Biomaterial Database

Binding of C-reactive protein to human polymorphonuclear leukocytes: evidence for association of binding sites with Fc receptors. 1986

H Müller, and J Fehr

The functional similarities between C-reactive protein (CRP) and IgG raised the question as to whether human phagocytes are stimulated by CRP in the same way as by binding of antigen-complexed or aggregated IgG to their Fc receptors. Studies with the use of highly purified 125I-labeled CRP showed specific and saturable binding to human polymorphonuclear leukocytes (PMN) with a KD of 10.5 +/- 5.7 X 10(-8) M only when carried out in heat-inactivated plasma. The number of specific binding sites per cell was estimated at 1 to 3 X 10(6). Competitive inhibition of CRP binding by antigen-complexed or aggregated IgG suggests CRP binding sites to be associated with PMN Fc receptors. Only when assayed in heat-inactivated plasma did CRP binding induce adherence of cells to tissue culture dishes. However, no metabolic and potentially cytotoxic stimulation of PMN was detected during CRP plasma-dependent attachment to surfaces: induction of aggregation, release of secondary granule constituents, and activation of the hexose monophosphate pathway were not observed. These results imply that CRP-PMN interactions is dependent on an additional factor present in heat-inactivated plasma and is followed only by a complement-independent increase in PMN attachment to surfaces. Because CRP was found to be deposited at sites of tissue injury, the CRP-mediated adherence of PMN may be an important step in localizing an inflammatory focus.

UI	MeSH Term	Description	Entries
D007074	Immunoglobulin G	The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B.	Gamma Globulin, 7S,IgG,IgG Antibody,Allerglobuline,IgG(T),IgG1,IgG2,IgG2A,IgG2B,IgG3,IgG4,Immunoglobulin GT,Polyglobin,7S Gamma Globulin,Antibody, IgG,GT, Immunoglobulin
D007249	Inflammation	A pathological process characterized by injury or destruction of tissues caused by a variety of cytologic and chemical reactions. It is usually manifested by typical signs of pain, heat, redness, swelling, and loss of function.	Innate Inflammatory Response,Inflammations,Inflammatory Response, Innate,Innate Inflammatory Responses
D009240	N-Formylmethionine Leucyl-Phenylalanine	A formylated tripeptide originally isolated from bacterial filtrates that is positively chemotactic to polymorphonuclear leucocytes, and causes them to release lysosomal enzymes and become metabolically activated.	F-Met-Leu-Phe,N-Formyl-Methionyl-Leucyl-Phenylalanine,Formylmet-Leu-Phe,Formylmethionyl Peptide,Formylmethionyl-Leucyl-Phenylalanine,Formylmethionylleucylphenylalanine,N-Formylated Peptide,N-formylmethionyl-leucyl-phenylalanine,fMet-Leu-Phe,F Met Leu Phe,Formylmet Leu Phe,Formylmethionyl Leucyl Phenylalanine,Leucyl-Phenylalanine, N-Formylmethionine,N Formyl Methionyl Leucyl Phenylalanine,N Formylated Peptide,N Formylmethionine Leucyl Phenylalanine,N formylmethionyl leucyl phenylalanine,Peptide, Formylmethionyl,Peptide, N-Formylated,fMet Leu Phe
D009504	Neutrophils	Granular leukocytes having a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes.	LE Cells,Leukocytes, Polymorphonuclear,Polymorphonuclear Leukocytes,Polymorphonuclear Neutrophils,Neutrophil Band Cells,Band Cell, Neutrophil,Cell, LE,LE Cell,Leukocyte, Polymorphonuclear,Neutrophil,Neutrophil Band Cell,Neutrophil, Polymorphonuclear,Polymorphonuclear Leukocyte,Polymorphonuclear Neutrophil
D010427	Pentose Phosphate Pathway	An oxidative decarboxylation process that converts GLUCOSE-6-PHOSPHATE to D-ribose-5-phosphate via 6-phosphogluconate. The pentose product is used in the biosynthesis of NUCLEIC ACIDS. The generated energy is stored in the form of NADPH. This pathway is prominent in tissues which are active in the synthesis of FATTY ACIDS and STEROIDS.	Hexose Monophosphate Shunt,Pentose Phosphate Shunt,Pentose Shunt,Pentosephosphate Pathway,Pentose-Phosphate Pathway,Pentosephosphate Shunt,Hexose Monophosphate Shunts,Pathway, Pentose Phosphate,Pathway, Pentose-Phosphate,Pathway, Pentosephosphate,Pathways, Pentose Phosphate,Pathways, Pentose-Phosphate,Pathways, Pentosephosphate,Pentose Phosphate Pathways,Pentose Phosphate Shunts,Pentose Shunts,Pentose-Phosphate Pathways,Pentosephosphate Pathways,Pentosephosphate Shunts,Shunt, Hexose Monophosphate,Shunt, Pentose,Shunt, Pentose Phosphate,Shunt, Pentosephosphate,Shunts, Hexose Monophosphate,Shunts, Pentose,Shunts, Pentose Phosphate,Shunts, Pentosephosphate
D010587	Phagocytosis	The engulfing and degradation of microorganisms; other cells that are dead, dying, or pathogenic; and foreign particles by phagocytic cells (PHAGOCYTES).	Phagocytoses
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
D002097	C-Reactive Protein	A plasma protein that circulates in increased amounts during inflammation and after tissue damage. C-Reactive Protein measured by more sensitive methods often for coronary heart disease risk assessment is referred to as High Sensitivity C-Reactive Protein (hs-CRP).	High Sensitivity C-Reactive Protein,hs-CRP,hsCRP,C Reactive Protein,High Sensitivity C Reactive Protein
D002449	Cell Aggregation	The phenomenon by which dissociated cells intermixed in vitro tend to group themselves with cells of their own type.	Aggregation, Cell,Aggregations, Cell,Cell Aggregations
D002634	Chemotaxis, Leukocyte	The movement of leukocytes in response to a chemical concentration gradient or to products formed in an immunologic reaction.	Leukotaxis,Leukocyte Chemotaxis