Anionization of an antigen promotes glomerular binding and immune complex formation

J. L. Barnes, M. J. Reznicek, R. A. Radnik, Manjeri A Venkatachalam

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Bovine serum albumin (BSA, pl 4.9) was maleylated to yield highly anionic MBSA (pl 3.0). Maleylation of BSA lead to an expansion of molecular size of native BSA from an effective molecular radius (EMR) of 37 Å to 57 Å for MBSA as assessed by gel filtration chromatography. MBSA, but not BSA, bound to peripheral capillary wall (PCW) and mesangium in vitro in frozen sections, and in vivo following i.v. injection (0.006 mg/g body wt), examined by immunofluorescence. When similarly injected rats or controls were given antibodies to either MBSA or BSA following injection of antigen, immune complexes were observed in glomeruli by immunofluorescence and EM only in MBSA injected rats. Deposits occurred in the mesangium and subendothelium in the PCW. In frozen sections, bound MBSA could be partially removed from tissue sections by high ionic strength buffer. Also, binding of MBSA was diminished by prior treatment of sections with synthetic polyanions. Maleylated bovine gamma-globulin and succinylated BSA showed identical binding patterns as described for MBSA, indicating that binding was not unique to the modified BSA molecule nor to the form of anionization. These results indicate that charge interactions between circulating highly anionic macromolecules and cationic domains within glomerular structures, are responsible, in part, for MBSA binding and subsequent localization of immune complexes. Furthermore, it is inferred that the selective binding of MBSA to glomeruli and formation of immune complexes occurred by a mechanism not related to difference in size between MBSA and BSA. These findings are different from conventionally understood charge interactions in glomerular immune complex formation.

Original languageEnglish (US)
Pages (from-to)156-163
Number of pages8
JournalKidney International
Volume34
Issue number2
StatePublished - 1988

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Antigen-Antibody Complex
Antigens
Frozen Sections
Fluorescent Antibody Technique
methylated bovine serum albumin
Injections
gamma-Globulins
Bovine Serum Albumin
Osmolar Concentration
Gel Chromatography
Buffers
Antibodies

ASJC Scopus subject areas

  • Nephrology

Cite this

Anionization of an antigen promotes glomerular binding and immune complex formation. / Barnes, J. L.; Reznicek, M. J.; Radnik, R. A.; Venkatachalam, Manjeri A.

In: Kidney International, Vol. 34, No. 2, 1988, p. 156-163.

Research output: Contribution to journalArticle

Barnes, J. L. ; Reznicek, M. J. ; Radnik, R. A. ; Venkatachalam, Manjeri A. / Anionization of an antigen promotes glomerular binding and immune complex formation. In: Kidney International. 1988 ; Vol. 34, No. 2. pp. 156-163.
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