The JI
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     
 

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sorensen, V.
Right arrow Articles by Sandlie, I.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sorensen, V.
Right arrow Articles by Sandlie, I.

The Journal of Immunology, Vol 156, Issue 8 2858-2865, Copyright © 1996 by American Association of Immunologists

ARTICLES

Effect of the IgM and IgA secretory tailpieces on polymerization and secretion of IgM and IgG

V Sorensen, IB Rasmussen, L Norderhaug, I Natvig, TE Michaelsen and I Sandlie
Department of Biology, Division of Molecular Cell Biology, University of Oslo, Norway.

Pentameric IgM and dimeric IgA both contain disulfide bonds between cysteines located in the secretory tailpieces of the heavy chains. To compare the influences of the mu and alpha tailpieces on the polymeric structure, we have replaced amino acids in the tailpiece of the human mu-chain with amino acids found in the corresponding positions in the human alpha tailpiece. We show that an IgM with an alpha tailpiece (IgM L561H, Y562V, L566V, S569A, D570E, T571V, and A572D) as well as IgM L561H, Y562V, and IgM A572D have a size distribution similar to that of wild-type IgM. However, one IgM mutant with a mu/alpha hybrid tailpiece (IgM L566V, S569A, D570E, T571V, and A572D) is secreted as a mixture of mainly hexamers, pentamers, tetramers, and dimers. The tetramers and dimers are specifically formed and secreted at the expense of pentamers and hexamers; no alterations in polymerization or secretion rates were observed. We have also incorporated the mu, alpha, and hybrid mu/alpha tailpieces to a human IgG3 or IgGL309C mutant. The IgG-tailpiece mutants are poorly secreted, but the secreted fractions contain multimeric molecules. Each of the mutants that contain both the L309C mutation and a secretory tailpiece forms mainly hexamers; however, small differences in polymer distribution exist for the different tailpieces. Comparison of the influence of different tailpieces on IgM and IgG polymeric structures suggests that the function of a specific tailpiece is dependent on other parts of the heavy chain, which can vary for different isotypes.


This article has been cited by other articles:


Home page
 J. Immunol.Home page
A. Ghumra, J.-P. Semblat, R. S. McIntosh, A. Raza, I. B. Rasmussen, R. Braathen, F.-E. Johansen, I. Sandlie, P. K. Mongini, J. A. Rowe, et al.
Identification of Residues in the C{micro}4 Domain of Polymeric IgM Essential for Interaction with Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1)
J. Immunol., August 1, 2008; 181(3): 1988 - 2000.
[Abstract] [Full Text] [PDF]

Home page
 Int ImmunolHome page
T. Shimizu, Y. Kozono, H. Kozono, M. Oda, and T. Azuma
Affinity maturation of secreted IgM pentamers on B cells
Int. Immunol., May 1, 2004; 16(5): 675 - 684.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
G. A. Loset, K. H. Roux, P. Zhu, T. E. Michaelsen, and I. Sandlie
Differential Segmental Flexibility and Reach Dictate the Antigen Binding Mode of Chimeric IgD and IgM: Implications for the Function of the B Cell Receptor
J. Immunol., March 1, 2004; 172(5): 2925 - 2934.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Braathen, V. Sorensen, P. Brandtzaeg, I. Sandlie, and F.-E. Johansen
The Carboxyl-terminal Domains of IgA and IgM Direct Isotype-specific Polymerization and Interaction with the Polymeric Immunoglobulin Receptor
J. Biol. Chem., November 1, 2002; 277(45): 42755 - 42762.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
F.-E. Johansen, R. Braathen, and P. Brandtzaeg
The J Chain Is Essential for Polymeric Ig Receptor-Mediated Epithelial Transport of IgA
J. Immunol., November 1, 2001; 167(9): 5185 - 5192.
[Abstract] [Full Text] [PDF]

Home page
 Int ImmunolHome page
V. Sorensen, I. B. Rasmussen, V. Sundvold, T. E. Michaelsen, and I. Sandlie
Structural requirements for incorporation of J chain into human IgM and IgA
Int. Immunol., January 1, 2000; 12(1): 19 - 27.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. M. Yoo, M. J. Coloma, K. R. Trinh, T. Q. Nguyen, L.-U. C. Vuong, S. L. Morrison, and K. R. Chintalacharuvu
Structural Requirements for Polymeric Immunoglobulin Assembly and Association with J Chain
J. Biol. Chem., November 19, 1999; 274(47): 33771 - 33777.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
V. Sorensen, V. Sundvold, T. E. Michaelsen, and I. Sandlie
Polymerization of IgA and IgM: Roles of Cys309/Cys414 and the Secretory Tailpiece
J. Immunol., March 15, 1999; 162(6): 3448 - 3455.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
K. H. Roux, L. Strelets, O. H. Brekke, I. Sandlie, and T. E. Michaelsen
Comparisons of the Ability of Human IgG3 Hinge Mutants, IgM, IgE, and IgA2, to Form Small Immune Complexes: A Role for Flexibility and Geometry
J. Immunol., October 15, 1998; 161(8): 4083 - 4090.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
E. J. Wiersma, C. Collins, S. Fazel, and M. J. Shulman
Structural and Functional Analysis of J Chain-Deficient IgM
J. Immunol., June 15, 1998; 160(12): 5979 - 5989.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1996 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1996 by The American Association of Immunologists, Inc. All rights reserved.