Antibody Pharmacokinetics and Pharmacodynamics

The U.S. Food and Drug administration (FDA) has approved several polyclonal antibody preparations and at least 18 monoclonal antibody preparations (antibodies, antibody fragments, antibody fusion proteins, etc.). These drugs, which may be considered as a diverse group of therapeutic proteins, are as...

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Published in	Journal of pharmaceutical sciences Vol. 93; no. 11; pp. 2645 - 2668
Main Authors	Lobo, Evelyn D., Hansen, Ryan J., Balthasar, Joseph P.
Format	Journal Article
Language	English
Published	Hoboken Elsevier Inc 01.11.2004 Wiley Subscription Services, Inc., A Wiley Company Wiley American Pharmaceutical Association
Subjects	Animals Antibodies - chemistry Antibodies - metabolism Antibodies - pharmacology Binding Sites, Antibody - drug effects Binding Sites, Antibody - physiology Biological and medical sciences General pharmacology Humans Immunoglobulin Fragments - chemistry Immunoglobulin Fragments - metabolism Immunoglobulin Fragments - pharmacology Medical sciences Pharmaceutical Preparations - chemistry Pharmaceutical Preparations - metabolism Pharmaceutical technology. Pharmaceutical industry Pharmacology. Drug treatments Pharmacokinetic pharmacodynamic relationship Antibody Pharmaceutical technology
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Abstract	The U.S. Food and Drug administration (FDA) has approved several polyclonal antibody preparations and at least 18 monoclonal antibody preparations (antibodies, antibody fragments, antibody fusion proteins, etc.). These drugs, which may be considered as a diverse group of therapeutic proteins, are associated with several interesting pharmacokinetic characteristics. Saturable binding with target antigen may influence antibody disposition, potentially leading to nonlinear distribution and elimination. Independent of antigen interaction, concentration‐dependent elimination may be expected for IgG antibodies, due to the influence of the Brambell receptor, FcRn, which protects IgG from catabolism. Antibody administration may induce the development of an endogenous antibody response, which may alter the pharmacokinetics of the therapeutic antibody. Additionally, the pharmacodynamics of antibodies are also complex; these drugs may be used for a wide array of therapeutic applications, and effects may be achieved by a variety of mechanisms. This article provides an overview of many of the complexities associated with antibody pharmacokinetics and pharmacodynamics. © 2004 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 93:2645–2668, 2004
AbstractList	The U.S. Food and Drug administration (FDA) has approved several polyclonal antibody preparations and at least 18 monoclonal antibody preparations (antibodies, antibody fragments, antibody fusion proteins, etc.). These drugs, which may be considered as a diverse group of therapeutic proteins, are associated with several interesting pharmacokinetic characteristics. Saturable binding with target antigen may influence antibody disposition, potentially leading to nonlinear distribution and elimination. Independent of antigen interaction, concentration-dependent elimination may be expected for IgG antibodies, due to the influence of the Brambell receptor, FcRn, which protects IgG from catabolism. Antibody administration may induce the development of an endogenous antibody response, which may alter the pharmacokinetics of the therapeutic antibody. Additionally, the pharmacodynamics of antibodies are also complex; these drugs may be used for a wide array of therapeutic applications, and effects may be achieved by a variety of mechanisms. This article provides an overview of many of the complexities associated with antibody pharmacokinetics and pharmacodynamics. The U.S. Food and Drug administration (FDA) has approved several polyclonal antibody preparations and at least 18 monoclonal antibody preparations (antibodies, antibody fragments, antibody fusion proteins, etc.). These drugs, which may be considered as a diverse group of therapeutic proteins, are associated with several interesting pharmacokinetic characteristics. Saturable binding with target antigen may influence antibody disposition, potentially leading to nonlinear distribution and elimination. Independent of antigen interaction, concentration-dependent elimination may be expected for IgG antibodies, due to the influence of the Brambell receptor, FcRn, which protects IgG from catabolism. Antibody administration may induce the development of an endogenous antibody response, which may alter the pharmacokinetics of the therapeutic antibody. Additionally, the pharmacodynamics of antibodies are also complex; these drugs may be used for a wide array of therapeutic applications, and effects may be achieved by a variety of mechanisms. This article provides an overview of many of the complexities associated with antibody pharmacokinetics and pharmacodynamics.The U.S. Food and Drug administration (FDA) has approved several polyclonal antibody preparations and at least 18 monoclonal antibody preparations (antibodies, antibody fragments, antibody fusion proteins, etc.). These drugs, which may be considered as a diverse group of therapeutic proteins, are associated with several interesting pharmacokinetic characteristics. Saturable binding with target antigen may influence antibody disposition, potentially leading to nonlinear distribution and elimination. Independent of antigen interaction, concentration-dependent elimination may be expected for IgG antibodies, due to the influence of the Brambell receptor, FcRn, which protects IgG from catabolism. Antibody administration may induce the development of an endogenous antibody response, which may alter the pharmacokinetics of the therapeutic antibody. Additionally, the pharmacodynamics of antibodies are also complex; these drugs may be used for a wide array of therapeutic applications, and effects may be achieved by a variety of mechanisms. This article provides an overview of many of the complexities associated with antibody pharmacokinetics and pharmacodynamics. The U.S. Food and Drug administration (FDA) has approved several polyclonal antibody preparations and at least 18 monoclonal antibody preparations (antibodies, antibody fragments, antibody fusion proteins, etc.). These drugs, which may be considered as a diverse group of therapeutic proteins, are associated with several interesting pharmacokinetic characteristics. Saturable binding with target antigen may influence antibody disposition, potentially leading to nonlinear distribution and elimination. Independent of antigen interaction, concentration‐dependent elimination may be expected for IgG antibodies, due to the influence of the Brambell receptor, FcRn, which protects IgG from catabolism. Antibody administration may induce the development of an endogenous antibody response, which may alter the pharmacokinetics of the therapeutic antibody. Additionally, the pharmacodynamics of antibodies are also complex; these drugs may be used for a wide array of therapeutic applications, and effects may be achieved by a variety of mechanisms. This article provides an overview of many of the complexities associated with antibody pharmacokinetics and pharmacodynamics. © 2004 Wiley‐Liss, Inc. and the American Pharmacists Association J Pharm Sci 93:2645–2668, 2004
Author	Hansen, Ryan J. Balthasar, Joseph P. Lobo, Evelyn D.
Author_xml	– sequence: 1 givenname: Evelyn D. surname: Lobo fullname: Lobo, Evelyn D. organization: Global PK/PD and Trial Simulations, Lilly Research Laboratories, Lilly Corporate Center, Indianapolis, Indiana 46285 – sequence: 2 givenname: Ryan J. surname: Hansen fullname: Hansen, Ryan J. organization: Global PK/PD and Trial Simulations, Lilly Research Laboratories, Lilly Corporate Center, Indianapolis, Indiana 46285 – sequence: 3 givenname: Joseph P. surname: Balthasar fullname: Balthasar, Joseph P. email: jb@acsu.buffalo.edu organization: Department of Pharmaceutical Sciences, University at Buffalo, The State University of New York, Buffalo, New York 14260
BackLink	http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16264447$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/15389672$$D View this record in MEDLINE/PubMed
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Keywords	Pharmacokinetic pharmacodynamic relationship Antibody Pharmaceutical technology
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Snippet	The U.S. Food and Drug administration (FDA) has approved several polyclonal antibody preparations and at least 18 monoclonal antibody preparations (antibodies,...
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SubjectTerms	Animals Antibodies - chemistry Antibodies - metabolism Antibodies - pharmacology Binding Sites, Antibody - drug effects Binding Sites, Antibody - physiology Biological and medical sciences General pharmacology Humans Immunoglobulin Fragments - chemistry Immunoglobulin Fragments - metabolism Immunoglobulin Fragments - pharmacology Medical sciences Pharmaceutical Preparations - chemistry Pharmaceutical Preparations - metabolism Pharmaceutical technology. Pharmaceutical industry Pharmacology. Drug treatments
Title	Antibody Pharmacokinetics and Pharmacodynamics
URI	https://dx.doi.org/10.1002/jps.20178 https://api.istex.fr/ark:/67375/WNG-7TDQ2C40-5/fulltext.pdf https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fjps.20178 https://www.ncbi.nlm.nih.gov/pubmed/15389672 https://www.proquest.com/docview/66938859
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