Abstract
The recognition subunit of C1, C1q, has emerged as an important player in various pathophysiologic conditions largely in part due to its ability to interact with pathogen-associated or cell surface expressed ligands and receptors. Identification and purification of these molecules is therefore of paramount importance if we are to procure valuable information with regards to the structure, function, and cell surface distribution. Since the interaction of C1q is better served when the receptors are purified from homologous species, we discuss here a simple guideline for the purification and characterization of the two C1q receptors, cC1qR (calreticulin) and gC1qR, from human cell lines.
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Abbreviations
- cC1q:
-
The collagen domain of C1q
- cC1qR:
-
Receptor for cC1q
- CRT:
-
Calreticulin another name for cC1qR
- gC1q:
-
The globular heads of C1q
- gC1qR:
-
Receptor for gC1q
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Acknowledgment
This work was supported in part by grants from the National Institutes of Health (R01 AI 060866 and R01 AI-084178).
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Ghebrehiwet, B., Peerschke, E.I.B. (2014). Purification of C1q Receptors and Functional Analysis. In: Gadjeva, M. (eds) The Complement System. Methods in Molecular Biology, vol 1100. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-724-2_26
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DOI: https://doi.org/10.1007/978-1-62703-724-2_26
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