The nature of the receptor for complement (C3b) in the human renal glomerulus

J. R. Carlo, Raymond B Nagle, M. L. Shin

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

The physicochemical nature of the human glomerular complement receptor was studied. Receptor activity was measured by determining the avidity of glomeruli of normal human renal tissue for fluorescein-labeled bacteria (S. typhi) coated with C3b. Maximal binding of C3b-coated bacteria to normal human glomeruli took place in phosphate-saline buffers of pH 6.5 and 0.08 to 0.15 μ ionic strength. Pretreatment of renal tissue with neuraminidase enhanced receptor activity. On the other hand, binding of C3b-coated bacteria to the glomeruli was diminished by pretreatment of the tissue with proteolytic enzymes, phospholipase C and certain lipid solvents. The binding of C3b-coated bacteria to the glomeruli was also diminished by pretreatment of the tissue with fluid-phase C3b, or by pretreatment of the bacteria with C3b inactivator. Normal human serum and purified fluid-phase C3 or the absence of magnesium and calcium ions had little effect on glomerular complement receptor activity.

Original languageEnglish (US)
Pages (from-to)486-493
Number of pages8
JournalAmerican Journal of Clinical Pathology
Volume69
Issue number5
StatePublished - 1978
Externally publishedYes

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Complement C3b
Bacteria
Kidney
Complement Receptors
Complement Factor I
Neuraminidase
Type C Phospholipases
Fluorescein
Osmolar Concentration
Magnesium
Buffers
Peptide Hydrolases
Phosphates
Ions
Calcium
Lipids
Serum

ASJC Scopus subject areas

  • Pathology and Forensic Medicine

Cite this

The nature of the receptor for complement (C3b) in the human renal glomerulus. / Carlo, J. R.; Nagle, Raymond B; Shin, M. L.

In: American Journal of Clinical Pathology, Vol. 69, No. 5, 1978, p. 486-493.

Research output: Contribution to journalArticle

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