The mouse anaphylatoxin C3a receptor: Molecular cloning, genomic organization, and functional expression

Journal of Immunology

Volumn 158, Issue 11, 1997, Pages 5277-5282

  Tornetta, Mark A ^a   Foley, James J ^a   Sarau, Henry M ^a   Ames, Robert S ^a,b  

^a Smith Kline Beecham Pharmaceutical ^*  (United States)

^b GLAXOSMITHKLINE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT C3A RECEPTOR; COMPLEMENT RECEPTOR; MEMBRANE PROTEIN;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; C57BL MOUSE; CHROMOSOME MAP; GENETICS; GENOME; HUMAN; MOLECULAR CLONING; MOLECULAR GENETICS; MOUSE; NUCLEOTIDE SEQUENCE; RAT; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CHROMOSOME MAPPING; CLONING, MOLECULAR; GENOME; HUMANS; MEMBRANE PROTEINS; MICE; MICE, INBRED C57BL; MOLECULAR SEQUENCE DATA; RATS; RECEPTORS, COMPLEMENT; SEQUENCE ALIGNMENT;

EID: 0031159817     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (7)

1. Hugli, T. E. 1981. The structural basis for anaphylatoxin and chemotactic functions of C3a, C4a, and C5a. Crit. Rev. Immunol. 1:321.
2. Hugli, T. E. 1984. Structure and function of the anaphylatoxins. Springer Semin. Immunopathol. 7:193.
3. Hugli, T. E. 1986. Biochemistry and biology of anaphylatoxins. [Published erratum appears in 1987 Complement 4:119.] Complement 3:111.
4. Gerard, C., and N. P. Gerard. 1994. C5a anaphylatoxin and its seven transmembrane-segment receptor. Annu. Rev. Immunol. 12:775.
5. Hugli, T. E. 1990. Structure and function of C3a anaphylatoxin. Curr. Top. Microbiol. Immunol. 153:181.
6. Daffern, P. J., P. H. Pfeifer, J. A. Ember, and T. E. Hugli. 1995. C3a is a chemotaxin for human eosinophils but not for neutrophils. I. C3a stimulation of neutrophils is secondary to eosinophil activation. J. Exp. Med. 181:2119.
7. Nilsson, G., M. Johnell, C. H. Hammer, H. L. Tiffany, K. Nilsson, D. D. Metcalfe, A. Siegbahn, and P. M. Murphy. 1996. C3a and C5a are chemotaxins for human mast cells and act through distinct receptors via a pertussis-toxin-sensitive signaltransduction pathway. J. Immunol. 157:1693.