WO1992001058A1 - Hybridomas - Google Patents
Hybridomas Download PDFInfo
- Publication number
- WO1992001058A1 WO1992001058A1 PCT/GB1991/001145 GB9101145W WO9201058A1 WO 1992001058 A1 WO1992001058 A1 WO 1992001058A1 GB 9101145 W GB9101145 W GB 9101145W WO 9201058 A1 WO9201058 A1 WO 9201058A1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- cell
- cells
- hybrid
- somatic
- myeloma
- Prior art date
Links
- 210000004408 hybridoma Anatomy 0.000 title description 2
- 210000004027 cell Anatomy 0.000 claims abstract description 34
- 210000004754 hybrid cell Anatomy 0.000 claims abstract description 24
- 210000001082 somatic cell Anatomy 0.000 claims abstract description 15
- 206010035226 Plasma cell myeloma Diseases 0.000 claims abstract description 10
- 201000000050 myeloid neoplasm Diseases 0.000 claims abstract description 10
- 230000028327 secretion Effects 0.000 claims abstract description 5
- 238000000034 method Methods 0.000 claims description 4
- 108090000623 proteins and genes Proteins 0.000 claims description 4
- 229930186217 Glycolipid Natural products 0.000 claims description 3
- 241000700605 Viruses Species 0.000 claims description 3
- 239000003795 chemical substances by application Substances 0.000 claims description 3
- 239000003102 growth factor Substances 0.000 claims description 3
- 230000001817 pituitary effect Effects 0.000 claims description 3
- 230000003248 secreting effect Effects 0.000 claims description 3
- HVCOBJNICQPDBP-UHFFFAOYSA-N 3-[3-[3,5-dihydroxy-6-methyl-4-(3,4,5-trihydroxy-6-methyloxan-2-yl)oxyoxan-2-yl]oxydecanoyloxy]decanoic acid;hydrate Chemical compound O.OC1C(OC(CC(=O)OC(CCCCCCC)CC(O)=O)CCCCCCC)OC(C)C(O)C1OC1C(O)C(O)C(O)C(C)O1 HVCOBJNICQPDBP-UHFFFAOYSA-N 0.000 claims description 2
- 102000003886 Glycoproteins Human genes 0.000 claims description 2
- 108090000288 Glycoproteins Proteins 0.000 claims description 2
- 102000004895 Lipoproteins Human genes 0.000 claims description 2
- 108090001030 Lipoproteins Proteins 0.000 claims description 2
- 210000002556 adrenal cortex cell Anatomy 0.000 claims description 2
- 210000001943 adrenal medulla Anatomy 0.000 claims description 2
- 239000012528 membrane Substances 0.000 claims description 2
- 239000003226 mitogen Substances 0.000 claims description 2
- 210000004102 animal cell Anatomy 0.000 claims 1
- 238000012258 culturing Methods 0.000 claims 1
- 210000005260 human cell Anatomy 0.000 claims 1
- 239000000047 product Substances 0.000 description 22
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 6
- 230000004927 fusion Effects 0.000 description 5
- 210000001685 thyroid gland Anatomy 0.000 description 4
- 108090001061 Insulin Proteins 0.000 description 3
- 102000004877 Insulin Human genes 0.000 description 3
- 229940125396 insulin Drugs 0.000 description 3
- 102000012673 Follicle Stimulating Hormone Human genes 0.000 description 2
- 108010079345 Follicle Stimulating Hormone Proteins 0.000 description 2
- 108010051696 Growth Hormone Proteins 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 102100038803 Somatotropin Human genes 0.000 description 2
- 102000003978 Tissue Plasminogen Activator Human genes 0.000 description 2
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 description 2
- 150000001413 amino acids Chemical group 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 201000011510 cancer Diseases 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 230000007910 cell fusion Effects 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 239000000122 growth hormone Substances 0.000 description 2
- 210000005229 liver cell Anatomy 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 229960000187 tissue plasminogen activator Drugs 0.000 description 2
- 241000709687 Coxsackievirus Species 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 102000003951 Erythropoietin Human genes 0.000 description 1
- 108090000394 Erythropoietin Proteins 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 238000003744 In vitro fertilisation Methods 0.000 description 1
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 description 1
- 206010025323 Lymphomas Diseases 0.000 description 1
- 102000043276 Oncogene Human genes 0.000 description 1
- 108700020796 Oncogene Proteins 0.000 description 1
- 241000702244 Orthoreovirus Species 0.000 description 1
- 102000052651 Pancreatic hormone Human genes 0.000 description 1
- 108700020479 Pancreatic hormone Proteins 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 102000003946 Prolactin Human genes 0.000 description 1
- 108010057464 Prolactin Proteins 0.000 description 1
- 102000013275 Somatomedins Human genes 0.000 description 1
- 102000009843 Thyroglobulin Human genes 0.000 description 1
- 108010034949 Thyroglobulin Proteins 0.000 description 1
- 102000003911 Thyrotropin Receptors Human genes 0.000 description 1
- 108090000253 Thyrotropin Receptors Proteins 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 210000000601 blood cell Anatomy 0.000 description 1
- 210000002798 bone marrow cell Anatomy 0.000 description 1
- 210000004958 brain cell Anatomy 0.000 description 1
- 230000005907 cancer growth Effects 0.000 description 1
- 230000032823 cell division Effects 0.000 description 1
- 229940105423 erythropoietin Drugs 0.000 description 1
- 210000002907 exocrine cell Anatomy 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 229940028334 follicle stimulating hormone Drugs 0.000 description 1
- 210000001035 gastrointestinal tract Anatomy 0.000 description 1
- 238000012215 gene cloning Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 230000030414 genetic transfer Effects 0.000 description 1
- 210000003494 hepatocyte Anatomy 0.000 description 1
- 125000005842 heteroatom Chemical group 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 231100000405 induce cancer Toxicity 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 210000004153 islets of langerhan Anatomy 0.000 description 1
- 125000003473 lipid group Chemical group 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 210000005265 lung cell Anatomy 0.000 description 1
- 230000001592 luteinising effect Effects 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 231100000590 oncogenic Toxicity 0.000 description 1
- 230000002246 oncogenic effect Effects 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 239000004025 pancreas hormone Substances 0.000 description 1
- 230000009996 pancreatic endocrine effect Effects 0.000 description 1
- 229940032957 pancreatic hormone Drugs 0.000 description 1
- 230000003169 placental effect Effects 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 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 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 229940097325 prolactin Drugs 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000002381 testicular Effects 0.000 description 1
- 229960002175 thyroglobulin Drugs 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 210000005253 yeast cell 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
- C07K14/575—Hormones
- C07K14/61—Growth hormone [GH], i.e. somatotropin
-
- 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
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- 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
- C07K14/575—Hormones
- C07K14/59—Follicle-stimulating hormone [FSH]; Chorionic gonadotropins, e.g.hCG [human chorionic gonadotropin]; Luteinising hormone [LH]; Thyroid-stimulating hormone [TSH]
-
- 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
- C07K14/575—Hormones
- C07K14/62—Insulins
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
- C12N5/10—Cells modified by introduction of foreign genetic material
- C12N5/12—Fused cells, e.g. hybridomas
- C12N5/16—Animal cells
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2510/00—Genetically modified cells
- C12N2510/02—Cells for production
Definitions
- This invention relates to immortalised hybrid cells which code for, express and secrete biological cell and membrane products, their production and use.
- Desired biological products can be produced by growing bacterial or yeast cells whose DNA has been modified, by recombinant technology, to express the products.
- Current genetic transfer/fusion techniques provide cells which are capable of secreting desired polypeptides.
- a desired product containing an amino-acid sequence and an additional moiety such as a carbohydrate, lipid or glycolipid cannot be easily secreted.
- the additional moiety must be added to the amino-acid sequence of the product at a later stage in product synthesis.
- biological products having such additional moieties are glycoproteins, lipoproteins and glycolipids.
- Moieties such as lipids or carbohydrates are important in the synthesis of biological products; their presence may be crucial in determining the stability and the biological/i munological activity of the final product.
- Immortalised hybrid cells are disclosed in WO-A-8705929.
- immortalised human liver cells and pancreatic islet cells are disclosed, respectively capable of secreting liver proteins and insulin.
- Such cells are also disclosed in WO-A-8907601. They are produced by fusing a heteromyeloma and a somatic cell.
- the present invention provides a hybrid cell line which is the product of cell fusion between a myeloma cell and a species-related somatic cell.
- Activation comprises infection, as by a virus, or other transformation, e.g. by means of growth factors or mitogens, by means of which the genetic signals are amplified, and secretion is increased.
- Hybrid cells of the present invention can be used to produce desired biological products that are expressed by the somatic cell. It is an advantage of the invention that, if the myeloma cells are of, say, animal origin, no human oncogenic products are secreted in addition to the desired product when the hybrid cell products are used in humans. It is preferred that the hybrid cells are the product of cell fusion between human myeloma cells and human somatic cells.
- Standard gene cloning or fusion technologies can be used to produce a human or other hetero yeloma cell line which is derived from, say, another animal myeloma cell line.
- Standard techniques can be used to fuse cells from the heteromyeloma cell line with cells from a line of selected human somatic cells such as thyroid cells, to produce a hybrid cell line. All the genes of the thyroid cell are incorporated into the hybrid and expressed, and cell products are secreted.
- hybrid cell lines derived from human somatic cells which are, for example, pituitary cells, pancreatic endocrine and exocrine cells, adrenal medulla and cortex cells, blood cells, liver cells, lung cells, brain cells, bone marrow cells, gut cells, placental cells, ovary cells and testicular cells.
- the hybrid cells can be cultured to express and secrete products expressed by the somatic cell; provided that the hybrid cells retain the appropriate genes, the products will continue to be secreted.
- Insulin and other pancreatic hormones and enzymes can be produced from hybrid pancreatic cells, while LH (luteinising hormone) , FSH (follicle-stimulating hormone) , GH (growth hormone) , prolactin and TSH can be produced from hybrid pituitary cells. LH and FSH are recognised to enhance the success rate of in vitro fertilisation procedures. Other products of interest are erythropoietin and TPA (tissue plasminogen activator) .
- some somatic cells, including pancreatic cells can be activated by certain Coxsackie viruses. Reoviruses will activate, for example, hepatic cells. Adrenoviruses, papovaviruses and leukoviruses can also infect and activate cells. The activating virus or other agent should have the effect of increasing cell division and thus increasing expression.
- Activated hybridomas of the invention are generally more stable than the corresponding known, unactivated hybrid cells. Fusion and expression/secretion are also more reliable.
- Example 1 illustrates the invention.
- Human thyroid cells were activated with a mixture of growth factors and cytokines from the supernatant of a lymphoma cell line supplemented with insulin and insulin-like growth factors; for 3 days.
- the activated thyroid cells were then fused with a myeloma fusion partner, HMYl, using polyethylene glycol.
- Hybrid cells were screened for the secretion of thyroglobulin and CAMP, and for expression of TSH receptors.
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Zoology (AREA)
- Endocrinology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Biophysics (AREA)
- Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Wood Science & Technology (AREA)
- Biotechnology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Reproductive Health (AREA)
- Cell Biology (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Diabetes (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
A hybrid cell comprising a myeloma cell fused to a somatic cell which has been transformed with an agent which enhances secretion.
Description
HYBRIDO AS
Field of the Invention
This invention relates to immortalised hybrid cells which code for, express and secrete biological cell and membrane products, their production and use. Background of the Invention
Desired biological products can be produced by growing bacterial or yeast cells whose DNA has been modified, by recombinant technology, to express the products. Current genetic transfer/fusion techniques provide cells which are capable of secreting desired polypeptides. However, a desired product containing an amino-acid sequence and an additional moiety such as a carbohydrate, lipid or glycolipid cannot be easily secreted. The additional moiety must be added to the amino-acid sequence of the product at a later stage in product synthesis. Examples of biological products having such additional moieties are glycoproteins, lipoproteins and glycolipids. Moieties such as lipids or carbohydrates are important in the synthesis of biological products; their presence may be crucial in determining the stability and the biological/i munological activity of the final product. It is known to produce immortal hybrid cells by transfection/fusion of oncogenes or myeloma lines with somatic cells, usually of the same species. The use of such hybrid cells to produce a desired product carries high risk that cancer products will also be produced. Contaminating cancer products could induce cancer growth in individuals that are treated with the product. Immortalised hybrid cells are disclosed in WO-A-8705929. For example, immortalised human liver cells and pancreatic islet cells are disclosed, respectively capable of secreting liver proteins and insulin.
-2-
Such cells are also disclosed in WO-A-8907601. They are produced by fusing a heteromyeloma and a somatic cell.
Summary of the Invention The present invention provides a hybrid cell line which is the product of cell fusion between a myeloma cell and a species-related somatic cell. Activation comprises infection, as by a virus, or other transformation, e.g. by means of growth factors or mitogens, by means of which the genetic signals are amplified, and secretion is increased. Detailed Description of the Invention
Hybrid cells of the present invention can be used to produce desired biological products that are expressed by the somatic cell. It is an advantage of the invention that, if the myeloma cells are of, say, animal origin, no human oncogenic products are secreted in addition to the desired product when the hybrid cell products are used in humans. It is preferred that the hybrid cells are the product of cell fusion between human myeloma cells and human somatic cells.
Standard gene cloning or fusion technologies can be used to produce a human or other hetero yeloma cell line which is derived from, say, another animal myeloma cell line. Standard techniques can be used to fuse cells from the heteromyeloma cell line with cells from a line of selected human somatic cells such as thyroid cells, to produce a hybrid cell line. All the genes of the thyroid cell are incorporated into the hybrid and expressed, and cell products are secreted.
Similar techniques to those outlined above can be used to produce hybrid cell lines derived from human somatic cells which are, for example, pituitary cells, pancreatic endocrine and exocrine cells, adrenal medulla and cortex cells, blood cells, liver cells, lung cells,
brain cells, bone marrow cells, gut cells, placental cells, ovary cells and testicular cells. The hybrid cells can be cultured to express and secrete products expressed by the somatic cell; provided that the hybrid cells retain the appropriate genes, the products will continue to be secreted.
Insulin and other pancreatic hormones and enzymes can be produced from hybrid pancreatic cells, while LH (luteinising hormone) , FSH (follicle-stimulating hormone) , GH (growth hormone) , prolactin and TSH can be produced from hybrid pituitary cells. LH and FSH are recognised to enhance the success rate of in vitro fertilisation procedures. Other products of interest are erythropoietin and TPA (tissue plasminogen activator) . By way of example, some somatic cells, including pancreatic cells, can be activated by certain Coxsackie viruses. Reoviruses will activate, for example, hepatic cells. Adrenoviruses, papovaviruses and leukoviruses can also infect and activate cells. The activating virus or other agent should have the effect of increasing cell division and thus increasing expression.
Activated hybridomas of the invention are generally more stable than the corresponding known, unactivated hybrid cells. Fusion and expression/secretion are also more reliable.
The following Example illustrates the invention. Example
Human thyroid cells were activated with a mixture of growth factors and cytokines from the supernatant of a lymphoma cell line supplemented with insulin and insulin-like growth factors; for 3 days. The activated thyroid cells were then fused with a myeloma fusion partner, HMYl, using polyethylene glycol. Hybrid cells were screened for the secretion of thyroglobulin and CAMP, and for expression of TSH receptors.
Claims
1. A hybrid cell comprising a myeloma cell fused to a somatic cell which has been transformed with an agent which enhances secretion.
2. A hybrid cell according to claim 1, in which the somatic cell is a pituitary cell.
3. A hybrid cell according to claim 1, in which the somatic cell is an adrenal medulla or cortex cell.
4. A hybrid cell according to claim 1, in which the somatic cell is a pancreatic cell.
5. A hybrid cell according to any preceding claim, in which the myeloma cell and somatic cell are human cells.
6. A hybrid cell according to claim 5, in which the myeloma cell contains genes from an animal cell.
7. A hybrid cell according to any preceding claim, which is capable of secreting a lipoprotein, glycoprotein or glycolipid.
8. A hybrid cell according to any preceding claim, in which the agent is a virus, growth factor or mitogen.
9. A method of producing a biological cell and/or membrane product, which comprises culturing a hybrid cell according to any preceding claim.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB909015327A GB9015327D0 (en) | 1990-07-12 | 1990-07-12 | Hybridomas |
| GB9015327.1 | 1990-07-12 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| WO1992001058A1 true WO1992001058A1 (en) | 1992-01-23 |
Family
ID=10678977
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PCT/GB1991/001145 WO1992001058A1 (en) | 1990-07-12 | 1991-07-11 | Hybridomas |
Country Status (2)
| Country | Link |
|---|---|
| GB (1) | GB9015327D0 (en) |
| WO (1) | WO1992001058A1 (en) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1999011759A1 (en) * | 1997-09-04 | 1999-03-11 | University Of Aberdeen | GLUCOSE RESPONSIVE β-CELL LINE |
Citations (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB2083826A (en) * | 1980-07-30 | 1982-03-31 | Hayashibara Biochem Lab | Process for the production of human insulin |
| GB2091741A (en) * | 1980-12-13 | 1982-08-04 | Hayashibara Biochem Lab | Process for the Production of Human Adrenocorticotropic Hormone |
| GB2092156A (en) * | 1980-12-30 | 1982-08-11 | Hayashibara Biochem Lab | Process for the production of human thyroid-stimulating hormone |
| GB2092157A (en) * | 1980-12-30 | 1982-08-11 | Hayashibara Biochem Lab | Process for the production of human calcitonin |
| GB2092596A (en) * | 1980-12-30 | 1982-08-18 | Hayashibara Biochem Lab | Process for the production of human parathyroid hormone |
| EP0163218A2 (en) * | 1984-05-31 | 1985-12-04 | Sloan-Kettering Institute For Cancer Research | Method for the production of human T-T cell hybridomas and production of suppressor factor by human T-T cell hybridomas |
| US4806476A (en) * | 1983-09-08 | 1989-02-21 | Lovelace Medical Foundation | Efficient cell fusion process |
-
1990
- 1990-07-12 GB GB909015327A patent/GB9015327D0/en active Pending
-
1991
- 1991-07-11 WO PCT/GB1991/001145 patent/WO1992001058A1/en unknown
Patent Citations (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB2083826A (en) * | 1980-07-30 | 1982-03-31 | Hayashibara Biochem Lab | Process for the production of human insulin |
| GB2091741A (en) * | 1980-12-13 | 1982-08-04 | Hayashibara Biochem Lab | Process for the Production of Human Adrenocorticotropic Hormone |
| GB2092156A (en) * | 1980-12-30 | 1982-08-11 | Hayashibara Biochem Lab | Process for the production of human thyroid-stimulating hormone |
| GB2092157A (en) * | 1980-12-30 | 1982-08-11 | Hayashibara Biochem Lab | Process for the production of human calcitonin |
| GB2092596A (en) * | 1980-12-30 | 1982-08-18 | Hayashibara Biochem Lab | Process for the production of human parathyroid hormone |
| US4806476A (en) * | 1983-09-08 | 1989-02-21 | Lovelace Medical Foundation | Efficient cell fusion process |
| EP0163218A2 (en) * | 1984-05-31 | 1985-12-04 | Sloan-Kettering Institute For Cancer Research | Method for the production of human T-T cell hybridomas and production of suppressor factor by human T-T cell hybridomas |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1999011759A1 (en) * | 1997-09-04 | 1999-03-11 | University Of Aberdeen | GLUCOSE RESPONSIVE β-CELL LINE |
| GB2343895A (en) * | 1997-09-04 | 2000-05-24 | Univ Aberdeen | Glucose responsive ß-cell line |
| GB2343895B (en) * | 1997-09-04 | 2001-09-05 | Univ Aberdeen | Glucose responsive ß-cell line |
Also Published As
| Publication number | Publication date |
|---|---|
| GB9015327D0 (en) | 1990-08-29 |
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