Intestine Small intestinal glandular epithelium was negative. Interspersed neuroendocrine cells were moderately positive. Occasionally, macrophages were faintly positive. Smooth muscle showed blush to faint positive staining. Ganglion cells were negative. Endothelium was largely negative, but intravascular neutrophils were strongly positive.

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  • Life Sciences & Earth Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Molecular Biology (AREA)
  • Engineering & Computer Science (AREA)
  • Immunology (AREA)
  • Chemical & Material Sciences (AREA)
  • Biomedical Technology (AREA)
  • Urology & Nephrology (AREA)
  • Hematology (AREA)
  • Biotechnology (AREA)
  • Analytical Chemistry (AREA)
  • Cell Biology (AREA)
  • Endocrinology (AREA)
  • Food Science & Technology (AREA)
  • Medicinal Chemistry (AREA)
  • Physics & Mathematics (AREA)
  • Microbiology (AREA)
  • Biochemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • General Physics & Mathematics (AREA)
  • Pathology (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
  • Peptides Or Proteins (AREA)
  • Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
  • Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)

Abstract

L'invention se rapporte à des systèmes, des procédés, des compositions et analogues telles que des compositions de diagnostic, des médicaments et des agents thérapeutiques, associés au GPR22, lesdites compositions comportant les séquences d'acides nucléiques et de polypeptides indiquées dans la description comme associées au GPR22. La présente invention se rapporte également au diagnostic, au traitement ou à l'inhibition de carcinomes, du type mélanome malin, carcinome du colon, carcinome de la prostate, carcinome ovarien, glioblastome multiforme et maladie de Hodgkin, ainsi qu'au diagnostic, au traitement ou à l'inhibition de myocytes cardiaques lésionnés, notamment ceux associés au diabète ou à l'infarctus du myocarde, au diagnostic, au traitement ou à l'inhibition des troubles du poumon, notamment des emphysèmes, des pneumonies et de l'asthme, au diagnostic, au traitement ou à l'inhibition de la maladie de Crohn, et au diagnostic, au traitement ou à l'inhibition de la polyarthrite rhumatoïde.
PCT/US2001/051388 2001-02-01 2002-02-01 Gpr22, recepteur couple aux proteines g (gpcr) et compositions et procedes associes a ce recepteur WO2002061432A2 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US26594001P 2001-02-01 2001-02-01
US60/265,940 2001-02-01

Publications (2)

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WO2002061432A2 true WO2002061432A2 (fr) 2002-08-08
WO2002061432A3 WO2002061432A3 (fr) 2003-01-30

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AU (1) AU2002239800A1 (fr)
WO (1) WO2002061432A2 (fr)

Cited By (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2005047905A1 (fr) * 2003-10-28 2005-05-26 Bayer Healthcare Ag Diagnostic et therapie de maladies associees au recepteur 22 couple a la proteine g (gpr22)
WO2008061209A2 (fr) * 2006-11-15 2008-05-22 Omeros Corporation Récepteurs couplés à la protéine g et leurs utilisations
US7611832B2 (en) 2002-08-01 2009-11-03 Arena Pharmaceuticals, Inc. Human G protein-coupled receptor and modulators thereof for the treatment of ischemic heart disease and congestive heart failure
EP2133433A1 (fr) * 2008-06-09 2009-12-16 Centre Georges François Leclerc Procédé de prédiction de la réactivité à un traitement avec un anticorps anti-HER2
US8999654B2 (en) 2002-09-09 2015-04-07 Omeros Corporation Method of identifying a compound for the treatment or prevention of obesity

Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5994097A (en) 1997-08-28 1999-11-30 Incyte Pharmaceuticals, Inc. Polynucleotide encoding human G-protein coupled receptor

Family Cites Families (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2000052204A2 (fr) * 1999-02-22 2000-09-08 Orntoft Torben F Expression genique dans les tumeurs de la vessie
WO2001030964A2 (fr) * 1999-10-22 2001-05-03 Lifespan Biosciences, Inc. Acides nucleiques anticancereux et cibles proteiniques
JP2003531637A (ja) * 2000-05-03 2003-10-28 アストラゼネカ アクチボラグ 方 法
AU2001282894A1 (en) * 2000-07-19 2002-01-30 Deltagen, Inc. Transgenic mice containing targeted gene disruptions

Patent Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5994097A (en) 1997-08-28 1999-11-30 Incyte Pharmaceuticals, Inc. Polynucleotide encoding human G-protein coupled receptor

Cited By (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US7611832B2 (en) 2002-08-01 2009-11-03 Arena Pharmaceuticals, Inc. Human G protein-coupled receptor and modulators thereof for the treatment of ischemic heart disease and congestive heart failure
US8999654B2 (en) 2002-09-09 2015-04-07 Omeros Corporation Method of identifying a compound for the treatment or prevention of obesity
US10292374B2 (en) 2002-09-09 2019-05-21 Omeros Corporation G protein coupled receptor 85 and SREB3 knockout mice and uses thereof
WO2005047905A1 (fr) * 2003-10-28 2005-05-26 Bayer Healthcare Ag Diagnostic et therapie de maladies associees au recepteur 22 couple a la proteine g (gpr22)
WO2008061209A2 (fr) * 2006-11-15 2008-05-22 Omeros Corporation Récepteurs couplés à la protéine g et leurs utilisations
WO2008061209A3 (fr) * 2006-11-15 2009-04-30 Omeros Corp Récepteurs couplés à la protéine g et leurs utilisations
EP2133433A1 (fr) * 2008-06-09 2009-12-16 Centre Georges François Leclerc Procédé de prédiction de la réactivité à un traitement avec un anticorps anti-HER2
WO2009150127A1 (fr) * 2008-06-09 2009-12-17 Centre Georges Francois Leclerc Procédé de prévision de la sensibilité à un traitement par un anticorps anti-her2

Also Published As

Publication number Publication date
AU2002239800A1 (en) 2002-08-12
WO2002061432A3 (fr) 2003-01-30

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