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 language | English (US) |
|---|---|
| Pages (from-to) | 486-493 |
| Number of pages | 8 |
| Journal | American Journal of Clinical Pathology |
| Volume | 69 |
| Issue number | 5 |
| State | Published - 1978 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Pathology and Forensic Medicine
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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 journal › Article
}
TY - JOUR
T1 - The nature of the receptor for complement (C3b) in the human renal glomerulus
AU - Carlo, J. R.
AU - Nagle, Raymond B
AU - Shin, M. L.
PY - 1978
Y1 - 1978
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0018192379&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0018192379&partnerID=8YFLogxK
M3 - Article
C2 - 655127
AN - SCOPUS:0018192379
VL - 69
SP - 486
EP - 493
JO - American Journal of Clinical Pathology
JF - American Journal of Clinical Pathology
SN - 0002-9173
IS - 5
ER -