A Two-Component System of Human Serum
Agglutinating Gelatine-Coated Erythrocytes

Wolff, I.; Timpl, R.; Pecker, I.; Steffen, C.

doi:10.1159/000464646

Cited by 5 publications

(7 citation statements)

References 8 publications

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“…To conclude, we would like to underline that in rsdioimmunoassay, using second antibody technique factors other than anticollagen antibodies that react with collagen, such as glycosaminoglycans ( I8, 19) or antigelatine factor (20), cannot interfere with the determination of anticollagen antibodies and thus cause false positive results. In radioimmunoassay only 14Ccollagen specifically bound by antibodies is precipitated by second antibody.…”

Section: Discussionmentioning

confidence: 99%

Demonstration of anticollagen antibodies in rheumatoid arthritis synovial fluids by ¹⁴c‐radioimmunoassay

Menzel

Steffen

Kolarz

et al. 1978

Arthritis & Rheumatism

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Twenty-seven synovial fluids from rheumatoid arthritis ( R A ) patients and 17 synovial fluids from controls were investigated in a new radioimmunoassay for anticollagen antibodies. In vitro labeled human 14C-collagen of type I in native or denatured state was used as antigen. Passive hemagglutination was used in comparison. Parameters for defining positive results in radioimmunoassay were evaluated on the basis of control synovial fluids. Synovial fluids from 20 RA patients (74%) showed antibodies to denatured collagen; synovial fluids from 8 RA patients (30%) also demonstrated antibodies to native collagen. Control fluids of posttraumatic effusions were negative; among the other controls synovial fluid from 1 psoriatic arthritis patient reacted positively. Inhibition experiments showed that antibodies to denatured collagen

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Section: Discussionmentioning

confidence: 99%

Demonstration of anticollagen antibodies in rheumatoid arthritis synovial fluids by ¹⁴c‐radioimmunoassay

Menzel

Steffen

Kolarz

et al. 1978

Arthritis & Rheumatism

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“…below, fibronectin appears to be involved in some platelet reactions (10,14,204) . As already mentioned, fibronectin has opsoníc activity for macrophages (3,18,19,94,241), which could be important for debriding the wound. Fibronectin may also be one of the agents attracting fibroblasts into the wound, because it is highly chemotactic for fibroblasts (61).…”

Section: Role Of Circulating Fibronectin In Wound Repairmentioning

confidence: 98%

“…Opsonic proteins that facilitate the phagocytic activities of macrophages are known to be present in serum (3,18,94,200,241) . These proteins, called anti-gelatin factor (241) and a2-SB-glycoprotein (18), were isolated from serum and subsequently shown by independent studies to be identical to serum fibronectin (38,200) .…”

Section: Fibronectinmentioning

confidence: 99%

Role of collagenous matrices in the adhesion and growth of cells.

Kleinman¹,

Klebe²,

Martin³

1981

The Journal of Cell Biology

1,291

434

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It has long been appreciated that, for many types of cells, attachment to a substrate is required for their replication. Collagen substrates enhance the growth (64,70,109,238) as well as the differentiation (40,69,85,86,146,161,184), of many cells in culture above that observed with other substrates such as plastic and glass. As discussed in this report, many cultured cells including fibroblasts, myoblasts, hepatocytes, chondrocytes, and certain epithelial cells are thought not to bind directly to the collagen substrate or to the plastic surface of culture dishes (31,73,74,76,77,89,93,113,164,220) . Instead, extracellular glycoproteins bind the cells to the substrate. One of these attachment proteins, fibronectin, has been extensively studied (99,151,166,227,228,244) . Fibronectin is produced by fibroblasts (13,197,246) and endothelial cells (102, 140) as well as some other cell types . It is also present in high concentrations in blood and serum (152) . In culture, serum fibronectin, as well as that produced by the cells, can bind to both the collagen substrates and the tissue culture plastic surface and mediate the attachment of cells (73,113,164,242) . Circulating fibronectin participates in a variety of reactions important to wound healing, including the adhesion and spreading of platelets on collagen (10, 14, 75, 100, 204), binding to the fibrin clot (74,150,198) and to collagen (37,46,94,103,119), promoting opsonization reactions by phagocytic cells (18,94,201), and promoting fibroblast migration (6, 61) . Thus, fibronectin not only functions as an attachment protein, but also may play an important role in repair reactions .In the case of certain differentiated cells, such as chondrocytes (89) and epithelial cells (159, 220), glycoproteins different from fibronectin are active in attachment. The components of these extracellular matrices of fibroblasts, chondrocytes, and epithelial cells differ with the cell type, and they require separate attachment proteins to provide additional specificity to the interaction of the cell with its matrix. Alterations in cellsubstratum interactions are observed in differentiating cells and after spontaneous transformation of cells or exposure to oncogenic agents (99,228) . This review will briefly outline our current knowledge of the types of collagen and their distribution and biosynthesis. Then, the interaction of cells with col-REVIEW

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“…coated with the denatured collagens (parent gelatine) and hemagglutination and inhibition tests were performed as described earlier [9]. I n investigation of 32 sera from healthy donors or pregnant women with all six antigens, no significant titer differences were observed.…”

mentioning

confidence: 99%

“…I n rabbit antisera t o native and denatured calf collagen, a n antibody was demonstrated which exhibited the same pattern of crossreaction as the anti-gelatine factor [7, 81 and was similarly better inhibited by Tthan by C-peptides [4, 71. It differed, however, in several respects, like for instance in its stability a t 56°C [9]. Since in both cases no or a strongly diminished reactivity with native collagen was observed [5, 91, it seems reasonable t o assume that the antigenic determinants are hidden in the helical interior of native collagen and become available after slight denaturation.…”

mentioning

confidence: 99%

Reaction of the Human Anti‐Gelatine Factor with Gelatine from Different Species and with Collagen Peptides

Wolff

Timpl

1968

Vox Sanguinis

Self Cite

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Naturally occurring anti-gelatine antibodies, detectable in human and in some animal sera by precipitation, showed an equal reactivity with gelatine from different species [2]. Recently we have demonstrated in human sera an anti-gelatine factor reacting in passive hemagglutination, which probably belongs t o the yM-globulin class [9]. I n the present study the cross-reacting properties of the antigelatine factor and its reaction with collagen peptides were investigated and compared with available data [4, 5, 7, 81 about the specificity of experimentally produced rabbit antibodies t o native and denatured collagen.Acid-soluble collagen was prepared from the skin of calf, sheep, rat and rabbit, the joint capsule tissue of a six-years-old child [6] and from the carp swim bladder [I]. Tanned human red cells were

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A Two-Component System of Human Serum Agglutinating Gelatine-Coated Erythrocytes

Cited by 5 publications

References 8 publications

Demonstration of anticollagen antibodies in rheumatoid arthritis synovial fluids by ¹⁴c‐radioimmunoassay

Demonstration of anticollagen antibodies in rheumatoid arthritis synovial fluids by ¹⁴c‐radioimmunoassay

Role of collagenous matrices in the adhesion and growth of cells.

Reaction of the Human Anti‐Gelatine Factor with Gelatine from Different Species and with Collagen Peptides

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A Two-Component System of Human Serum Agglutinating Gelatine-Coated Erythrocytes

Cited by 5 publications

References 8 publications

Demonstration of anticollagen antibodies in rheumatoid arthritis synovial fluids by 14c‐radioimmunoassay

Demonstration of anticollagen antibodies in rheumatoid arthritis synovial fluids by 14c‐radioimmunoassay

Role of collagenous matrices in the adhesion and growth of cells.

Reaction of the Human Anti‐Gelatine Factor with Gelatine from Different Species and with Collagen Peptides

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Demonstration of anticollagen antibodies in rheumatoid arthritis synovial fluids by ¹⁴c‐radioimmunoassay

Demonstration of anticollagen antibodies in rheumatoid arthritis synovial fluids by ¹⁴c‐radioimmunoassay