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PubMedDate not supplied

The nature of IgG complexes in alcoholic liver disease.

Circulating immune complexes have been described in most liver diseases, including alcoholic liver disease, although their pathogenic significance remains unclear. Currently available immune complex assays do not distinguish immunoglobulin aggregates from antigen-antibody complexes. Immunoglobulin aggregate formation occurs in vitro at 37 degrees C in the presence of hypergammaglobulinemia and/or hypoalbuminemia, conditions common in liver disease. To determine if hypergammaglobulinemia and/or hypoalbuminemia could predispose to immunoglobulin aggregate formation in vivo, 25 patients with alcoholic liver disease were studied. Using sucrose density gradient fractionation followed by quantitation of IgG by radioimmunoassay, high molecular weight IgG complexes (greater than 11S) were frequently present in alcoholic liver disease sera, and correlated with the degree of hypergammaglobulinemia and/or hypoalbuminemia, and with 125I-C1q binding activity. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of these complexes revealed only IgG and nonspecific trapping of several normal serum proteins. A specific complex-associated antigen could not be identified. While small, undetectable quantities of true antigen-antibody complexes might also be present, our data suggest that IgG complexes in alcoholic liver disease may represent immunoglobulin aggregate formation in vivo.

Antigen-Antibody Complex↗
PubMed1982

Spontaneous circulating immune complex like material in Brown-Norway rats. Role of environmental factors.

Brown-Norway rats maintained under conventional housing conditions showed a significant increase in the C1q binding activity of serum and to a lesser extent of the Raji cell assay whereas no change was observed, in BN rats maintained under specific pathogen free (SPF) conditions. Glomerular IgG deposits were encountered among rats with circulating immune complexes (CIC). This suggests that microbiological environment is a major factor in the spontaneous appearance of CIC which could be of pathogenic significance.

Animals↗
PubMed1994

Early response of brain resident microglia to kainic acid-induced hippocampal lesions.

We investigated the early response of microglia with complement and other proteins in well controlled rat central nervous system lesions. A selective neuronal degeneration in the hippocampal CA3 region was induced without direct tissue damage by an intraventricular injection of a small amount of kainic acid. As early as 1 h post injection, complement proteins C1q, C4, and C3 and immunoglobulin(Ig)G were found in the lesioned area. After 2 h, non-specific leakage of other plasma proteins occurred. By 3 h, reactive microglia gathered around the injured pyramidal neurons. Areas surrounding the lesions were depleted, on the other hand, indicating that these reactive microglia had originally resided in and migrated from such vacant areas. Upregulation of ICAM-1 expression by vascular endothelial cells commenced after 6 h. LFA-1-positive leucocytes were, then, accumulated in the vasculature, which was followed by an infiltration of leucocytes into the lesioned brain parenchyma. These results indicate that, following an acute neuronal injury, the response of the humoral factors such as complement proteins and IgG precedes the microglial reaction. Activation of vascular endothelial cells and subsequent infiltration of blood leucocytes occurs much later than the activation and migration of brain resident microglia. The origin of complement proteins and IgG in the lesioned brain parenchyma remains to be determined, although the production of complement proteins by microglia is suggested.

Animals↗
PubMed2005

Human renal epithelial cells produce the long pentraxin PTX3.

BACKGROUND: Pentraxin 3 (PTX3) is a prototypic long pentraxin with structural similarities in the C-terminal domain to the classical short pentraxins C-reactive protein (CRP) and serum amyloid P component. PTX3 is suggested to play an important role in the innate resistance against pathogens, regulation of inflammatory reactions, and clearance of apoptotic cells. Unlike the classic pentraxins, PTX3 is mainly expressed extrahepatically. The present study was designed to investigate the expression of PTX3 by human proximal renal tubular epithelial cells (PTECs). METHODS: PTECs were cultured in the presence or absence of inflammatory cytokines. PTX3 mRNA expression was measured by reverse transcription-polymerase chain reaction (RT-PCR) in human kidney and PTECs. PTX3 protein levels in PTEC cultures were quantified by enzyme-linked immunosorbent assay (ELISA). RESULTS: PTX3 mRNA was shown to be constitutively expressed in human kidney. Constitutive expression and production of PTX3 was shown in primary mesangial cells, in primary PTECs, and in renal fibroblasts. Further analysis showed that interleukin (IL)-1 and tumor necrosis factor-alpha (TNF-alpha) stimulation strongly enhanced the expression and production of PTX3 in PTECs in a dose- and time-dependent manner. In addition, activation of PTECs with IL-17 and CD40L, respectively, but not with IL-6 or IL-4, resulted in strongly increased production of PTX3, whereas granulocyte macrophage-colony-stimulating factor (GM-CSF) inhibited IL-1-induced PTX3 production. PTX3 produced by PTEC is functionally active in binding C1q. CONCLUSION: These results indicate that PTX3 is expressed and released by PTECs and that in proinflammatory conditions PTX3 production is up-regulated. Local expression of PTX3 may play a role in the innate immune response and inflammatory reactions in the kidney.

C-Reactive Protein↗
PubMed1995

C1Q complexes with beta-2-microglobulin and amyloid P-component in sera of patients with dialysis-associated amyloidosis.

We studied complexes composed of C1q and beta 2-microglobulin (C1q.beta 2M) or serum amyloid P-component (C1q.SAP) in the sera of 38 patients receiving hemodialysis (HD) and 20 healthy control subjects using an enzyme-linked immunoassay. We also compared complex levels in HD patients with and without symptoms of HD-associated amyloidosis (HA). Serum C1q-beta 2M levels were significantly higher in HD patients without HA than in healthy control subjects and significantly higher in HD patients with HA than in HD patients without HA. Serum C1q.SAP levels were significantly lower in patients with HA than in those without HA. These results suggest that C1q.beta 2M may contribute to HA.

Amyloidosis↗
PubMed1985

Evaluation of circulating immune complexes in lymphomas and leukemias using two different assays.

Circulating immune complexes (CICs) have been detected in the sera of patients with non-Hodgkin's lymphoma (NHL), Hodgkin's disease, chronic myeloid leukemia, and acute lymphoblastic leukemia by using C1q-binding and L1210-binding assays. Both assays gave broadly similar patterns of reactivity in terms of frequency and magnitude, though there are some differences. Significantly elevated CIC levels were observed in all pathologic groups. However, sera from NHL patients with an unfavorable prognosis consistently exhibited the highest frequency of positive values and mean CIC levels in both these assays. The two tests showed concordance in 66.6% of the NHL patients' sera and were significantly correlated. Of the sera from NHL patients 12.7% were positive in the C1q-binding assay only and 15.9% in the L1210-binding assay only. Both the assays gave positive results in some patients, and a degree of overlap indicates the presence of different types of CIC in cancer patients' sera. The combined use of two methods for detecting CICs may be useful for evaluation of the activity, the extent, and the prognosis of the malignant disease.

Animals↗
PubMed2001

Expression of membrane C1q in human monocyte-derived macrophages is developmentally regulated and enhanced by interferon-gamma.

The present study investigated when during "in vitro" maturation macrophages (MPhi) express membrane C1q (mC1q), and whether cell activation affects expression and function of mC1q. Although C1q mRNA was repeatedly detected in freshly isolated monocytes using reverse transcriptase-polymerase chain reaction, C1q protein was observed only in developing MPhi from day 1 to 4 on using immunodetection and flow cytometry. However, the quantity of mC1q and other MPhi membrane proteins differed strikingly in cells from different donors. We report here for the first time that CD14(+) and CD14(-) mC1q-bearing MPhi can develop, and that interferon-gamma increases mC1q display at the cell surface, and mC1q-mediated phagocytosis.

Cell Differentiation↗
PubMed1983

Structural aspects of hydroxyproline-containing proteins.

The occurrence of hydroxyproline (Hyp) in collagen, C1q and acetylcholineesterase (AChE) raises important questions concerning the role of this unusual imino acid in the structure and function of these proteins. Available data on collagen indicate that Hyp is necessary for the normal secretion of the protein after its synthesis and for the integrity of the triple-helical conformation. Studies from our laboratory have dealt with the structural aspects of the posttranslational conversion of proline to hydroxyproline in collagen mediated by prolyl hydroxylase. We proposed that the beta-turn conformation at the Pro-Gly segments in the nascent procollagen molecule are the sites of the enzymatic hydroxylation and that this conformation changes over to the collagen-like helix as a result of the hydroxylation process. Recently, we have provided additional experimental support to our proposal by a) synthesizing specific beta-turn oligopeptides containing the Pro-Gly as well as Pro-Ala and Pro-DAla sequences and showing that these act as inhibitors of the enzymatic hydroxylation of a synthetic substrate and b) demonstrating, by circular dichroism spectroscopy, the occurrence of a conformational change leading to the triple-helix as a direct consequence of proline hydroxylation in a non-helical polypeptide substrate. We have also observed that the acquisition of hydroxylation results in a significant enhancement of the rate of folding of the polypeptide chain from the unfolded to the triple-helical conformation. We believe that our observations on proline hydroxylation in collagen should also be applicable to C1q and acetylcholineesterase both of which share the general structural and functional properties of collagen in their "tail" regions. Using the techniques employed in collagen studies, one should be able to assess the role of hydroxyproline in the folding, structural stabilities and functions of C1q and AChE. This would also involve the study of the unhydroxylated and hydroxylated precursors of these proteins which may share common structural features with their collagen counterparts. Finally, a systematic study of hydroxyproline-containing peptides and polypeptides has been initiated by us so as to understand the exact manner in which Hyp participates in the formation and stability of the triple-helical conformation in the proteins in which it occurs.

Acetylcholinesterase↗
PubMed1993

Functional domains of the human C1q A-chain.

This brief review was inspired by discussions relating to the IIIrd. International C1 Workshop (this volume) and the realization that certain functional properties of the C1q molecule are limited exclusively to the A-chain. The collagen-like region of the A-chain contains a major binding site for non-immunoglobulin substances, which include C-reactive protein, serum amyloid P, LPS and DNA. This binding site is immediately adjacent to, and partially overlapping with, an arthritis-modulating epitope common to the C1q A-chain and various types of collagen, including cartilage type II collagen. At the N-terminal end of the C1q A-chain is a leader peptide sequence that anchors the intact C1q molecule firmly in the membrane of macrophages, the C1q molecule can thus be classified as a type II membrane protein, functioning as an additional receptor for molecules known to react with C1q in fluid phase such as the Fc region of IgG, LPS and polyanionic molecules (e.g. chondroitin sulphate, heparin, dextran sulphate etc.). The various domains within the A-chain, and their respective functions (or potential functions), are presented and discussed in the context of the intact C1 molecule and with regard to any wider functional relevance.

Amino Acid Sequence↗
PubMed1997

Evidence that the two C1q binding membrane proteins, gC1q-R and cC1q-R, associate to form a complex.

Two types of widely coexpressed, highly acidic, cell membrane binding proteins that display preferential domain specificity for C1q have been described: a 60-kDa calreticulin homologue, designated cC1q-R, that binds to the collagen-like "stalk" and a 33-kDa glycoprotein with affinity for the globular "heads" (gC1q-R). Although the two molecules are known to be coexpressed on all cell types examined to date and often coelute during purification, there is no direct evidence showing that they associate with each other either on the membrane or when examined in a purified system. In this report we present the first evidence that 1) biotinylated cC1q-R binds to recombinant as well as native gC1q-R, as assessed by solid phase ELISA; 2) binding sites for cC1q-R are located within N-terminal residues 76 through 93 of the mature form of gC1q-R and within residues 204 through 218; 3) this interaction is inhibited by two mAbs, 60.11 and 46.23, that recognize primarily epitopes within the N terminus of gC1q-R corresponding to residues 74 through 96 and by mAb 74.5.2 that recognizes epitopes within residues 204 through 218; and 4) biotinylated cC1q-R binds to microtiter-fixed Raji and K562 cells, and this interaction is inhibited by mAb 60.11. Furthermore, coimmunoprecipitation analysis of Raji cell membranes with anti-gC1q-R mAbs showed the presence of cC1q-R in addition to gC1q-R. Taken together, the evidence suggests that cC1q-R is able to form a complex with gC1q-R and may associate with gC1q-R on the cell surface.

Amino Acid Sequence↗
PubMed1982

Circulating immune complexes in eosinophilic fasciitis.

Serum immune complexes were measured in 22 patients with eosinophilic fasciitis, 8 of whom had serial determinations. Elevated levels were found by Raji cell radioimmunoassay in 14 (64%) patients, by agarose gel electrophoresis in 13 (59%), and by C1q agglutination-inhibition in 9 (41%). Elevated levels by Raji cell assay were present more frequently at times of active disease [17 of 22 sera (77%)] than at times of inactive disease [2 of 24 (8%) (P less than 0.0005)] and were more closely correlated with disease activity than were eosinophilia, hypergammaglobulinemia, or increased erythrocyte sedimentation rate.

Adult↗
PubMed1993

Similarity in structure between C1q and the collectins as judged by electron microscopy.

The collectins are carbohydrate binding proteins which, like C1q, contain collagen-like sequences. The collectins belong to group III of the family of lectins containing C-type carbohydrate recognition domains (CRDs). The structural similarity between the collectins and C1q is clearly demonstrated by electron microscopy in that they all contain multiple polypeptides which are organised into subunits containing triple-helical stalks throughout their collagen-like regions and globular 'heads' in the C-terminal regions. Four, or six, of these structures are associated via distinct, short, N-terminal regions to form the oligomeric molecules seen in the electron microscope. The overall structural similarity between C1q and the collectins, however, does not extend to similarity in amino acid sequences over the C-terminal regions. The C-terminal regions of C1q, unlike those of the collectins, do not contain the conserved residues found in the CRDs present in the C-type lectins. Instead, C1q has a high degree of homology to collagen sequences (Type VIII and X) and this is consistent with the fact that, unlike the collectins, C1q binds to protein motifs in IgG, or IgM, rather than to carbohydrate structures. Also, despite sometimes showing interruptions in their collagen-like regions, the collectins do not always display a 'bend' in their collagen-like 'stalks' similar to that which is seen in C1q. Therefore, C1q may be more closely related to collagens than to the collectins. The collectins can be classed into two distinct group, with MBP and SP-A being hexamers and SP-D, conglutinin and collectin-43 (CL-43) being tetramers, with proteins in the latter group also having significantly larger dimensions with respect to the length of their collagen-like 'stalks'.

Amino Acid Sequence↗
PubMed2001

gC1q-R/p33, a member of a new class of multifunctional and multicompartmental cellular proteins, is involved in inflammation and infection.

Human gC1q-R (p33, p32, C1qBP, TAP) is a ubiquitously expressed, multiligand-binding, multicompartmental cellular protein involved in various ligand-mediated cellular responses. Although expressed on the surface of cells, an intriguing feature of the membrane-associated form of gC1q-R is that its translated amino acid sequence does not predict the presence of either a sequence motif compatible with a transmembrane segment or a consensus site for a glycosylphosphatidylinositol anchor. Moreover, the N-terminal sequence of the pre-pro-protein gC1q-R contains a motif that targets the molecule to the mitochondria and as such was deemed unlikely to be expressed on the surface. However, several lines of experimental evidence clearly show that gC1q-R is present in all compartments of the cell, including the extracellular cell surface. First, surface labeling of B lymphocytes with the membrane-impermeable reagent sulfosuccinimidyl 6-(biotinamido)hexanoate shows specific biotin incorporation into the surface-expressed but not the intracellular form of gC1q-R. Second, FACS and confocal laser scanning microscopic analyses using anti-gC1q-R IgG mAb 60.11 or 74.5.2, and the fluorophore Alexa 488-conjugated F(ab')2 goat anti-mouse IgG as a probe, demonstrated specific staining of Raji cells (>95% viable). Three-dimensional analyses of the same cells by confocal microscopy showed staining distribution that was consistent with surface expression. Third, endothelial gC1q-R, which is associated with the urokinase plasminogen activator receptor, and cytokeratin 1 bind 125I-high molecular weight kininogen in a specific manner, and the binding is inhibited dose-dependently by mAb 74.5.2 recognizing gC1q-R residues 204-218. Fourth, native gC1q-R purified from Raji cell membranes but not intracellular gC1q-R is glycosylated, as evidenced by a positive periodic acid Schiff stain as well as sensitivity to digestion with endoglycosidase H and F. Finally, cross-linking experiments using C1q as a ligand indicate that both cC1q-R and gC1q-R are co-immunoprecipitated with anti-C1q. Taken together, the evidence accumulated to date supports the concept that in addition to its intracellular localization, gC1q-R is expressed on the cell surface and can serve as a binding site for plasma and microbial proteins, but also challenges the existing paradigm that mitochondrial proteins never leave their designated compartment. It is therefore proposed that gC1q-R belongs to a growing list of a class of proteins initially targeted to the mitochondria but then exported to different compartments of the cell through specific mechanisms which have yet to be identified. The designation 'multifunctional and multicompartmental cellular proteins' is proposed for this class of proteins.

Amino Acid Motifs↗
PubMed1976

Insulin--anti-insulin complexes.

When guinea pig antibodies (ab) bind insulin (ag), they can make complexes of different sizes. We propose the following model: In ab excess: (see article) Intermediate: (see article) In ag excess: (see article). An insulin molecule acts as a bivalent antigen, although more than two different antigenic determinants may be present. In vivo the large C II type disappears more rapidly from the blood than does the C I. The C II binds to complement factor C1q, whilst C I and C III do not. In sera from insulin treated patients we found C I and C III. The lack of lattice formation, due to the bivalency, may explain the difficulty in obtaining precipitation. The different complexes may influence calculations of antibody concentrations and affinity constants of the binding sites. The in vivo effects and possible clinical effects of antibodies to insulin may depend on the type of complex formed. Possibly, prevailing C II formation tends to cause large insulin requirements, although C II may seldomly be detected in the blood, because of rappid trapping. The immune complexes could affect the progression of angiopathy a) by interfering with insulin metabolism and control of diabetes, and b) by complement activation (mainly C II) and trapping in the vascular bed.

Animals↗
PubMed1989

Functions associated with the C1q receptor.

Information gathered from various sources indicates that the receptor for human C1q is expressed on a wide range of normal and cultured cell lines. Similarly, the functions mediated by the C1qR are as diverse as the cells that express the molecule. On B lymphocytes, for instance, the C1qR is known to mediate cellular cytotoxicity, induce an anti-proliferative response, inhibit synthesis of IL-1 and modulate the synthesis of Ig, whereas on PMNs and monocytes the C1qR participates in the increase of oxidative metabolism and enhancement of phagocytosis of opsonized target particles. Endothelial cells which form an important barrier between blood and vascular basement membrane use their C1qR to localize C1q bearing immune complexes into the basement membrane and thus initiate an inflammatory response. Human diploid fibroblasts express two types of C1qRs: a low affinity C1qR for the collagen-like domain and a small subpopulation expressing high affinity C1qR which binds to the globular region of C1q. Since the high affinity subpopulation manifests characteristics of fibroblasts participating in wound healing and tissue regeneration, the C1qR on these cells may play an important role at sites of inflammation. Recently, binding of C1q to the C1qR on mouse fibroblasts was shown to induce chemotaxis and K+ conductance activation with an increase in cytosolic Ca2+. Although isolation of C1qR from every cell type has not been accomplished as yet, partial characterization of highly purified C1qR from Raji cells and platelets indicate that at least on these cell types, the structure of the molecule is similar. Both molecules are anionic, single chain glycoproteins of approximately 67-70 kDA and upon reduction on SDS-PAGE migrate to an apparent 80-85 kDa indicative of the presence of disulfide bonds. The sedimentation coefficient was estimated to be 2.4-4.2S for platelet C1qR and 4.2S for that of Raji. Equilibrium isoelectric focusing showed the Raji cell C1qR to migrate with a pI of 5.5-6.0. Because the Raji C1qR reveals two components when analyzed by two dimensional SDS-PAGE, the possibility that the C1qR may be a doublet of two apparent 70 kDa molecules only one of which contains relatively more intrachain disulfide bonds is being raised.

Animals↗
PubMed1996

Isolation and characterization of the kininogen-binding protein p33 from endothelial cells. Identity with the gC1q receptor.

Kininogens, the precursor proteins of the vasoactive kinins, bind specifically, reversibly, and saturably to platelets, neutrophils, and endothelial cells. Two domains of the kininogens expose major cell binding sites: domain D3 that is shared by H- and L-kininogen and domain D5H that is exclusively present in H-kininogen. Previously we have mapped the kininogen cell binding sites to 27 residues of D3 ("LDC27") and 20 residues of D5H ("HKH20"", respectively (Herwald, H., Hasan, A. A. K., Godovac-Zimmermann, J., Schmaier, A. H., and Müller-Esterl, W. (1995) J. Biol. Chem. 270, 14634-14642; Hasan, A. A. K., Cines, D. B., Herwald, H., Schmaier, A. H., and Müller-Esterl, W. (1995) J. Biol. Chem. 270, 19256-19261). The corresponding kininogen acceptor site(s) exposed by the cell surfaces are still poorly defined. Using a non-ionic detergent, Nonidet P-40, we have been able to solubilize kininogen binding sites from an endothelial cell line, EA.hy926, in their functionally active form. Affinity chromatography of the solubilized kininogen binding sites on HKH20, a synthetic peptide representing the D5H cell binding site, allowed us to isolate a 33-kDa protein ("p33") that binds specifically and reversibly to H-kininogen with a KD (apparent dissociation constant) of 9 +/- 2 nM. Preparative SDS electrophoresis followed by NH2-terminal amino acid sequence analysis identified the kininogen-binding protein p33 as the gC1q receptor ("gC1qR"), an extrinsic membrane protein that interacts with the globular domains of the complement component C1q. The purified p33 binds C1q with moderate affinity, KD = 240 +/- 10 nM. Recombinant expression of the corresponding cDNA in Escherichia coli demonstrated that p33 binds H-kininogen, but not L-kininogen. Peptide HKH20 but not peptide LDC27 inhibited binding of H-kininogen to the recombinant p33 in a concentration-dependent manner, indicating that H-kininogen binds to p33 via domain D5H. Recombinant p33 efficiently inhibited the binding of H-kininogen to EA.hy926 cells. Factor XII, but not prekallikrein, competed with H-kininogen binding to p33. These findings suggest that an endothelial binding protein mediates the assembly of critical components of the kinin-generating pathway on the surface of endothelial cells, thereby linking the early events of kinin formation and complement activation.

Amino Acid Sequence↗
PubMed2005

Detection of an autologous ligand for mannan-binding lectin on human B lymphocytes.

Mannan-binding lectin (MBL) is a collectin and a major soluble pattern-recognition protein. MBL can distinguish self from nonself and altered self using its C-type carbohydrate recognition domain and may also interact via its collagen-like region with autologous cells. Recently, it was found that MBL could bind to adherent cells (monocytes) and dendritic cells in a specific and sugar-sensitive manner. We have now investigated the interaction of MBL with fresh human peripheral blood cells and report binding to B lymphocytes and natural killer cells. The binding to B lymphocytes was studied in detail and was compared with the binding of MBL to monocytes and dendritic cells. Binding of MBL to B cells was evident at physiological MBL and calcium concentrations but was optimal at supraphysiological MBL concentrations. It was readily inhibited by autologous serum, mannan, mannose, GlcNAc and (to a lesser extent) galactose but not by C1q. A similar, but not identical, inhibition profile was observed with dendritic cells, but monocytes were not sensitive to mannose or mannan. We conclude that MBL is capable of binding to differently glycosylated ligands on several autologous cell types via its carbohydrate-recognition domain. We speculate that this could have functional significance at extravascular sites, but perhaps only in individuals possessing MBL genotypes conferring MBL sufficiency.

Antibodies↗
PubMed1985

Development of a novel C1q immunoadsorbent for removal of circulating immunecomplexes: quantitative isolation of hepatitis B virus surface antigen and immunecomplexes.

A technique for large scale production of human C1q from plasma by affinity chromatography on an anti-C1q column is described. Affinity purified C1q was covalently coupled to a newly developed agarose polyacrolein microsphere beads immunoadsorbent. This immunoadsorbent was utilized for quantitative removal of artificially formed bovine serum albumin (BSA)-anti-BSA immune complexes (IC). The C1q affinity column was then used for the isolation of immunecomplexes containing hepatitis B virus (HBV) surface antigen (HBsAg) from serum of an HBsAg carrier. Identical columns may be utilized for quantitative removal of a variety of IC from blood of patients with infectious and autoimmune diseases, as well as neoplastic diseases. Furthermore, dissociated immunecomplexes will provide an additional source for purification of specific antigens.

Animals↗