DOI: 10.4049/jimmunol.123.2.523. Complement Receptor Binding of C3b-Coated Cells Treated with C3b Inactivator, β1H Globulin and Trypsin

Complement Receptor Binding of C3b-Coated Cells Treated with C3b Inactivator, β1H Globulin and Trypsin

10.4049/jimmunol.123.2.523

Crossref journal-article

Oxford University Press (OUP)

The Journal of Immunology (286)

Abstract

Abstract Treatment of 125I-C3b bound to EAC1423b with C3b inactivator (C3bINA) and β1H globulin (β1H) cleaved the α-chain of C3b into 65,000- and 42,000-dalton fragments, both of which remained disulfide-bonded to the intact β-chain (C3bi). Subsequent treatment with trypsin (0.1 µg/ml) released 125I into the supernatant and yielded cells coated with a 33,000-dalton fragment of α-chain, presumably C3d. These results are in agreement with those obtained by others using fluid phase C3b. C3b-coated cells (EAC1423b) adhered to complement (C) receptors on human erythrocytes, glomeruli, and monocytes. C3bi-coated cells adhered to the receptors on glomeruli and monocytes, but not to those on human erythrocytes. C3d-coated cells adhered only to the monocyte receptors. The findings suggest that the glomerular C receptor recognizes portions of the C3 molecule different from those recognized by either the erythrocyte or monocyte receptors.

Bibliography

Carlo, J. R., Ruddy, S., Studer, E. J., & Conrad, D. H. (1979). Complement Receptor Binding of C3b-Coated Cells Treated with C3b Inactivator, Î²1H Globulin and Trypsin. The Journal of Immunology, 123(2), 523â528.

Authors 4

Jaime R Carlo (first)
Shaun Ruddy (additional)
Elaine J Studer (additional)
Daniel H Conrad (additional)

References 0 Referenced 63

None

Dates

Type	When
Created	2 years, 8 months ago (Dec. 30, 2022, 7:36 p.m.)
Deposited	5 months ago (March 31, 2025, 9:24 p.m.)
Indexed	5 months ago (March 31, 2025, 9:40 p.m.)
Issued	46 years, 1 month ago (Aug. 1, 1979)
Published	46 years, 1 month ago (Aug. 1, 1979)
Published Online	46 years, 1 month ago (Aug. 1, 1979)
Published Print	46 years, 1 month ago (Aug. 1, 1979)

Funders 0

None

BibTeX

@article{Carlo_1979, title={Complement Receptor Binding of C3b-Coated Cells Treated with C3b Inactivator, β1H Globulin and Trypsin}, volume={123}, ISSN={1550-6606}, url={http://dx.doi.org/10.4049/jimmunol.123.2.523}, DOI={10.4049/jimmunol.123.2.523}, number={2}, journal={The Journal of Immunology}, publisher={Oxford University Press (OUP)}, author={Carlo, Jaime R and Ruddy, Shaun and Studer, Elaine J and Conrad, Daniel H}, year={1979}, month=aug, pages={523–528} }

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  "abstract": "<jats:title>Abstract</jats:title>\n               <jats:p>Treatment of 125I-C3b bound to EAC1423b with C3b inactivator (C3bINA) and \u03b21H globulin (\u03b21H) cleaved the \u03b1-chain of C3b into 65,000- and 42,000-dalton fragments, both of which remained disulfide-bonded to the intact \u03b2-chain (C3bi). Subsequent treatment with trypsin (0.1 \u00b5g/ml) released 125I into the supernatant and yielded cells coated with a 33,000-dalton fragment of \u03b1-chain, presumably C3d. These results are in agreement with those obtained by others using fluid phase C3b. C3b-coated cells (EAC1423b) adhered to complement (C) receptors on human erythrocytes, glomeruli, and monocytes. C3bi-coated cells adhered to the receptors on glomeruli and monocytes, but not to those on human erythrocytes. C3d-coated cells adhered only to the monocyte receptors. The findings suggest that the glomerular C receptor recognizes portions of the C3 molecule different from those recognized by either the erythrocyte or monocyte receptors.</jats:p>",
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