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PMID: 1798669 Published · ppublish English Comparative Study Journal Article

Interspecies scaling of clearance and volume of distribution data for five therapeutic proteins.

Pharmaceutical research ·Vol. 8 ·No. 11 ·1991-11-00 ·Pages 1351-9

Mordenti J, Chen SA, Moore JA, Ferraiolo BL, Green JD

Abstract

The clearance and volume of distribution of five human proteins (recombinant CD4, CD4 immunoglobulin G, growth hormone, tissue-plasminogen activator, and relaxin) in humans and laboratory animals were analyzed as a function of body weight using allometric scaling techniques. These proteins cover a 16-fold range of molecular weight (6 to 98 kD), are produced by recombinant or synthetic methods, and may be cleared by different mechanisms. The analyses revealed that the clearance and volume data for each protein were satisfactorily described by an allometric equation (Y = a Wb). The allometric exponent (b) for clearance (ml/min) ranged from 0.65 to 0.84, the allometric exponent for the initial volume of distribution (ml) ranged from 0.83 to 1.05, and the allometric exponent for the volume of distribution at steady state (ml) ranged from 0.84 to 1.02. Exponent values from 0.6 to 0.8 for clearance and 0.8 to 1.0 for volumes are frequently cited for small molecules and are expected based on empirical interspecies relationships. When the preclinical data were analyzed separately, the preclinical allometric relationships were usually predictive of the human results. These findings indicate that the clearance and volume of distribution of select biomacromolecules follow well-defined, size-related physiologic relationships, and preclinical pharmacokinetic studies provide reasonable estimates of human disposition. Employing this methodology during the early phases of drug development may provide a more rational basis for dose selection in the clinical environment.

MeSH Terms
Animals CD4 Antigens/metabolism Growth Hormone/pharmacokinetics Humans Immunoglobulin G/metabolism Macaca fascicularis Macaca mulatta Mice Proteins/administration & dosage,pharmacokinetics Rabbits Rats Recombinant Proteins/pharmacokinetics Relaxin/pharmacokinetics Species Specificity Tissue Plasminogen Activator/pharmacokinetics
Chemicals
CD4 Antigens Immunoglobulin G Proteins Recombinant Proteins Relaxin Growth Hormone Tissue Plasminogen Activator
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Mordenti J
Department of Pharmacokinetics, Genentech, Inc., South San Francisco, California 94080.
Chen S A
Moore J A
Ferraiolo B L
Green J D
References (39)
39 references, click to expand
  1. The CD4 antigen: physiological ligand and HIV receptor.
    Cell. 1988 Mar 11;52(5):631-3 PMID: 2830988
  2. [Determination of the antiactivator activity in human and animal blood plasma using tissue plasminogen activator].
    Vopr Med Khim. 1983 Sep-Oct;29(5):112-4 PMID: 6417906
  3. The pharmacokinetics and pharmacodynamics of a human relaxin in the mouse pubic symphysis bioassay.
    Endocrinology. 1989 Dec;125(6):2922-6 PMID: 2583048
  4. Dose-dependent pharmacokinetics of recombinant tissue-type plasminogen activator in anesthetized dogs following intravenous infusion.
    Drug Metab Dispos. 1988 Mar-Apr;16(2):201-6 PMID: 2898333
  5. Biological properties of a CD4 immunoadhesin.
    Nature. 1990 Apr 12;344(6267):667-70 PMID: 1970124
  6. Characterization studies of human tissue-type plasminogen activator produced by recombinant DNA technology.
    Cold Spring Harb Symp Quant Biol. 1986;51 Pt 1:551-62 PMID: 2953546
  7. T-cell development. Accessories or coreceptors?
    Nature. 1988 Sep 15;335(6187):208-10 PMID: 3261842
  8. The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain.
    Cell. 1986 Nov 7;47(3):333-48 PMID: 3094962
  9. Interspecies pharmacokinetic scaling and the evolutionary-comparative paradigm.
    Drug Metab Rev. 1984;15(5-6):1071-121 PMID: 6396053
  10. The Thrombolysis in Myocardial Infarction (TIMI) trial. Phase I findings.
    N Engl J Med. 1985 Apr 4;312(14 ):932-6 PMID: 4038784
  11. Pharmacokinetics and systemic effects of tissue-type plasminogen activator in normal subjects.
    Clin Pharmacol Ther. 1989 Aug;46(2):155-62 PMID: 2503283
  12. Equivalent potency and pharmacokinetics of recombinant human growth hormones with or without an N-terminal methionine.
    Endocrinology. 1988 Jun;122(6):2920-6 PMID: 3371267
  13. Renal extraction, filtration, absorption, and catabolism of growth hormone.
    Am J Physiol. 1977 Sep;233(3):F185-96 PMID: 910912
  14. The influence of carbohydrate structure on the clearance of recombinant tissue-type plasminogen activator.
    Thromb Haemost. 1988 Oct 31;60(2):255-61 PMID: 2851193
  15. Characterization of a soluble form of human CD4. Peptide analyses confirm the expected amino acid sequence, identify glycosylation sites and demonstrate the presence of three disulfide bonds.
    Eur J Biochem. 1990 Mar 10;188(2):291-300 PMID: 2318210
  16. Interspecies scaling, allometry, physiological time, and the ground plan of pharmacokinetics.
    J Pharmacokinet Biopharm. 1982 Apr;10(2):201-27 PMID: 7120049
  17. Nonlinear pharmacokinetics of tissue-type plasminogen activator in three animal species and isolated perfused rat liver.
    J Pharmacol Exp Ther. 1990 Oct;255(1):318-24 PMID: 2120422
  18. The safety and pharmacokinetics of recombinant soluble CD4 (rCD4) in subjects with the acquired immunodeficiency syndrome (AIDS) and AIDS-related complex. A phase 1 study.
    Ann Intern Med. 1990 Feb 15;112(4):254-61 PMID: 2297204
  19. Purification and characterization of a melanoma cell plasminogen activator.
    Eur J Biochem. 1983 May 16;132(3):681-6 PMID: 6682760
  20. Carbohydrate structures of recombinant soluble human CD4 expressed in Chinese hamster ovary cells.
    Biochemistry. 1991 Mar 5;30(9):2395-406 PMID: 2001369
  21. Designing CD4 immunoadhesins for AIDS therapy.
    Nature. 1989 Feb 9;337(6207):525-31 PMID: 2536900
  22. A specific growth hormone-binding protein in human plasma: initial characterization.
    J Clin Endocrinol Metab. 1986 Jan;62(1):134-41 PMID: 3940261
  23. Characterization of in vitro inhibition of human immunodeficiency virus by purified recombinant CD4.
    J Virol. 1989 Oct;63(10):4370-5 PMID: 2550671
  24. Isolation, identification and pharmacokinetic properties of human tissue-type plasminogen activator species: possible localisation of a clearance recognition site.
    Thromb Haemost. 1988 Jun 16;59(3):523-8 PMID: 3142086
  25. Plasminogen activator inhibitors.
    Blood. 1987 Feb;69(2):381-7 PMID: 3099859
  26. Cellular catabolism of recombinant tissue-type plasminogen activator. Identification and characterization of a novel high affinity uptake system on rat hepatocytes.
    J Biol Chem. 1987 Jun 25;262(18):8716-20 PMID: 2439503
  27. The circulating growth hormone (GH)-binding protein complex: a major constituent of plasma GH in man.
    Endocrinology. 1988 Mar;122(3):976-84 PMID: 3342762
  28. Blocking of HIV-1 infectivity by a soluble, secreted form of the CD4 antigen.
    Science. 1987 Dec 18;238(4834):1704-7 PMID: 3500514
  29. The effect of circulating growth hormone-binding protein on metabolic clearance, distribution, and degradation of human growth hormone.
    J Clin Endocrinol Metab. 1987 Apr;64(4):657-60 PMID: 3818897
  30. Disposition of a novel recombinant tissue plasminogen activator, delta 2-89 TPA, in mice.
    Thromb Res. 1988 Apr 1;50(1):33-41 PMID: 3135637
  31. Interspecies variation in liver weight, hepatic blood flow, and antipyrine intrinsic clearance: extrapolation of data to benzodiazepines and phenytoin.
    J Pharmacokinet Biopharm. 1980 Apr;8(2):165-76 PMID: 6107379
  32. Cloning and expression of human tissue-type plasminogen activator cDNA in E. coli.
    Nature. 1983 Jan 20;301(5897):214-21 PMID: 6337343
  33. Randomised trial of intravenous recombinant tissue-type plasminogen activator versus intravenous streptokinase in acute myocardial infarction. Report from the European Cooperative Study Group for Recombinant Tissue-type Plasminogen Activator.
    Lancet. 1985 Apr 13;1(8433):842-7 PMID: 2858711
  34. Coronary thrombolysis with recombinant human tissue-type plasminogen activator: a prospective, randomized, placebo-controlled trial.
    Circulation. 1984 Dec;70(6):1012-7 PMID: 6388898
  35. Structural characterization of a recombinant CD4-IgG hybrid molecule.
    Eur J Biochem. 1990 Dec 12;194(2):611-20 PMID: 2269286
  36. Acute coronary reocclusion after thrombolysis with recombinant human tissue-type plasminogen activator: prevention by a maintenance infusion.
    Circulation. 1986 Feb;73(2):347-52 PMID: 3080262
  37. The rabbit as a model for studies of fibrinolysis.
    Thromb Res. 1986 Aug 1;43(3):313-23 PMID: 3488605
  38. Identification and characterization of specific binding proteins for growth hormone in normal human sera.
    J Clin Invest. 1986 Jun;77(6):1817-23 PMID: 3711337
  39. Uptake and degradation of tissue plasminogen activator in rat liver.
    Thromb Haemost. 1988 Jun 16;59(3):474-9 PMID: 3142083
Article Info
Journal
Pharmaceutical research
Abbr.
Pharm Res
ISSN
0724-8741
Published
1991-11-00
Pages
1351-9
Language
English
Region
United States
NLM ID
8406521
Subset
IM
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