Enzyme-linked immunoassay (ELISA) for connective tissue components

Rennard, Stephen I.; Berg, Richard A.; Martin, George R.; Foidart, Jean‐Michel; Robey, Pamela Gehron

doi:10.1016/0003-2697(80)90300-0

Cited by 571 publications

(170 citation statements)

References 22 publications

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“…Measurement of fibronectin immunoactivity and ligand binding by ELISA (21). Microtiter plate wells (Dynatech, Alexandria, VA) were coated with purified plasma fibronectin (200 ng/well) by overnight incubation at 4°C.…”

Section: Methodsmentioning

confidence: 99%

The immunoreactivity, ligand, and cell binding characteristics of rheumatoid synovial fluid fibronectin

Carsons

Lavietes

Diamond

et al. 1985

Arthritis & Rheumatism

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Fibronectin promotes macrophage adherence and expression of Fc receptors, is chemotactic for fibroblasts, and is an opsonin for fibrin and denatured collagen. These properties suggest a role for fibronectin in the modulation of joint inflammation. Since structural modification of the fibronectin molecule has been shown to result in loss or de novo acquisition of opsonic and chemotactic activity, we determined the functional and immunochemical properties of fibronectin isolated from the inflamed joint. Eighty‐six percent of synovial fluids obtained from patients with active rheumatoid arthritis (RA) contained fibronectin fragments, and 39% of the fluids no longer displayed the dimeric form. Compared with native fibronectin, RA peptides were as active in promoting synoviocyte chemotaxis and in glycosaminoglycan binding, but displayed lower affinity for fibrin and gelatin. Although comparable with intact protein in augmenting monocyte attachment to gelatin, the RA synovial fluid peptides did not augment monocyte attachment to fibrin. Analysis of whole synovial fluid and isolated fibronectins by enzyme immunoassay showed that the increased fibronectin immunoreactivity, previously reported in RA synovial fluid, measures intact and nearly intact protein and does not measure extensively degraded fragments.

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Section: Methodsmentioning

confidence: 99%

The immunoreactivity, ligand, and cell binding characteristics of rheumatoid synovial fluid fibronectin

Carsons

Lavietes

Diamond

et al. 1985

Arthritis & Rheumatism

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“…These antibodies were raised in sheep using an antigen extracted from the mouse EHS tumor and purified by salt precipitation and ion exchange chromatography [33,34]; they react with basal laminae of various animal tissues and in particular with rat glomerular basal laminae [16,18], and their high specificity has been demonstrated previously using several approaches [16,18,35]. To locate type IV collagen, the protein A-gold immunocytochemical postembedding approach was applied [25].…”

Section: Methodsmentioning

confidence: 99%

Alteration in the distribution of type IV collagen in glomerular basal laminae in diabetic rats as revealed by immunocytochemistry and morphometrical approach

Bendayan

1985

Diabetologia

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Summary.The gomerular basal laminae of normoglycaemic and long-term streptozotocin-induced hyperglycaemic rats was studied by morphometrical and immunocytochemical approaches. Using the orthogonal intercept method, we have confirmed that in long-term diabetes, the thickness of the glomerular basal laminae increases significantly. Applying the high resolution protein A-gold immunocytochemical technique, type IV collagen was localized in the glomerular basal laminae. In tissues from normoglycaemic animals the labelling was present over the central lamina densa. However, the labelling obtained over the thickened glomerular basal laminae of the hyperglycaemic animals was restricted to the subendothelial site of the lamina. Thus major alteration in the distribution of type IV collagen occurs during the development of diabetic microangiopathy in hyperglycaemic animals.

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“…Typespecific anti-collagen antibodies were purified from crude antisera by cross-adsorption of affinity columns consisting of heterogenous collagen types coupled with activated CH-Sepharose 4B (Pharmacia Fine Chemicals, Uppsala, Sweden) followed by immunoadsorption of affinity columns prepared from the same type of collagen immunized and by elution. 23 The specificity of each antibody was analyzed by the inhibition test using ELISA, 24 and each antibody showed no cross-reactivity with any other types of collagen. 25 All animals used for the production of antibodies were maintained in accordance with the guidelines of the Committee on Animal Care and Use of the Kanazawa University School of Medicine.…”

Section: Preparation Of Type-specific Anti-collagen Antibodiesmentioning

confidence: 99%

Collagens in human atherosclerosis. Immunohistochemical analysis using collagen type-specific antibodies.

Katsuda

Okada

Minamoto

et al. 1992

Arterioscler Thromb

182

126

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This study represents a systematic analysis of the distribution of collagen types in human atherosclerotic lesions. Formalin-fixed, paraffin-embedded aortic tissues of 40 lesions from 16 different individuals ranging in age from 1 month to 84 years were examined immunohistochemically using antibodies to type I, III, IV, V, and VI collagens. Preembedding immunoelectron microscopy was used to simultaneously localize type V and VI collagens within the lesions. Localization of type HI collagen was very similar to that of type L and type VI collagen appeared together with these two types of collagen in the thickened intlmas of all stages of the lesion. Type V collagen was not detected in either fatty streaks or the mild Intimal thickening of the aortas of children. With advancing age and lesion progression, the immunoreactivity with anti-type V collagen antibody became more intense. Type IV collagen was detected in the basement membrane region of intimal cells. In advanced lesions thick deposits of type IV collagen were found around the elongated smooth muscle cells. Using immunoelectron microscopy, type V collagen was found to be localized to cross-banded collagen fibers, and type VI collagen was found to be localized to beaded filaments present throughout the interstitium of the thickened intima. These findings suggest that collagens preserve the pathophysiological and functional integrity of the vascular wall by providing mechanical support as well as assuring the proper interaction of cells during the formation of atherosclerotic lesions. (Arteriosclerosis and Thrombosis 1992;12:494-502) KEYWORDS • atherosclerosis • collagen • immunohistochemistryA therosclerosis is a disease of large and medium-/ \ sized arteries and is characterized by focal X A . thickening of the inner portion of the artery wall in association with fatty deposits.1 -2 The common underlying events responsible for lesion formation are intimal smooth muscle cell proliferation, formation of new extracellular matrix by these cells, and the possible accumulation of lipid. Collagens are regarded as important in this disease not only because they represent the major extracellular component in the atherosclerotic plaque and thereby contribute to the occlusive nature of the disease but also because they may play an important role in hemostasis and thrombosis through stimulation of blood platelets. 3 In addition, recent studies have indicated that collagens can influence the proliferation and state of differentiation of smooth muscle cells in vitro.4 -6 Thus, it seems likely that collagens could play a vital role in the pathogenesis of this disease.Collagen is now recognized as a family of proteins of at least 13 genetically distinct subtypes, each of which has a unique tissue specificity. -9 Of these 13 collagen types, six (I, III, IV, V, VI, and VIII) are present in blood vessels. 10 All of these collagen types except type VIII collagen are known to be synthesized by smooth From the Department of Pathology, School of Medicine, Kanazawa University, K...

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Enzyme-linked immunoassay (ELISA) for connective tissue components

Cited by 571 publications

References 22 publications

The immunoreactivity, ligand, and cell binding characteristics of rheumatoid synovial fluid fibronectin

The immunoreactivity, ligand, and cell binding characteristics of rheumatoid synovial fluid fibronectin

Alteration in the distribution of type IV collagen in glomerular basal laminae in diabetic rats as revealed by immunocytochemistry and morphometrical approach

Collagens in human atherosclerosis. Immunohistochemical analysis using collagen type-specific antibodies.

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