DK2760463T3 - Regulering af natriumkanaler ved hjælp af plunc-proteiner - Google Patents
Regulering af natriumkanaler ved hjælp af plunc-proteiner Download PDFInfo
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- DK2760463T3 DK2760463T3 DK12833524.7T DK12833524T DK2760463T3 DK 2760463 T3 DK2760463 T3 DK 2760463T3 DK 12833524 T DK12833524 T DK 12833524T DK 2760463 T3 DK2760463 T3 DK 2760463T3
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
- A61P11/06—Antiasthmatics
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Pulmonology (AREA)
- Engineering & Computer Science (AREA)
- General Chemical & Material Sciences (AREA)
- Immunology (AREA)
- Cell Biology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Claims (14)
1. Polypeptid, der består af aminosyresekvensen ifølge SEQ ID NO: 14 og eventuelt i alt 1, 2, 3, 4, 5, 6, 7, 8 eller 9 yderligere aminosyrer, hvor polypeptidet binder til en natriumkanal.
2. Polypeptid ifølge krav 1, hvor polypeptidet består af aminosyresekvensen ifølge SEQ ID NO: 14.
3. Polynukleotid, der koder for polypeptidet ifølge et hvilket som helst af kravene 1-2.
4. Vektor, der omfatter polynukleotidet ifølge krav 3.
5. Celle, der omfatter polynukleotidet ifølge krav 3 eller vektoren ifølge krav 4.
6. Kit, der omfatter polypeptidet, polynukleotidet, vektoren eller cellen ifølge et hvilket som helst af kravene 1-5.
7. In v/Yro-fremgangsmåde til inhibering af aktiveringen af en natriumkanal eller inhibering af natriumabsorption gennem en natriumkanal, som omfatter etablering af kontakt mellem en natriumkanal og polypeptidet ifølge et hvilket som helst af kravene 1-2.
8. Fremgangsmåde ifølge krav 7, hvor natriumkanalen er til stede i en isoleret celle.
9. Fremgangsmåde ifølge krav 7, hvor etablering af kontakt mellem natriumkanalen og et polypeptid omfatter fremføring af polypeptidet til en celle, der omfatter natriumkanalen.
10. Fremgangsmåde ifølge krav 7, hvor etablering af kontakt mellem natriumkanalen og et polypeptid omfatter fremføring af et polynukleotid, der koder for polypeptidet, til en celle, der omfatter natriumkanalen.
11. Polypeptid ifølge et hvilket som helst af kravene 1-2 til anvendelse i en fremgangsmåde til behandling af en forstyrrelse, der viser respons på inhibering af natriumabsorption over en epitelslimhinde, hos et individ, der har brug for det, som omfatter administrering til individet af en terapeutisk effektiv mængde af polypeptidet ifølge et hvilket som helst af kravene 1-2.
12. Polypeptid til anvendelse i en fremgangsmåde ifølge krav 11, hvor forstyrrelsen er en lungeforstyrrelse, en gastrointestinal forstyrrelse eller en nyreforstyrrelse.
13. Polypeptid til anvendelse i en fremgangsmåde ifølge krav 12, hvor lungeforstyrrelsen er cystisk fibrose, kronisk obstruktiv lungesygdom, akut eller kronisk bronkitis eller astma.
14. Farmaceutisk sammensætning, der omfatter polypeptidet, polynukleotidet, vektoren eller cellen ifølge et hvilket som helst af kravene 1-6 og et bæremiddel.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201161536647P | 2011-09-20 | 2011-09-20 | |
| PCT/US2012/056112 WO2013043720A1 (en) | 2011-09-20 | 2012-09-19 | Regulation of sodium channels by plunc proteins |
Publications (1)
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| DK2760463T3 true DK2760463T3 (da) | 2019-03-18 |
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| DK12833524.7T DK2760463T3 (da) | 2011-09-20 | 2012-09-19 | Regulering af natriumkanaler ved hjælp af plunc-proteiner |
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| EP (1) | EP2760463B1 (da) |
| AU (2) | AU2012312520A1 (da) |
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| CA (1) | CA2849267A1 (da) |
| DK (1) | DK2760463T3 (da) |
| ES (1) | ES2716723T3 (da) |
| HU (1) | HUE041740T2 (da) |
| IL (1) | IL231614B (da) |
| PL (1) | PL2760463T3 (da) |
| PT (1) | PT2760463T (da) |
| WO (1) | WO2013043720A1 (da) |
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| WO2010138794A2 (en) | 2009-05-29 | 2010-12-02 | The University Of North Carolina At Chapel Hill | Regulation of sodium channels by plunc proteins |
| SG11201702769QA (en) * | 2014-10-08 | 2017-05-30 | Univ North Carolina | Improved peptide inhibitors of sodium channels |
| RU2017146661A (ru) | 2015-06-02 | 2019-07-15 | Эббви С.А.Р.Л. | Замещенные пиридины и способ их применения |
| US9840513B2 (en) | 2015-07-16 | 2017-12-12 | Abbvie S.Á.R.L. | Substituted tricyclics and method of use |
| JP2018529707A (ja) | 2015-10-09 | 2018-10-11 | アッヴィ・エス・ア・エール・エル | 嚢胞性線維症の処置のための新規な化合物 |
| TW201735769A (zh) | 2015-10-09 | 2017-10-16 | 盧森堡商艾伯維公司 | 經取代之吡唑并[3,4-b]吡啶-6-羧酸及使用方法 |
| US9890158B2 (en) | 2015-10-09 | 2018-02-13 | Abbvie S.Á.R.L. | N-sulfonylated pyrazolo[3,4-b]pyridin-6-carboxamides and method of use |
| WO2017147128A1 (en) | 2016-02-22 | 2017-08-31 | The University Of North Carolina At Chapel Hill | Peptide inhibitors of calcium channels |
| CA3016303A1 (en) | 2016-04-26 | 2017-11-02 | Abbvie S.A.R.L. | Modulators of cystic fibrosis transmembrane conductance regulator protein |
| US10138227B2 (en) | 2016-06-03 | 2018-11-27 | Abbvie S.Á.R.L. | Heteroaryl substituted pyridines and methods of use |
| US20200031866A1 (en) * | 2016-09-29 | 2020-01-30 | Spyryx Biosciences, Inc. | Peptide inhibitors of sodium channels |
| US10399940B2 (en) | 2016-10-07 | 2019-09-03 | Abbvie S.Á.R.L. | Substituted pyrrolidines and methods of use |
| US9981910B2 (en) | 2016-10-07 | 2018-05-29 | Abbvie S.Á.R.L. | Substituted pyrrolidines and methods of use |
| CA3046361A1 (en) * | 2016-12-13 | 2018-06-21 | Spyryx Biosciences, Inc. | Saline formulations of splunc1 peptides |
| WO2018116185A1 (en) | 2016-12-20 | 2018-06-28 | AbbVie S.à.r.l. | Deuterated cftr modulators and methods of use |
| CN106749679A (zh) * | 2017-01-10 | 2017-05-31 | 中国人民解放军疾病预防控制所 | 抗P选择素单链抗体靶向抑制物融合蛋白ScFv‑SPLUNC1及其表达方法与应用 |
| TW201831471A (zh) | 2017-02-24 | 2018-09-01 | 盧森堡商艾伯維公司 | 囊腫纖化症跨膜傳導調節蛋白的調節劑及其使用方法 |
| US10988454B2 (en) | 2017-09-14 | 2021-04-27 | Abbvie Overseas S.À.R.L. | Modulators of the cystic fibrosis transmembrane conductance regulator protein and methods of use |
| WO2019193062A1 (en) | 2018-04-03 | 2019-10-10 | Abbvie S.Á.R.L | Substituted pyrrolidines and their use |
| US11345691B2 (en) | 2019-06-03 | 2022-05-31 | AbbVie Global Enterprises Ltd. | Prodrug modulators of the cystic fibrosis transmembrane conductance regulator protein and methods of use |
| TW202115014A (zh) | 2019-07-12 | 2021-04-16 | 美商奧佛麥德公司 | 用於治療囊腫纖維化之化合物 |
| EP4058434A1 (en) | 2019-11-12 | 2022-09-21 | Genzyme Corporation | 6-membered heteroarylaminosulfonamides for treating diseases and conditions mediated by deficient cftr activity |
| WO2021113809A1 (en) | 2019-12-05 | 2021-06-10 | Genzyme Corporation | Arylamides and methods of use thereof |
| WO2021113806A1 (en) | 2019-12-05 | 2021-06-10 | Genzyme Corporation | Arylamides and methods of use thereof |
| US20220211692A1 (en) | 2021-01-06 | 2022-07-07 | AbbVie Global Enterprises Ltd. | Modulators of the Cystic Fibrosis Transmembrane Conductance Regulator Protein and Methods of Use |
| US20220213041A1 (en) | 2021-01-06 | 2022-07-07 | AbbVie Global Enterprises Ltd. | Modulators of the Cystic Fibrosis Transmembrane Conductance Regulator Protein and Methods of Use |
| JP2024511119A (ja) * | 2021-03-22 | 2024-03-12 | ザ・ユニヴァーシティ・オヴ・ノース・キャロライナ・アト・チャペル・ヒル | 修飾されたペプチド模倣薬および使用方法 |
| EP4396179A1 (en) | 2021-09-03 | 2024-07-10 | Genzyme Corporation | Indole compounds and methods of use |
| EP4396176A1 (en) | 2021-09-03 | 2024-07-10 | Genzyme Corporation | Indole compounds and uses thereof in the treatement of cystic fibrosis |
| WO2024054845A1 (en) | 2022-09-07 | 2024-03-14 | Sionna Therapeutics | Macrocycic compounds, compositions, and methods of using thereof |
| WO2024054851A1 (en) | 2022-09-07 | 2024-03-14 | Sionna Therapeutics | Macrocyclic compounds, compositions and methods of using thereof |
| KR20250091331A (ko) | 2022-09-07 | 2025-06-20 | 시오나 테라퓨틱스 인크. | 거대환식 화합물, 조성물, 및 이의 사용 방법 |
| WO2025132358A1 (en) | 2023-12-21 | 2025-06-26 | Galapagos Nv | Novel compounds and pharmaceutical compositions thereof for the treatment of infectious diseases |
| JP7755910B1 (ja) * | 2024-02-29 | 2025-10-17 | 一般財団法人生産技術研究奨励会 | 細胞組織の電気シグナルを計測する方法及び増感剤 |
Family Cites Families (38)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3023787A1 (de) | 1980-06-25 | 1982-01-21 | Studiengesellschaft Kohle mbH, 4330 Mülheim | Verfahren zur erhoehung der inkorporation und der expression von genetischem material in die kerne von intakten zellen mit hilfe von liposomen |
| US4554101A (en) | 1981-01-09 | 1985-11-19 | New York Blood Center, Inc. | Identification and preparation of epitopes on antigens and allergens on the basis of hydrophilicity |
| US4474893A (en) | 1981-07-01 | 1984-10-02 | The University of Texas System Cancer Center | Recombinant monoclonal antibodies |
| US5023243A (en) | 1981-10-23 | 1991-06-11 | Molecular Biosystems, Inc. | Oligonucleotide therapeutic agent and method of making same |
| US4501729A (en) | 1982-12-13 | 1985-02-26 | Research Corporation | Aerosolized amiloride treatment of retained pulmonary secretions |
| NZ207394A (en) | 1983-03-08 | 1987-03-06 | Commw Serum Lab Commission | Detecting or determining sequence of amino acids |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4957735A (en) | 1984-06-12 | 1990-09-18 | The University Of Tennessee Research Corporation | Target-sensitive immunoliposomes- preparation and characterization |
| US4676980A (en) | 1985-09-23 | 1987-06-30 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Target specific cross-linked heteroantibodies |
| US4987071A (en) | 1986-12-03 | 1991-01-22 | University Patents, Inc. | RNA ribozyme polymerases, dephosphorylases, restriction endoribonucleases and methods |
| US5080891A (en) | 1987-08-03 | 1992-01-14 | Ddi Pharmaceuticals, Inc. | Conjugates of superoxide dismutase coupled to high molecular weight polyalkylene glycols |
| US5162215A (en) | 1988-09-22 | 1992-11-10 | Amgen Inc. | Method of gene transfer into chickens and other avian species |
| GB8823869D0 (en) | 1988-10-12 | 1988-11-16 | Medical Res Council | Production of antibodies |
| US5354844A (en) | 1989-03-16 | 1994-10-11 | Boehringer Ingelheim International Gmbh | Protein-polycation conjugates |
| US5703055A (en) | 1989-03-21 | 1997-12-30 | Wisconsin Alumni Research Foundation | Generation of antibodies through lipid mediated DNA delivery |
| US5693622A (en) | 1989-03-21 | 1997-12-02 | Vical Incorporated | Expression of exogenous polynucleotide sequences cardiac muscle of a mammal |
| AU625013B2 (en) | 1989-11-03 | 1992-06-25 | Vanderbilt University | Method of in vivo delivery of functioning foreign genes |
| US5149797A (en) | 1990-02-15 | 1992-09-22 | The Worcester Foundation For Experimental Biology | Method of site-specific alteration of rna and production of encoded polypeptides |
| US5264618A (en) | 1990-04-19 | 1993-11-23 | Vical, Inc. | Cationic lipids for intracellular delivery of biologically active molecules |
| DE69127627T2 (de) | 1990-08-29 | 1998-02-19 | Genpharm Int | Produktion und Nützung nicht-menschliche transgentiere zur Produktion heterologe Antikörper |
| US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| ATE256738T1 (de) | 1992-10-30 | 2004-01-15 | Gen Hospital Corp | Ein neues zellzyklus kontrollprotein |
| FR2714830B1 (fr) | 1994-01-10 | 1996-03-22 | Rhone Poulenc Rorer Sa | Composition contenant des acides nucléiques, préparation et utilisations. |
| FR2715847B1 (fr) | 1994-02-08 | 1996-04-12 | Rhone Poulenc Rorer Sa | Composition contenant des acides nucléiques, préparation et utilisations. |
| FR2727679B1 (fr) | 1994-12-05 | 1997-01-03 | Rhone Poulenc Rorer Sa | Nouveaux agents de transfection et leurs applications pharmaceutiques |
| FR2730637B1 (fr) | 1995-02-17 | 1997-03-28 | Rhone Poulenc Rorer Sa | Composition pharmaceutique contenant des acides nucleiques, et ses utilisations |
| ES2150832B1 (es) | 1996-06-12 | 2001-06-16 | Fichtel & Sachs Ag | Dispositivo de maniobra para la maniobra, en particular maniobra neumatica, de un embrague de friccion. |
| JP2001500015A (ja) | 1996-09-06 | 2001-01-09 | トラステイーズ・オブ・ザ・ユニバーシテイ・オブ・ペンシルベニア | T7ポリメラーゼを利用する組換えアデノ随伴ウイルスの誘導可能な製造方法 |
| AU729655B2 (en) | 1996-11-12 | 2001-02-08 | Regents Of The University Of California, The | Preparation of stable formulations of lipid-nucleic acid complexes for efficient in vivo delivery |
| US7384910B2 (en) * | 1997-10-08 | 2008-06-10 | Castillo Gerardo M | Small peptides for the treatment of Alzheimer's disease and other beta-amyloid protein fibrillogenesis disorders |
| US7790867B2 (en) | 2002-12-05 | 2010-09-07 | Rosetta Genomics Inc. | Vaccinia virus-related nucleic acids and microRNA |
| WO2005056045A1 (en) * | 2003-12-04 | 2005-06-23 | The University Of Iowa Research Foundation | Methods and compositions related to plunc polypeptides |
| US20070154916A1 (en) | 2005-11-04 | 2007-07-05 | Johji Inazawa | Method for detecting cancer and a method for suppressing cancer |
| US7951781B2 (en) | 2006-11-02 | 2011-05-31 | University Of Iowa Research Foundation | Methods and compositions related to PLUNC surfactant polypeptides |
| WO2010138794A2 (en) * | 2009-05-29 | 2010-12-02 | The University Of North Carolina At Chapel Hill | Regulation of sodium channels by plunc proteins |
-
2012
- 2012-09-19 DK DK12833524.7T patent/DK2760463T3/da active
- 2012-09-19 US US14/345,975 patent/US9127040B2/en not_active Expired - Fee Related
- 2012-09-19 ES ES12833524T patent/ES2716723T3/es active Active
- 2012-09-19 EP EP12833524.7A patent/EP2760463B1/en not_active Not-in-force
- 2012-09-19 HU HUE12833524A patent/HUE041740T2/hu unknown
- 2012-09-19 CA CA2849267A patent/CA2849267A1/en not_active Abandoned
- 2012-09-19 BR BR112014006535A patent/BR112014006535A2/pt not_active Application Discontinuation
- 2012-09-19 WO PCT/US2012/056112 patent/WO2013043720A1/en not_active Ceased
- 2012-09-19 AU AU2012312520A patent/AU2012312520A1/en not_active Abandoned
- 2012-09-19 PL PL12833524T patent/PL2760463T3/pl unknown
- 2012-09-19 PT PT12833524T patent/PT2760463T/pt unknown
-
2014
- 2014-03-19 IL IL231614A patent/IL231614B/en active IP Right Grant
-
2015
- 2015-12-16 US US14/971,523 patent/US20160159879A1/en not_active Abandoned
-
2018
- 2018-02-06 AU AU2018200871A patent/AU2018200871A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| HUE041740T2 (hu) | 2019-05-28 |
| EP2760463B1 (en) | 2018-11-21 |
| AU2012312520A1 (en) | 2014-05-08 |
| IL231614B (en) | 2019-02-28 |
| CA2849267A1 (en) | 2013-03-28 |
| PL2760463T3 (pl) | 2019-05-31 |
| BR112014006535A2 (pt) | 2017-03-28 |
| US20160159879A1 (en) | 2016-06-09 |
| IL231614A0 (en) | 2014-05-28 |
| US20140228276A1 (en) | 2014-08-14 |
| EP2760463A1 (en) | 2014-08-06 |
| US9127040B2 (en) | 2015-09-08 |
| EP2760463A4 (en) | 2015-07-29 |
| ES2716723T3 (es) | 2019-06-14 |
| HK1200729A1 (en) | 2015-08-14 |
| PT2760463T (pt) | 2019-02-27 |
| AU2018200871A1 (en) | 2018-02-22 |
| WO2013043720A1 (en) | 2013-03-28 |
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