English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Human IgG1/IgG3 cryoglobulin suggesting lack of allelic exclusion

Mohanty, S., Weiner, S. M., Mentele, R., Vaith, P., Lottspeich, F., & Illges, H. (2003). Human IgG1/IgG3 cryoglobulin suggesting lack of allelic exclusion. Molecular Immunology, 39(16), 1003-1011.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : Mol. Immunol.

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Mohanty, S., Author
Weiner, S. M., Author
Mentele, R.1, Author           
Vaith, P., Author
Lottspeich, F.2, Author           
Illges, H., Author
Affiliations:
1External Organizations, ou_persistent22              
2Lottspeich, Friedrich / Protein Analysis, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565158              

Content

show
hide
Free keywords: cryoglobulinemia; membranoproliferative glonerulonephritis; proteinuria
 Abstract: Immunoglobulins undergoing cold-dependent precipitation are known as cryoglobulins. A type I cryoglobulin after Brouet et al. from serum of a patient with severe cutaneous vasculitis and membranoproliferative glomerulonephritis was purified by reversible temperature-dependent precipitation and analyzed using FPLC, Western blotting and peptide sequencing. The isolated cryoglobulin consisted of a single complex of a molecular weight of above 210 kDa observed under non-reducing conditions in SDS-polyacrylamide gel electrophoresis (PAGE). Under reducing conditions, this complex resolved into three bands, two of which were reminiscent of Ig heavy (HQ chains and one of Ig-light chains (LC). The FPLC-purified type I cryoglobulin showed reversible precipitation analyzed by spectrophotometry. Delineation of the peptides involved in complex formation by immunoblot analysis and peptide sequencing revealed IgG3-V(H)4/Igkappa-VkappaIII/JkappaII and IgG1/V(H)3 molecules with evidence of somatic mutation. Coomassie blue- staining suggested that molar amounts of the IgG3-heavy chain were much higher than that of the IgG1-heavy chain. Treatment with SDS and boiling did not disrupt the unusually high molecular weight Ig complex. Pre-treatment of the cryoglobulin in 6 M guadinium hydrochloride followed by gel filtration chromatography suggested covalent association of the IgG3, IgG1 and Igkappa molecules. Therefore, it might be that the cryoglobulin was produced by a single plasma B cell clone which passed immunological check-points in terms of B cell selection in the bone marrow in the absence of allelic exclusion, class switching and affinity maturation by somatic mutation. (C) 2003 Elsevier Science Ltd. All rights reserved.

Details

show
hide
Language(s): eng - English
 Dates: 2003-06
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 27748
ISI: 000183119800003
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Molecular Immunology
  Alternative Title : Mol. Immunol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 39 (16) Sequence Number: - Start / End Page: 1003 - 1011 Identifier: ISSN: 0161-5890