Document Detail


Comparison of blocking effects of monoclonal antibodies anti-MO1-alpha and anti-LFA1-alpha on human neutrophil functions.
MedLine Citation:
PMID:  2958406     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In order to analyse the role of LFA1 and MO1 on neutrophil functions, the blocking effects of two monoclonal antibodies (MAb), one (anti-MO1) recognizing an epitope of the MO1-alpha chain and the other (25.31) an epitope of the LFA1-alpha chain, were measured. Adherence of 51Cr-labelled control neutrophils was 66 + 8% (mean +/- 1 SD) on plastic nuclon plates; this figure decreased to 33 +/- 5% and 23 +/- 6% of control adherence when the neutrophils had been pretreated with anti-LFA1-alpha (anti-alpha L) and anti-MO1-alpha (anti-alpha M), respectively. On another support (plastic culture chambers), 84 +/- 6% of control neutrophils adhered and the adherence of neutrophils pretreated with anti-alpha L or anti-alpha M was 10% and 43% of the control figure, respectively. These results show that adherence of neutrophils is dependent upon the plastic used. Moreover, inhibition of adhesion by the two MAbs was also dependent upon the support used for the assay, suggesting that MO1 and LFA1 may be surface proteins with different specificities. Both antigens capped upon adhesion, while they were randomly distributed in resting neutrophils. Anti-alpha L inhibited (congruent to 50%) locomotion more than did anti-alpha M (congruent to 25%), without altering chemoattractant-induced shape changes. These results suggest that the two MAbs inhibit chemokinesis but not chemotaxis. Many other adherence-associated functions, such as ingestion of opsonized Klebsiella pneumoniae, and cytotoxicity towards K/562 cells were decreased more by anti-alpha L than by anti-alpha M. In contrast, chemiluminescence and iodination induced by opsonized zymosan were inhibited more by anti-alpha M than by anti-alpha L. Degranulation induced by zymosan or opsonized zymosan was altered by anti-alpha M only, and this alteration involved azurophilic and not specific granules. Chemiluminescence induced by phorbol myristate acetate was inhibited to a greater extent by anti-alpha M than by anti-alpha L, while degranulation induced by phorbol myristate acetate was not altered by either of the two Mabs.
Authors:
T Pham Huu; S Chollet-Martin; A Perianin; C Marquetty; P Sourbier; C Babin-Chevaye; D Olive; M A Gougerot-Pocidalo; P Debre; J Hakim
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  Immunology     Volume:  62     ISSN:  0019-2805     ISO Abbreviation:  Immunology     Publication Date:  1987 Sep 
Date Detail:
Created Date:  1987-10-30     Completed Date:  1987-10-30     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0374672     Medline TA:  Immunology     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  61-7     Citation Subset:  IM    
Affiliation:
Inserm U. 294, CHU Xavier Bichat, Université Paris, France.
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MeSH Terms
Descriptor/Qualifier:
Adult
Antibodies, Monoclonal / immunology
Antigens, Surface / immunology*
Binding, Competitive
Cell Adhesion
Cell Movement
Cytotoxicity, Immunologic
Humans
Lymphocyte Function-Associated Antigen-1
Neutrophils / immunology*,  physiology
Phagocytosis
Receptors, Complement / immunology*
Receptors, Complement 3b
Chemical
Reg. No./Substance:
0/Antibodies, Monoclonal; 0/Antigens, Surface; 0/Lymphocyte Function-Associated Antigen-1; 0/Receptors, Complement; 0/Receptors, Complement 3b
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