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J. Sorvillo, I. Gigli, E. Pearlstein (1986)
The effect of fibronectin on the processing of C1q- and C3b/bi-coated immune complexes by peripheral blood monocytes.Journal of immunology, 136 3
D. Bobak, M. Frank, A. Tenner (1988)
Clq acts synergistically with phorbol dibutyrate to activate CR1‐mediated phagocytosis by human mononuclear phagocytesEuropean Journal of Immunology, 18
Ronald Nepomuceno, A. Tenner (1998)
C1qRP, the C1q receptor that enhances phagocytosis, is detected specifically in human cells of myeloid lineage, endothelial cells, and platelets.Journal of immunology, 160 4
Marcella Kuhlman, Keith Joiner (1989)
The human mannose-binding protein functions as an opsoninThe Journal of Experimental Medicine, 169
(1998)
C 1 qRp , the C 1 q receptor that enhances phagocytosis , is detected specifically in human cells of myeloid lineage , endothelial cells , and platelets
E. Guan, W. Burgess, S. Robinson, E. Goodman, K. McTigue, A. Tenner (1991)
Phagocytic cell molecules that bind the collagen-like region of C1q. Involvement in the C1q-mediated enhancement of phagocytosis.The Journal of biological chemistry, 266 30
A. Tenner, N. Cooper (1981)
Identification of types of cells in human peripheral blood that bind C1q.Journal of immunology, 126 3
B. Ghebrehiwet, R. Kew, Barry Gruber, M. Marchese, E. Peerschke, Kenneth Reid (1995)
Murine mast cells express two types of C1q receptors that are involved in the induction of chemotaxis and chemokinesis.Journal of immunology, 155 5
M. Geertsma, P. Nibbering, H. Haagsman, M. Daha, R. Furth (1994)
Binding of surfactant protein A to C1q receptors mediates phagocytosis of Staphylococcus aureus by monocytes.The American journal of physiology, 267 5 Pt 1
E. Guan, S. Robinson, E. Goodman, A. Tenner (1994)
Cell-surface protein identified on phagocytic cells modulates the C1q-mediated enhancement of phagocytosis.Journal of immunology, 152 8
C. Lozada, R. Levin, M. Huie, R. Hirschhorn, D. Naime, M. Whitlow, P. Recht, B. Golden, B. Cronstein (1995)
Identification of C1q as the heat-labile serum cofactor required for immune complexes to stimulate endothelial expression of the adhesion molecules E-selectin and intercellular and vascular cell adhesion molecules 1.Proceedings of the National Academy of Sciences of the United States of America, 92 18
D. Bobak, T. Gaither, M. Frank, A. Tenner (1987)
Modulation of FcR function by complement: subcomponent C1q enhances the phagocytosis of IgG-opsonized targets by human monocytes and culture-derived macrophages.Journal of immunology, 138 4
E. Peerschke, K. Reid, B. Ghebrehiwet (1994)
Identification of a novel 33-kDa C1q-binding site on human blood platelets.Journal of immunology, 152 12
Paul Eggleton, B. Ghebrehiwet, K. Sastry, JP Coburn, Ken Zaner, Kenneth Reid, Alfred Tauber (1995)
Identification of a gC1q-binding protein (gC1q-R) on the surface of human neutrophils. Subcellular localization and binding properties in comparison with the cC1q-R.The Journal of clinical investigation, 95 4
E. Peerschke, B. Ghebrehiwet (1988)
Identification and partial characterization of human platelet C1q binding sites.Journal of immunology, 141 10
B. Ghebrehiwet, L. Silvestri, C. McDevitt (1984)
Identification of the Raji cell membrane-derived C1q inhibitor as a receptor for human C1q. Purification and immunochemical characterizationThe Journal of Experimental Medicine, 160
R. Nepomuceno, A. Henschen-Edman, W. Burgess, A. Tenner (1997)
cDNA cloning and primary structure analysis of C1qR(P), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro.Immunity, 6 2
M. Daha, N. Klar, R. Hoekzema, L. Es (1990)
Enhanced Ig production by human peripheral lymphocytes induced by aggregated C1q.Journal of immunology, 144 4
A. Feinberg, B. Vogelstein (1983)
A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity.Analytical biochemistry, 132 1
R. Malhotra, A. Willis, J. Jensenius, J. Jackson, Robert Sim (1993)
Structure and homology of human C1q receptor (collectin receptor).Immunology, 78 3
J. Dedio, Willi Jahnen-Dechent, Michael Bachmann, Werner Müller-Esterl (1998)
The multiligand-binding protein gC1qR, putative C1q receptor, is a mitochondrial protein.Journal of immunology, 160 7
G. Habicht, G. Beck, B. Ghebrehiwet (1987)
C1q inhibits the expression of B lymphoblastoid cell line interleukin 1 (IL 1).Journal of immunology, 138 8
E. Brown (1986)
The Role of Extracellular Matrix Proteins in the Control of PhagocytosisJournal of Leukocyte Biology, 39
A. Tenner, N. Cooper (1982)
Stimulation of a human polymorphonuclear leukocyte oxidative response by the C1q subunit of the first complement component.Journal of immunology, 128 6
M. Daha, A. Miltenburg, P. Hiemstra, N. Klar‐Mohamad, L. Es, V. Hinsbergh (1988)
The complement subcomponent C1q mediates binding of immune complexes and aggregates to endothelial cells in vitroEuropean Journal of Immunology, 18
A. Tenner, S. Robinson, R. Ezekowitz (1995)
Mannose binding protein (MBP) enhances mononuclear phagocyte function via a receptor that contains the 126,000 M(r) component of the C1q receptor.Immunity, 3 4
J. Pikaar, W. Voorhout, L.M.G. Golde, J. Verhoef, J. Strijp, J. Iwaarden (1995)
Opsonic activities of surfactant proteins A and D in phagocytosis of gram-negative bacteria by alveolar macrophages.The Journal of infectious diseases, 172 2
(1997)
cDNA cloning and primary structure analysis
Stephen Mount (1982)
A catalogue of splice junction sequences.Nucleic acids research, 10 2
(1986)
Molecular Cloning: A Laboratory Manual,2nd ed. (Cold Spring Harbor, N.Y.: Cold Spring Harbor Laboratory
Andrea, J., Tenner, Susan, Robinson, Jenny Borcheltq, Jo Wright (1989)
Human pulmonary surfactant protein (SP-A), a protein structurally homologous to C1q, can enhance FcR- and CR1-mediated phagocytosis.The Journal of biological chemistry, 264 23
Binding of C1q to cell surfaces has been shown to mediate a number of biological activities including enhancement of phagocytosis and stimulation of superoxide production. Several C1q binding proteins have been proposed as candidate receptors for these functions. The 126-kDa human C1q membrane receptor, termed C1qRp, has recently been cloned. This molecule is believed to play a role in the enhancement of phagocytosis in monocytes and macrophages, and its expression has been shown to be restricted to cells of the myeloid lineage, endothelial cells, and platelets. Here we report the isolation and genomic characterization of the murine homolog of C1qRp. Degenerate oligonucleotide primers based on the published human sequence were used to amplify a region of the murine homolog spanning from the carbohydrate recognition domain to the fourth epidermal growth factor (EGF) domain. This fragment was used as a probe to isolate the murine gene from a 129/Sv genomic λ library. The predicted primary protein sequence displayed 68.1% identity with the human homolog. All the major structural domains were conserved between the two molecules. The coding sequence of the murine gene was contained within two exons separated by a small intron of approximately 250 bp. The structure of the human gene was found to be similar, with the position of the intron conserved. Cloning of the murine C1qRp will facilitate further investigation of the physiological function of this molecule.
Mammalian Genome – Springer Journals
Published: Aug 1, 1999
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