Document Detail

Recombinant therapeutic monoclonal antibodies: mechanisms of action in relation to structural and functional duality.
MedLine Citation:
PMID:  17716905     Owner:  NLM     Status:  MEDLINE    
Naked therapeutic recombinant monoclonal antibodies (mAbs) are bifunctional molecules. On the one hand, they recognize their antigen through the variable regions of the antigen binding portion (Fab). The recombinant mAb binding to a soluble or a membrane antigen may interfere with one or several functions of this antigen, leading to the therapeutic effect. On the other hand, since their crystalisable portion (Fc) is humanized (usually IgG1), they interact efficiently with human Fc-binding molecules, such as C1q and receptors for the Fc portion of IgG (FcgammaR). Thus, they initiate the classical pathway of complement and activate FcgammaR-expressing cells. The recruitment of these patient immune effector functions is essential in the therapeutic effect of several recombinant mAbs used in oncology. The aim of this review is to describe the main mechanisms of action of recombinant mAbs in relation to this structural and functional duality.
Nicolas Congy-Jolivet; Alicia Probst; Hervé Watier; Gilles Thibault
Related Documents :
1688565 - Stimulation of cd5 enhances signal transduction by the t cell antigen receptor.
16462125 - Cell surface expression of a chimeric protein containing mouse immunoglobulin g1 fc dom...
605365 - Interaction between a synthetic polypeptide, tigal, and fc receptors on non-bursa-deriv...
354125 - Mechanisms of immunoregulation. immunoregulation by antibody and antigen-antibody compl...
2424935 - Reactivity of t lymphotropic retrovirus antibody (12/1-2) in man: comparison of epiderm...
20885325 - Mature wines are better: cdc as the leading method to define highly sensitized patients.
Publication Detail:
Type:  Evaluation Studies; Journal Article; Review     Date:  2007-08-22
Journal Detail:
Title:  Critical reviews in oncology/hematology     Volume:  64     ISSN:  1040-8428     ISO Abbreviation:  Crit. Rev. Oncol. Hematol.     Publication Date:  2007 Dec 
Date Detail:
Created Date:  2007-11-07     Completed Date:  2008-02-15     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8916049     Medline TA:  Crit Rev Oncol Hematol     Country:  Ireland    
Other Details:
Languages:  eng     Pagination:  226-33     Citation Subset:  IM    
Université François Rabelais de Tours, EA 3853 Immuno-Pharmaco-Génétique des Anticorps thérapeutiques, 10 Boulevard Tonnellé, 37032 Tours Cedex, France.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Antibodies, Monoclonal / chemistry*,  physiology,  therapeutic use*
Immunoglobulin Fab Fragments / chemistry,  physiology
Immunoglobulin Fc Fragments / chemistry,  physiology
Models, Biological
Neoplasms / therapy*
Recombinant Proteins / chemistry*,  therapeutic use*
Structure-Activity Relationship
Reg. No./Substance:
0/Antibodies, Monoclonal; 0/Immunoglobulin Fab Fragments; 0/Immunoglobulin Fc Fragments; 0/Recombinant Proteins
Comment In:
Crit Rev Oncol Hematol. 2007 Dec;64(3):208-9   [PMID:  17986426 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Photobiological effects of UVA and UVB light in zebrafish embryos: evidence for a competent photorep...
Next Document:  Production of IL-6, in contrast to other cytokines and chemokines, in macrophage innate immune respo...