Result 1 - 10 of total 374
2022
| Language | English |
|---|---|
| Publishing date | 2022-11-02 |
| Publishing country | de |
| Document type | Article ; Online |
| Database | BASE - Bielefeld Academic Search Engine (life sciences selection) |
Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.
1996 Volume 54, Issue 2-3, Page(s) 101–104
| MeSH term(s) | Complement Activation/immunology ; Humans ; Immunoglobulin G/immunology ; Oligosaccharides/immunology ; Receptors, IgG/immunology ; Tumor Cells, Cultured |
|---|---|
| Chemical Substances | Immunoglobulin G ; Oligosaccharides ; Receptors, IgG |
| Language | English |
| Publishing date | 1996-12 |
| Publishing country | Netherlands |
| Document type | Journal Article ; Research Support, Non-U.S. Gov't |
| ZDB-ID | 445150-8 |
| ISSN | 1879-0542 ; 0165-2478 |
| ISSN (online) | 1879-0542 |
| ISSN | 0165-2478 |
| DOI | 10.1016/s0165-2478(96)02656-9 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
| Zs.A 1512: Show issues | Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG) |
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British journal of hospital medicine (London, England : 2005)
2017 Volume 78, Issue 8, Page(s) 443–447
Abstract: In principle the whole human proteome is available for the generation of recombinant proteins and glycoproteins that may serve as drugs (biologics). Endogenous human proteins and glycoproteins are structurally heterogeneous but are recognized as self by ... ...
| Abstract | In principle the whole human proteome is available for the generation of recombinant proteins and glycoproteins that may serve as drugs (biologics). Endogenous human proteins and glycoproteins are structurally heterogeneous but are recognized as self by the immune system; however, recombinant protein and glycoprotein molecules are necessarily produced in heterologous systems and may include structural variants that are non-self and potentially immunogenic. The addition of human type oligosaccharides may be critical to function while the addition of non-human sugar residues can render biologics immunogenic. A particular concern is the structure of oligosaccharides attached by the hamster and murine cell lines that provide the dominant production platform. Critical structure and function properties that contribute to optimization of therapeutic potential are illustrated through recombinant erythropoietin and antibody therapeutics. |
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| MeSH term(s) | Animals ; Biological Products/economics ; Biological Products/immunology ; Biological Products/pharmacology ; Cost-Benefit Analysis ; Genetic Heterogeneity ; Humans ; Polymorphism, Genetic ; Recombinant Proteins/genetics ; Recombinant Proteins/immunology ; Recombinant Proteins/pharmacology ; Translational Medical Research/methods ; Translational Medical Research/trends |
| Chemical Substances | Biological Products ; Recombinant Proteins |
| Language | English |
| Publishing date | 2017-08-03 |
| Publishing country | England |
| Document type | Journal Article ; Review |
| ISSN | 1750-8460 |
| ISSN | 1750-8460 |
| DOI | 10.12968/hmed.2017.78.8.443 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
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Advances in biochemical engineering/biotechnology
2017 Volume 175, Page(s) 281–318
Abstract: The human genome has become a subject of public interest, whilst the proteome remains the province of specialists. Less appreciated is the human glycoprotein (GP) repertoire (proteoglycome!); however, some 50% of open reading frame genes encode for ... ...
| Abstract | The human genome has become a subject of public interest, whilst the proteome remains the province of specialists. Less appreciated is the human glycoprotein (GP) repertoire (proteoglycome!); however, some 50% of open reading frame genes encode for proteins (P) that may accept the addition of N-linked and/or O-linked sugar chains (oligosaccharides). It is established that the attachment of defined oligosaccharide structures impacts mechanisms of action (MoAs), pharmacokinetics, pharmacodynamics, etc., and is a critical quality attribute (CQA) for recombinant GP therapeutics. The oligosaccharide structure attached at a given site may exhibit structural heterogeneity, and individual structures (glycoforms) may modulate MoAs. The biopharmaceutical industry is challenged, therefore, to produce recombinant GP therapeutics that have structural fidelity to the natural (endogenous) molecule, in non-human cells. Multiple production platforms have been developed that, in addition to the natural glycoform, may produce unnatural glycoforms, including sugar residues that can be immunogenic in human subjects. Following a general introduction to the field, this review discusses glycosylation of recombinant monoclonal antibodies (mAbs), the contribution of glycoforms to MoAs and the development of customised mAb therapeutic glycoforms to optimise MoAs for individual disease indications. |
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| MeSH term(s) | Antibodies, Monoclonal/metabolism ; Glycoproteins/metabolism ; Glycosylation ; Oligosaccharides ; Recombinant Proteins/genetics |
| Chemical Substances | Antibodies, Monoclonal ; Glycoproteins ; Oligosaccharides ; Recombinant Proteins |
| Language | English |
| Publishing date | 2017-10-23 |
| Publishing country | Germany |
| Document type | Journal Article ; Review |
| ISSN | 0724-6145 |
| ISSN | 0724-6145 |
| DOI | 10.1007/10_2017_32 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
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Current pharmaceutical biotechnology
2016 Volume 17, Issue 15, Page(s) 1333–1347
Abstract: Advances in genetic and protein engineering and the ability to maintain proliferating mammalian cells in vitro, has allowed reverse engineering of antibodies, i.e. generation of antibodies having specificity for self-antigens. Thus, the lethal ... ...
| Abstract | Advances in genetic and protein engineering and the ability to maintain proliferating mammalian cells in vitro, has allowed reverse engineering of antibodies, i.e. generation of antibodies having specificity for self-antigens. Thus, the lethal consequence of horror autotoxicus, anti-self-responses as envisaged by Paul Ehrlich (1854-1915), has been turned to advantage for treatment of multiple disease states. In order to reap these benefits, it is essential that, in addition to target specificity, the antibody is customised to deliver appropriate downstream biologic effector activities. Genetic engineering allows the development of any chosen isotype; however, The IgG class predominates in human serum and the majority of monoclonal antibody (mAb) therapeutics are based on the IgG format. This review focuses on the structure and function of the four human IgG isotypes (subclasses) and the biologic functions that their immune complexes activate through interactions with cellular Fc receptors (FcγR & FcRn) and/or the C1q component of complement. The long catabolic half-life (~21 days) of IgG contributes to its efficacy as a therapeutic. Each human IgG subclass exhibits a unique profile of biologic activities that are dependent on the glycoform profile of the IgG-Fc. Our current understanding of IgG structure/function relationships allows protein and glycosylation engineering of the IgG-Fc to enhance or eliminate biologic activities and the generation of therapeutics optimal for a given disease indication. |
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| Language | English |
| Publishing date | 2016 |
| Publishing country | Netherlands |
| Document type | Journal Article |
| ZDB-ID | 2132197-8 |
| ISSN | 1873-4316 ; 1389-2010 |
| ISSN (online) | 1873-4316 |
| ISSN | 1389-2010 |
| DOI | 10.2174/1389201017666161029225929 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
| Zs.A 6212: Show issues | Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG) |
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Journal of immunology research
2016 Volume 2016, Page(s) 5358272
Abstract: Whilst the amino acid sequence of a protein is determined by its gene sequence, the final structure and function are determined by posttranslational modifications (PTMs), including quality control (QC) in the endoplasmic reticulum (ER) and during passage ...
| Abstract | Whilst the amino acid sequence of a protein is determined by its gene sequence, the final structure and function are determined by posttranslational modifications (PTMs), including quality control (QC) in the endoplasmic reticulum (ER) and during passage through the Golgi apparatus. These processes are species and cell specific and challenge the biopharmaceutical industry when developing a production platform for the generation of recombinant biologic therapeutics. Proteins and glycoproteins are also subject to chemical modifications (CMs) both in vivo and in vitro. The individual is naturally tolerant to molecular forms of self-molecules but nonself variants can provoke an immune response with the generation of anti-drug antibodies (ADA); aggregated forms can exhibit enhanced immunogenicity and QC procedures are developed to avoid or remove them. Monoclonal antibody therapeutics (mAbs) are a special case because their purpose is to bind the target, with the formation of immune complexes (ICs), a particular form of aggregate. Such ICs may be removed by phagocytic cells that have antigen presenting capacity. These considerations may frustrate the possibility of ameliorating the immunogenicity of mAbs by rigorous exclusion of aggregates from drug product. Alternate strategies for inducing immunosuppression or tolerance are discussed. |
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| MeSH term(s) | Animals ; Antibodies, Monoclonal/immunology ; Antigen-Antibody Complex ; Biological Therapy/adverse effects ; Humans ; Immune Tolerance ; Protein Aggregates/immunology ; Protein Processing, Post-Translational ; Recombinant Proteins/immunology ; Recombinant Proteins/metabolism |
| Chemical Substances | Antibodies, Monoclonal ; Antigen-Antibody Complex ; Protein Aggregates ; Recombinant Proteins |
| Language | English |
| Publishing date | 2016-04-14 |
| Publishing country | Egypt |
| Document type | Journal Article ; Review |
| ZDB-ID | 2817541-4 |
| ISSN | 2314-7156 ; 2314-7156 |
| ISSN (online) | 2314-7156 |
| ISSN | 2314-7156 |
| DOI | 10.1155/2016/5358272 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
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1990 Volume 27, Issue 12, Page(s) 1237–1240
Abstract: ... recognition and binding. It appears logical that the evolutionarily-related Fc gamma R molecules ...
| Abstract | Evidence from several experimental approaches allows us to conclude that the primary amino acid sequence of the lower hinge region (residues 234-237) of human IgG molecules determines recognition by human Fc gamma RI, Fc gamma RII and Fc gamma RIII. Glycosylation of the CH2 domain is also essential, although the carbohydrate is not accessible for direct interaction with ligands. The role of the carbohydrate moiety may be to maintain a protein conformation that allows accessibility to amino acid side chains essential for ligand recognition and binding. It appears logical that the evolutionarily-related Fc gamma R molecules should interact with overlapping non-identical sites on the IgG molecule. |
|---|---|
| MeSH term(s) | Amino Acids/physiology ; Animals ; Antibodies ; Antibodies, Monoclonal ; Antigens, Differentiation/chemistry ; Antigens, Differentiation/metabolism ; Chimera ; Glycosylation ; Humans ; Immunoglobulin Fc Fragments/metabolism ; Immunoglobulin G/metabolism ; Immunoglobulin Isotypes/metabolism ; Mice ; Rabbits ; Receptors, Fc/chemistry ; Receptors, Fc/metabolism ; Receptors, IgG ; Structure-Activity Relationship |
| Chemical Substances | Amino Acids ; Antibodies ; Antibodies, Monoclonal ; Antigens, Differentiation ; Immunoglobulin Fc Fragments ; Immunoglobulin G ; Immunoglobulin Isotypes ; Receptors, Fc ; Receptors, IgG |
| Language | English |
| Publishing date | 1990-12 |
| Publishing country | England |
| Document type | Journal Article |
| ZDB-ID | 424427-8 |
| ISSN | 1872-9142 ; 0161-5890 |
| ISSN (online) | 1872-9142 |
| ISSN | 0161-5890 |
| DOI | 10.1016/0161-5890(90)90027-w |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
| Zs.A 166: Show issues | Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG) |
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1989 Volume 66, Issue 4, Page(s) 491–498
Abstract: ... antibody-dependent cellular cytotoxicity (ADCC); (ii) to mediate binding to monocyte and lymphocyte Fc gamma R; (iii) to stimulate ... IgG1-induced lysis, suggesting that each subclass engages the same Fc gamma R receptor but that lysis ...
| Abstract | Polyclonal and monoclonal anti-Rh (D) antibodies of IgG1 and IgG3 subclass were evaluated for their capacity to sensitize erythrocytes and (i) to trigger monocyte and K-cell mediated antibody-dependent cellular cytotoxicity (ADCC); (ii) to mediate binding to monocyte and lymphocyte Fc gamma R; (iii) to stimulate phagocytosis by monocytes. All antibodies were equally effective in mediating monocyte or activated U937 cell ADCC but IgG1 was more active than IgG3 in K-cell mediated ADCC. IgG3-sensitized erythrocytes inhibited IgG1-induced lysis, suggesting that each subclass engages the same Fc gamma R receptor but that lysis requires a further 'signal' that the IgG3 molecule can not deliver. Two monoclonal IgG3 anti-D antibodies were shown to have higher binding (two times) and phagocytic (three times) indices than IgG1 antibody for monocytes; similar differences were observed for polyclonal IgG1 and IgG3 antibodies. The same pattern was observed in an EA rosette assay when a total lymphocyte population was used; however, this difference was not seen with a B-cell depleted (T+ null cell) lymphocyte population. |
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| MeSH term(s) | Antibodies, Monoclonal/immunology ; Antibody-Dependent Cell Cytotoxicity ; Antigens, Differentiation/immunology ; Erythrocytes/immunology ; Humans ; Immunoglobulin G/immunology ; Killer Cells, Natural/immunology ; Monocytes/immunology ; Phagocytosis ; Receptors, Fc/immunology ; Receptors, IgG ; Rh-Hr Blood-Group System/immunology ; Rosette Formation |
| Chemical Substances | Antibodies, Monoclonal ; Antigens, Differentiation ; Immunoglobulin G ; Receptors, Fc ; Receptors, IgG ; Rh-Hr Blood-Group System |
| Language | English |
| Publishing date | 1989-04 |
| Publishing country | England |
| Document type | Journal Article |
| ZDB-ID | 80124-0 |
| ISSN | 1365-2567 ; 0019-2805 ; 0953-4954 |
| ISSN (online) | 1365-2567 |
| ISSN | 0019-2805 ; 0953-4954 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
| Ud II Zs.181: Show issues | Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG) |
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2023 Volume 37, Issue 1, Page(s) 7–21
Abstract: Kidney function is strongly influenced by genetic factors with both monogenic and polygenic factors contributing to kidney function. Monogenic disorders with primarily autosomal dominant inheritance patterns account for 10% of adult and 50% of paediatric ...
| Abstract | Kidney function is strongly influenced by genetic factors with both monogenic and polygenic factors contributing to kidney function. Monogenic disorders with primarily autosomal dominant inheritance patterns account for 10% of adult and 50% of paediatric kidney diseases. However, kidney function is also a complex trait with polygenic architecture, where genetic factors interact with environment and lifestyle factors. Family studies suggest that kidney function has significant heritability at 35-69%, capturing complexities of the genome with shared environmental factors. Genome-wide association studies estimate the single nucleotide polymorphism-based heritability of kidney function between 7.1 and 20.3%. These heritability estimates, measuring the extent to which genetic variation contributes to CKD risk, indicate a strong genetic contribution. Polygenic Risk Scores have recently been developed for chronic kidney disease and kidney function, and validated in large populations. Polygenic Risk Scores show correlation with kidney function but lack the specificity to predict individual-level changes in kidney function. Certain kidney diseases, such as membranous nephropathy and IgA nephropathy that have significant genetic components, may benefit most from polygenic risk scores for improved risk stratification. Genetic studies of kidney function also provide a potential avenue for the development of more targeted therapies and interventions. Understanding the development and validation of genomic scores is required to guide their implementation and identify the most appropriate potential implications in clinical practice. In this review, we provide an overview of the heritability of kidney function traits in population studies, explore both monogenic and polygenic concepts in kidney disease, with a focus on recently developed polygenic risk scores in kidney function and chronic kidney disease, and review specific diseases which are most amenable to incorporation of genomic scores. |
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| MeSH term(s) | Adult ; Child ; Humans ; Multifactorial Inheritance ; Genome-Wide Association Study ; Phenotype ; Genetic Risk Score ; Renal Insufficiency, Chronic/diagnosis ; Renal Insufficiency, Chronic/genetics ; Genetic Predisposition to Disease ; Polymorphism, Single Nucleotide |
| Language | English |
| Publishing date | 2023-11-21 |
| Publishing country | Italy |
| Document type | Journal Article ; Review |
| ZDB-ID | 1093991-x |
| ISSN | 1724-6059 ; 1120-3625 ; 1121-8428 |
| ISSN (online) | 1724-6059 |
| ISSN | 1120-3625 ; 1121-8428 |
| DOI | 10.1007/s40620-023-01804-8 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
| Zs.A 3369: Show issues | Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG) |
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Archives of biochemistry and biophysics
2012 Volume 526, Issue 2, Page(s) 159–166
Abstract: We live in a hostile environment but are protected by the innate and adaptive immune system. A major component of the latter is mediated by antibody molecules that bind to pathogens, with exquisite specificity, and the immune complex formed activates ... ...
| Abstract | We live in a hostile environment but are protected by the innate and adaptive immune system. A major component of the latter is mediated by antibody molecules that bind to pathogens, with exquisite specificity, and the immune complex formed activates cellular mechanisms leading to the removal and destruction of the complex. Five classes of antibody are identified; however, the IgG class predominates in serum and a majority of monoclonal antibody (mAb) therapeutics are based on the IgG format. Selection within the antibody repertoire allows the generation of (mAb) having specificity for any selected target, including human antigens. This review focuses on the structure and function of the Fc region of IgG molecules that mediates biologic functions, within immune complexes, by interactions with cellular Fc receptors (FcγR) and/or the C1q component of complement. A property of IgG that is suited to its use as a therapeutic is the long catabolic half life of ~21 days, mediated through the structurally distinct neonatal Fc receptor (FcRn). Our understanding of structure/function relationships is such that we can contemplate engineering the IgG-Fc to enhance or eliminate biologic activities to generate therapeutics considered optimal for a given disease indication. There are four subclasses of human IgG that exhibit high sequence homology but a unique profile of biologic activities. The FcγR and the C1q binding functions are dependent on glycosylation of the IgG-Fc. Normal human serum IgG is comprised of multiple glycoforms and biologic activities, other than catabolism, varies between glycoforms. |
|---|---|
| MeSH term(s) | Animals ; Carbohydrate Sequence ; Complement Activation ; Complement C1q/immunology ; Glycosylation ; Humans ; Immunoglobulin Fc Fragments/chemistry ; Immunoglobulin Fc Fragments/immunology ; Immunoglobulin Fc Fragments/metabolism ; Immunoglobulin G/chemistry ; Immunoglobulin G/immunology ; Immunoglobulin G/metabolism ; Models, Molecular ; Molecular Sequence Data ; Oligosaccharides/chemistry ; Oligosaccharides/immunology ; Oligosaccharides/metabolism ; Protein Conformation ; Protein Isoforms/chemistry ; Protein Isoforms/immunology ; Protein Isoforms/metabolism ; Receptors, Fc/immunology |
| Chemical Substances | Immunoglobulin Fc Fragments ; Immunoglobulin G ; Oligosaccharides ; Protein Isoforms ; Receptors, Fc ; Complement C1q (80295-33-6) |
| Language | English |
| Publishing date | 2012-10-15 |
| Publishing country | United States |
| Document type | Journal Article ; Review |
| ZDB-ID | 523-x |
| ISSN | 1096-0384 ; 0003-9861 |
| ISSN (online) | 1096-0384 |
| ISSN | 0003-9861 |
| DOI | 10.1016/j.abb.2012.03.021 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
| Uc I Zs.237: Show issues | Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG) |
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