IE913426A1 - Hybrid growth factors - Google Patents
Hybrid growth factorsInfo
- Publication number
- IE913426A1 IE913426A1 IE342691A IE342691A IE913426A1 IE 913426 A1 IE913426 A1 IE 913426A1 IE 342691 A IE342691 A IE 342691A IE 342691 A IE342691 A IE 342691A IE 913426 A1 IE913426 A1 IE 913426A1
- Authority
- IE
- Ireland
- Prior art keywords
- amino acid
- molecule
- recombinant
- hematopoietic molecule
- hematopoietic
- Prior art date
Links
- 239000003102 growth factor Substances 0.000 title description 4
- 230000003394 haemopoietic effect Effects 0.000 claims abstract description 85
- 230000004069 differentiation Effects 0.000 claims abstract description 22
- 230000000694 effects Effects 0.000 claims abstract description 21
- 239000008194 pharmaceutical composition Substances 0.000 claims abstract description 10
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 9
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 9
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 9
- 108010002386 Interleukin-3 Proteins 0.000 claims description 59
- 102000000646 Interleukin-3 Human genes 0.000 claims description 56
- 210000004027 cell Anatomy 0.000 claims description 48
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 32
- 150000001413 amino acids Chemical class 0.000 claims description 30
- 108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 claims description 19
- 102000004269 Granulocyte Colony-Stimulating Factor Human genes 0.000 claims description 18
- 102000004457 Granulocyte-Macrophage Colony-Stimulating Factor Human genes 0.000 claims description 8
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 claims description 8
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims description 8
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 claims description 7
- 238000000034 method Methods 0.000 claims description 6
- 101001033279 Homo sapiens Interleukin-3 Proteins 0.000 claims description 5
- 102000007651 Macrophage Colony-Stimulating Factor Human genes 0.000 claims description 5
- 108010046938 Macrophage Colony-Stimulating Factor Proteins 0.000 claims description 5
- 102000055276 human IL3 Human genes 0.000 claims description 5
- 239000013598 vector Substances 0.000 claims description 5
- 230000011132 hemopoiesis Effects 0.000 claims description 4
- 238000004519 manufacturing process Methods 0.000 claims description 4
- 101000746367 Homo sapiens Granulocyte colony-stimulating factor Proteins 0.000 claims description 3
- 239000003937 drug carrier Substances 0.000 claims description 3
- 239000013604 expression vector Substances 0.000 claims description 3
- 210000004962 mammalian cell Anatomy 0.000 claims description 3
- 108010002616 Interleukin-5 Proteins 0.000 claims description 2
- 102000000743 Interleukin-5 Human genes 0.000 claims description 2
- 125000000539 amino acid group Chemical group 0.000 claims description 2
- 230000001737 promoting effect Effects 0.000 claims description 2
- 238000012258 culturing Methods 0.000 claims 1
- 101150002621 EPO gene Proteins 0.000 description 55
- 229940076264 interleukin-3 Drugs 0.000 description 53
- 108090000623 proteins and genes Proteins 0.000 description 31
- 108091034117 Oligonucleotide Proteins 0.000 description 19
- 239000013612 plasmid Substances 0.000 description 18
- 239000012634 fragment Substances 0.000 description 13
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 12
- 108020004705 Codon Proteins 0.000 description 9
- 102000004169 proteins and genes Human genes 0.000 description 9
- 102000001554 Hemoglobins Human genes 0.000 description 8
- 108010054147 Hemoglobins Proteins 0.000 description 8
- 102000005962 receptors Human genes 0.000 description 7
- 108020003175 receptors Proteins 0.000 description 7
- 108091028043 Nucleic acid sequence Proteins 0.000 description 6
- 238000002474 experimental method Methods 0.000 description 6
- SXTAYKAGBXMACB-UHFFFAOYSA-N methionine S-imide-S-oxide Natural products CS(=N)(=O)CCC(N)C(O)=O SXTAYKAGBXMACB-UHFFFAOYSA-N 0.000 description 6
- 108020004414 DNA Proteins 0.000 description 5
- 241001529936 Murinae Species 0.000 description 5
- 108010076504 Protein Sorting Signals Proteins 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- 238000003776 cleavage reaction Methods 0.000 description 5
- 239000003636 conditioned culture medium Substances 0.000 description 5
- 230000012010 growth Effects 0.000 description 5
- 230000007017 scission Effects 0.000 description 5
- 238000001890 transfection Methods 0.000 description 5
- 238000003556 assay Methods 0.000 description 4
- 230000035800 maturation Effects 0.000 description 4
- 108091008146 restriction endonucleases Proteins 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- 241000283707 Capra Species 0.000 description 3
- 102000053602 DNA Human genes 0.000 description 3
- 108020004682 Single-Stranded DNA Proteins 0.000 description 3
- 210000004369 blood Anatomy 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 108020002326 glutamine synthetase Proteins 0.000 description 3
- 230000001404 mediated effect Effects 0.000 description 3
- 102000003951 Erythropoietin Human genes 0.000 description 2
- 108090000394 Erythropoietin Proteins 0.000 description 2
- 101000987586 Homo sapiens Eosinophil peroxidase Proteins 0.000 description 2
- 101000920686 Homo sapiens Erythropoietin Proteins 0.000 description 2
- HMNZFMSWFCAGGW-XPWSMXQVSA-N [3-[hydroxy(2-hydroxyethoxy)phosphoryl]oxy-2-[(e)-octadec-9-enoyl]oxypropyl] (e)-octadec-9-enoate Chemical compound CCCCCCCC\C=C\CCCCCCCC(=O)OCC(COP(O)(=O)OCCO)OC(=O)CCCCCCC\C=C\CCCCCCCC HMNZFMSWFCAGGW-XPWSMXQVSA-N 0.000 description 2
- 230000004075 alteration Effects 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 210000001185 bone marrow Anatomy 0.000 description 2
- AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 2
- 230000010261 cell growth Effects 0.000 description 2
- 238000010367 cloning Methods 0.000 description 2
- 230000005757 colony formation Effects 0.000 description 2
- 230000001332 colony forming effect Effects 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 210000003743 erythrocyte Anatomy 0.000 description 2
- 230000000925 erythroid effect Effects 0.000 description 2
- 229940105423 erythropoietin Drugs 0.000 description 2
- 102000018146 globin Human genes 0.000 description 2
- 108060003196 globin Proteins 0.000 description 2
- 102000005396 glutamine synthetase Human genes 0.000 description 2
- 102000044890 human EPO Human genes 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 210000000066 myeloid cell Anatomy 0.000 description 2
- 230000037361 pathway Effects 0.000 description 2
- OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- HKZAAJSTFUZYTO-LURJTMIESA-N (2s)-2-[[2-[[2-[[2-[(2-aminoacetyl)amino]acetyl]amino]acetyl]amino]acetyl]amino]-3-hydroxypropanoic acid Chemical compound NCC(=O)NCC(=O)NCC(=O)NCC(=O)N[C@@H](CO)C(O)=O HKZAAJSTFUZYTO-LURJTMIESA-N 0.000 description 1
- 208000030507 AIDS Diseases 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 208000031637 Erythroblastic Acute Leukemia Diseases 0.000 description 1
- 208000036566 Erythroleukaemia Diseases 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 241000701024 Human betaherpesvirus 5 Species 0.000 description 1
- 102000010790 Interleukin-3 Receptors Human genes 0.000 description 1
- 108010038452 Interleukin-3 Receptors Proteins 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 208000001647 Renal Insufficiency Diseases 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 208000021841 acute erythroid leukemia Diseases 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 229960002749 aminolevulinic acid Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- 208000007502 anemia Diseases 0.000 description 1
- 238000000211 autoradiogram Methods 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 210000003651 basophil Anatomy 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 238000000423 cell based assay Methods 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000036755 cellular response Effects 0.000 description 1
- 238000002512 chemotherapy Methods 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 230000009977 dual effect Effects 0.000 description 1
- 210000003979 eosinophil Anatomy 0.000 description 1
- 210000003013 erythroid precursor cell Anatomy 0.000 description 1
- 230000010437 erythropoiesis Effects 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 230000037433 frameshift Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 210000003958 hematopoietic stem cell Anatomy 0.000 description 1
- BTIJJDXEELBZFS-QDUVMHSLSA-K hemin Chemical compound CC1=C(CCC(O)=O)C(C=C2C(CCC(O)=O)=C(C)\C(N2[Fe](Cl)N23)=C\4)=N\C1=C/C2=C(C)C(C=C)=C3\C=C/1C(C)=C(C=C)C/4=N\1 BTIJJDXEELBZFS-QDUVMHSLSA-K 0.000 description 1
- 229940025294 hemin Drugs 0.000 description 1
- 230000002607 hemopoietic effect Effects 0.000 description 1
- -1 i.e. Proteins 0.000 description 1
- 238000000099 in vitro assay Methods 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 201000006370 kidney failure Diseases 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 210000003593 megakaryocyte Anatomy 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 150000003904 phospholipids Chemical class 0.000 description 1
- 210000001778 pluripotent stem cell Anatomy 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 239000007921 spray Substances 0.000 description 1
- 210000000130 stem cell Anatomy 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 230000007704 transition Effects 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- 238000002054 transplantation Methods 0.000 description 1
- 238000005199 ultracentrifugation Methods 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 210000001325 yolk sac Anatomy 0.000 description 1
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
- C07K14/52—Cytokines; Lymphokines; Interferons
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
-
- 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
- C07K14/475—Growth factors; Growth regulators
- C07K14/505—Erythropoietin [EPO]
-
- 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
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/54—Interleukins [IL]
- C07K14/5403—IL-3
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
- C07K2319/74—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor
- C07K2319/75—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor containing a fusion for activation of a cell surface receptor, e.g. thrombopoeitin, NPY and other peptide hormones
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Genetics & Genomics (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Diabetes (AREA)
- Hematology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Polymers With Sulfur, Phosphorus Or Metals In The Main Chain (AREA)
- Enzymes And Modification Thereof (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US58995890A | 1990-09-28 | 1990-09-28 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| IE913426A1 true IE913426A1 (en) | 1992-04-08 |
Family
ID=24360286
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IE342691A IE913426A1 (en) | 1990-09-28 | 1991-09-27 | Hybrid growth factors |
Country Status (8)
| Country | Link |
|---|---|
| EP (1) | EP0503050A4 (fr) |
| JP (1) | JPH05502463A (fr) |
| AU (2) | AU8735991A (fr) |
| CA (1) | CA2069746A1 (fr) |
| IE (1) | IE913426A1 (fr) |
| PT (1) | PT99107A (fr) |
| WO (1) | WO1992006116A1 (fr) |
| ZA (1) | ZA917766B (fr) |
Families Citing this family (29)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5718893A (en) * | 1984-04-15 | 1998-02-17 | Foster; Preston F. | Use of G-CSF to reduce acute rejection |
| WO1992004455A1 (fr) * | 1990-08-29 | 1992-03-19 | Genetics Institute, Inc. | Stimulateurs d'hematopoiese multidomaine |
| US5738849A (en) * | 1992-11-24 | 1998-04-14 | G. D. Searle & Co. | Interleukin-3 (IL-3) variant fusion proteins, their recombinant production, and therapeutic compositions comprising them |
| US6153183A (en) | 1992-11-24 | 2000-11-28 | G. D. Searle & Company | Co-administration of interleukin-3 mutant polypeptides with CSF's or cytokines for multi-lineage hematopoietic cell production |
| AU690088B2 (en) * | 1992-11-24 | 1998-04-23 | G.D. Searle & Co. | Interleukin-3 (IL-3) multiple mutation polypeptides |
| US6057133A (en) * | 1992-11-24 | 2000-05-02 | G. D. Searle | Multivariant human IL-3 fusion proteins and their recombinant production |
| US5501962A (en) * | 1993-06-21 | 1996-03-26 | G. D. Searle & Co. | Interleuken-3 (IL-3) human/murine hybrid polypeptides and recombinant production of the same |
| WO1995028427A1 (fr) * | 1994-04-15 | 1995-10-26 | Imclone Systems Incorporated | Lymphokine chimere composee de l'interleukine 3 et d'une muteine de l'interleukine 6 |
| US5536495A (en) * | 1994-04-15 | 1996-07-16 | Foster; Preston F. | Use of G-CSF to reduce acute rejection |
| ITFI940106A1 (it) * | 1994-05-27 | 1995-11-27 | Menarini Ricerche Sud Spa | Molecola ibrida di formula gm-csf-l-epo o epo-l-gm-csf per la stimolaz ione eritropoietica |
| IT1271688B (it) * | 1994-08-04 | 1997-06-04 | Menarini Ricerche Sud Spa | Molecole ibride per il trattamento antitumorale loro preparazione e loro uso in composizioni farmaceutiche |
| DE69636714T2 (de) * | 1995-04-26 | 2007-10-18 | Kyowa Hakko Kogyo Co., Ltd. | G-CSF TPO Fusionsproteine |
| US6066318A (en) | 1995-10-05 | 2000-05-23 | G.D. Searle & Co. | Multi-functional hematopoietic fusion proteins between sequence rearranged C-MPL receptor agonists and other hematopoietic factors |
| IL129028A0 (en) * | 1996-09-20 | 2000-02-17 | Ortho Mcneil Pharm Inc | Method for in vitro determination of erythropoietin bioactivity |
| WO1998018926A1 (fr) * | 1996-10-25 | 1998-05-07 | G.D. Searle & Co. | Agonistes de recepteurs d'erythropoietine permutes de maniere circulaire |
| US6967092B1 (en) | 1996-10-25 | 2005-11-22 | Mc Kearn John P | Multi-functional chimeric hematopoietic receptor agonists |
| NZ335382A (en) * | 1996-10-25 | 2001-03-30 | Searle & Co | Multi-functional chimeric hematopoietic polypeptides of IL-3, GCSF, Flt3L, EPO, stem cell factor, cmpl link with or without linker group consisting of Alanine, Glycine and/or Serine for treating autoimmune and tumour related diseases |
| US6165476A (en) * | 1997-07-10 | 2000-12-26 | Beth Israel Deaconess Medical Center | Fusion proteins with an immunoglobulin hinge region linker |
| US6187564B1 (en) | 1997-07-10 | 2001-02-13 | Beth Israel Deaconess Medical Center | DNA encoding erythropoietin multimers having modified 5′ and 3′ sequences and its use to prepare EPO therapeutics |
| EP0902085B1 (fr) * | 1997-09-01 | 2003-12-03 | Aventis Pharma Deutschland GmbH | Erythropoiétine humaine recombinante caractérisée par une glycosylation avantageuse |
| AU2866599A (en) * | 1998-02-17 | 1999-08-30 | Hyseq, Inc. | A novel interleukin-3 and uses thereof |
| BR9917606A (pt) * | 1998-11-06 | 2002-12-31 | Bio Sidus S A | Procedimento para a purificação de eritropoetina humana recombinante a partir de sobrenadantes de cultivo de células e eritropoetina humana recombinante obtida com tal procedimento |
| KR20050121762A (ko) | 2000-05-15 | 2005-12-27 | 에프. 호프만-라 로슈 아게 | 신규한 약학 조성물 |
| US7220407B2 (en) | 2003-10-27 | 2007-05-22 | Amgen Inc. | G-CSF therapy as an adjunct to reperfusion therapy in the treatment of acute myocardial infarction |
| ATE544463T1 (de) | 2004-11-05 | 2012-02-15 | Univ Northwestern | Verwendung von scf und g-scf bei der behandlung von hirnischämie und neurologischen störungen |
| EP2542574B1 (fr) | 2010-03-04 | 2017-08-09 | Pfenex Inc. | Procédé pour la production de la protéine interféron recombinante soluble sans dénaturation |
| PL2552949T3 (pl) | 2010-04-01 | 2017-01-31 | Pfenex Inc. | Sposoby wytwarzania G-CSF w komórce gospodarza Pseudomonas |
| SG11201500414SA (en) | 2012-07-31 | 2015-04-29 | Asahi Kasei E Materials Corp | Epoxy resin composition, epoxy resin, and cured product |
| LT6161B (lt) | 2013-09-27 | 2015-06-25 | Uab Profarma | Granuliocitų kolonijas stimuliuojančio faktoriaus sulieti baltymai su kitais augimo faktoriais, optimaliai su kamieninių ląstelių faktoriumi, ir jų gavimo būdas |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ES8407097A1 (es) * | 1982-05-12 | 1984-08-16 | Harvard College | Un procedimiento para obtener una proteina hibrida. |
| US4935352A (en) * | 1985-10-21 | 1990-06-19 | Takeda Chemical Industries, Ltd. | Expression vector for animal cell line and use thereof |
| US4935233A (en) * | 1985-12-02 | 1990-06-19 | G. D. Searle And Company | Covalently linked polypeptide cell modulators |
| DE3751664T2 (de) * | 1986-08-01 | 1996-06-05 | Commw Scient Ind Res Org | Rekombinanter impfstoff |
| EP0425536A4 (en) * | 1988-07-20 | 1992-01-02 | Immunex Corporation | Nonglycosylated human interleukin-3 compositions |
| US5166322A (en) * | 1989-04-21 | 1992-11-24 | Genetics Institute | Cysteine added variants of interleukin-3 and chemical modifications thereof |
| WO1991001004A1 (fr) * | 1989-07-06 | 1991-01-24 | Seragen, Inc. | Molecules hybrides |
| ES2055445T3 (es) * | 1989-08-22 | 1994-08-16 | Immunex Corp | Proteinas de fusion que comprenden gm-csf e il-3. |
| US5073627A (en) * | 1989-08-22 | 1991-12-17 | Immunex Corporation | Fusion proteins comprising GM-CSF and IL-3 |
| IL96477A0 (en) * | 1989-12-01 | 1991-08-16 | Amgen Inc | Megakaryocyte production |
| WO1992004455A1 (fr) * | 1990-08-29 | 1992-03-19 | Genetics Institute, Inc. | Stimulateurs d'hematopoiese multidomaine |
-
1991
- 1991-09-26 WO PCT/US1991/007053 patent/WO1992006116A1/fr not_active Application Discontinuation
- 1991-09-26 JP JP3517013A patent/JPH05502463A/ja active Pending
- 1991-09-26 AU AU87359/91A patent/AU8735991A/en not_active Abandoned
- 1991-09-26 EP EP19910918221 patent/EP0503050A4/en not_active Withdrawn
- 1991-09-26 CA CA002069746A patent/CA2069746A1/fr not_active Abandoned
- 1991-09-27 ZA ZA917766A patent/ZA917766B/xx unknown
- 1991-09-27 PT PT99107A patent/PT99107A/pt not_active Application Discontinuation
- 1991-09-27 IE IE342691A patent/IE913426A1/en not_active Application Discontinuation
-
1995
- 1995-02-06 AU AU11576/95A patent/AU1157695A/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| WO1992006116A1 (fr) | 1992-04-16 |
| EP0503050A4 (en) | 1994-07-06 |
| CA2069746A1 (fr) | 1992-03-29 |
| AU1157695A (en) | 1995-04-13 |
| ZA917766B (en) | 1993-03-29 |
| EP0503050A1 (fr) | 1992-09-16 |
| AU8735991A (en) | 1992-04-28 |
| PT99107A (pt) | 1992-08-31 |
| JPH05502463A (ja) | 1993-04-28 |
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| FC9A | Application refused sect. 31(1) |