Demonstration of a C1q receptor on the surface of human endothelial cells. 1981

B S Andrews, and M Shadforth, and P Cunningham, and J S Davis

A receptor for C1q on the surface of human endothelial cells has been demonstrated. This receptor is present on the surface of viable cultured endothelial cells derived from human umbilical veins, and C1q binding can also be demonstrated to the endothelial lining cells of human umbilical artery and vein on frozen tissue sections. Receptors for the complement components C3b and C3d were not detected on tissue sections or endothelial cells in suspension. Endothelial cell C1q receptors are discussed in relationship to possible immune complex localization in vivo.

UI MeSH Term Description Entries
D007141 Immunoglobulin Fc Fragments Crystallizable fragments composed of the carboxy-terminal halves of both IMMUNOGLOBULIN HEAVY CHAINS linked to each other by disulfide bonds. Fc fragments contain the carboxy-terminal parts of the heavy chain constant regions that are responsible for the effector functions of an immunoglobulin (COMPLEMENT fixation, binding to the cell membrane via FC RECEPTORS, and placental transport). This fragment can be obtained by digestion of immunoglobulins with the proteolytic enzyme PAPAIN. Fc Fragment,Fc Fragments,Fc Immunoglobulin,Fc Immunoglobulins,Ig Fc Fragments,Immunoglobulin Fc Fragment,Immunoglobulins, Fc,Immunoglobulins, Fc Fragment,Fc Fragment Immunoglobulins,Fc Fragment, Immunoglobulin,Fc Fragments, Ig,Fc Fragments, Immunoglobulin,Fragment Immunoglobulins, Fc,Fragment, Fc,Fragments, Ig Fc,Immunoglobulin, Fc
D011951 Receptors, Complement Molecules on the surface of some B-lymphocytes and macrophages, that recognize and combine with the C3b, C3d, C1q, and C4b components of complement. Complement Receptors,Complement Receptor,Complement Receptor Type 1,Receptor, Complement
D011961 Receptors, Fc Molecules found on the surface of some, but not all, B-lymphocytes, T-lymphocytes, and macrophages, which recognize and combine with the Fc (crystallizable) portion of immunoglobulin molecules. Fc Receptors,Fc Receptor,Receptor, Fc
D003166 Complement Activating Enzymes Enzymes that activate one or more COMPLEMENT PROTEINS in the complement system leading to the formation of the COMPLEMENT MEMBRANE ATTACK COMPLEX, an important response in host defense. They are enzymes in the various COMPLEMENT ACTIVATION pathways. Activating Enzymes, Complement,Enzymes, Complement Activating
D004727 Endothelium A layer of epithelium that lines the heart, blood vessels (ENDOTHELIUM, VASCULAR), lymph vessels (ENDOTHELIUM, LYMPHATIC), and the serous cavities of the body. Endotheliums
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D012397 Rosette Formation The in vitro formation of clusters consisting of a cell (usually a lymphocyte) surrounded by antigenic cells or antigen-bearing particles (usually erythrocytes, which may or may not be coated with antibody or antibody and complement). The rosette-forming cell may be an antibody-forming cell, a memory cell, a T-cell, a cell bearing surface cytophilic antibodies, or a monocyte possessing Fc receptors. Rosette formation can be used to identify specific populations of these cells. Immunocytoadherence,Formation, Rosette,Formations, Rosette,Immunocytoadherences,Rosette Formations
D014471 Umbilical Veins Venous vessels in the umbilical cord. They carry oxygenated, nutrient-rich blood from the mother to the FETUS via the PLACENTA. In humans, there is normally one umbilical vein. Umbilical Vein,Vein, Umbilical,Veins, Umbilical
D015922 Complement C1q A subcomponent of complement C1, composed of six copies of three polypeptide chains (A, B, and C), each encoded by a separate gene (C1QA; C1QB; C1QC). This complex is arranged in nine subunits (six disulfide-linked dimers of A and B, and three disulfide-linked homodimers of C). C1q has binding sites for antibodies (the heavy chain of IMMUNOGLOBULIN G or IMMUNOGLOBULIN M). The interaction of C1q and immunoglobulin activates the two proenzymes COMPLEMENT C1R and COMPLEMENT C1S, thus initiating the cascade of COMPLEMENT ACTIVATION via the CLASSICAL COMPLEMENT PATHWAY. C1q Complement,Complement 1q,Complement Component 1q,C1q, Complement,Complement, C1q,Component 1q, Complement

Related Publications

B S Andrews, and M Shadforth, and P Cunningham, and J S Davis
January 1986, Tissue & cell,
B S Andrews, and M Shadforth, and P Cunningham, and J S Davis
February 1993, Journal of leukocyte biology,
B S Andrews, and M Shadforth, and P Cunningham, and J S Davis
January 1993, Mediators of inflammation,
B S Andrews, and M Shadforth, and P Cunningham, and J S Davis
September 1990, Journal of immunology (Baltimore, Md. : 1950),
B S Andrews, and M Shadforth, and P Cunningham, and J S Davis
March 2001, Journal of immunology (Baltimore, Md. : 1950),
B S Andrews, and M Shadforth, and P Cunningham, and J S Davis
June 1984, Canadian journal of biochemistry and cell biology = Revue canadienne de biochimie et biologie cellulaire,
B S Andrews, and M Shadforth, and P Cunningham, and J S Davis
February 2007, Molecular immunology,
B S Andrews, and M Shadforth, and P Cunningham, and J S Davis
December 1997, Immunopharmacology,
B S Andrews, and M Shadforth, and P Cunningham, and J S Davis
July 1989, Behring Institute Mitteilungen,
B S Andrews, and M Shadforth, and P Cunningham, and J S Davis
February 1998, Journal of immunology (Baltimore, Md. : 1950),
Copied contents to your clipboard!