The small proteoglycans of cartilage matrix

Stănescu, V.

doi:10.1016/0049-0172(90)90047-j

Cited by 35 publications

(25 citation statements)

References 110 publications

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“…Biglycan is composed of a 38 kDa core protein that is substituted with 2 GAGs chains on N-terminal Ser-Gly sites (Neame et al, 1989;Fisher et al, 1991). Biglycans are found in the interterritorial matrix and in the pericellular area where they are thought to modulate morphogenesis and differentiation (Stanescu, 1990). Decorin is mainly located in the interterritorial matrix involved in the regulation of important biological functions like matrix organization, cell adhesion, migration and proliferation (Gallagher, 1989;Bock et al, 2001).…”

Section: Discussionmentioning

confidence: 99%

Fourier transform infrared imaging of focal lesions in Human osteoarthritic cartilage

David-Vaudey

Burghardt²,

Keshari³

et al. 2005

eCM

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Fourier Transform Infrared Imaging (FTIRI) is a new method for quantitatively assessing the spatial-chemical composition of complex materials. This technique has been applied to examine the feasibility of measuring changes in the composition and distribution of collagen and proteoglycan macromolecules in human osteoarthritic cartilage. Human cartilage was acquired post-operatively from total joint replacement patients. Samples were taken at the site of a focal lesion, adjacent to the lesion, and from relatively healthy cartilage away from the lesion. Sections were prepared for FTIRI and histochemical grading. FTIRI spectral images were acquired for the superficial, intermediate, and deep layers for each sample. Euclidean distance mapping and quantitative partial least squares analysis (PLS) were performed using reference spectra for type-II collagen and chondroitin 6-sulphate (CS6). FTIRI results were correlated to the histology-based Mankin scoring system. PLS analysis found relatively low relative concentrations of collagen (38 ± 10%) and proteoglycan (22 ± 9%) in osteoarthritic cartilage. Focal lesions were generally found to contain less CS6 compared to cartilage tissue adjacent to the lesion. Loss of proteoglycan content was well correlated to histological Mankin scores (r=0.69, p<0.0008). The evaluation of biological tissues with FTIRI can provide unique quantitative information on how disease can affect biochemical distribution and composition. This study has demonstrated that FTIRI is useful in quantitatively assessing pathology-related changes in the composition and distribution of primary macromolecular components of human osteoarthritic cartilage.

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Section: Discussionmentioning

confidence: 99%

Fourier transform infrared imaging of focal lesions in Human osteoarthritic cartilage

David-Vaudey

Burghardt²,

Keshari³

et al. 2005

eCM

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“…The extracellular matrix of the eye shares a number of structural components with hyaline cartilage. FMOD is found in sclera (38), and it is expressed by epithelial cells of the eye (39). FMOD often contains one or two polyanionic keratan sulfate chains, distributed among the four potential substitution sites that are present in the leucine-rich region (40).…”

Section: The Tyr-384 Variant Of Fh Interacts With Fmod With Higher Afmentioning

confidence: 99%

The Factor H Variant Associated with Age-related Macular Degeneration (His-384) and the Non-disease-associated Form Bind Differentially to C-reactive Protein, Fibromodulin, DNA, and Necrotic Cells

Sjöberg

Trouw

Clark

et al. 2007

Journal of Biological Chemistry

125

109

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Recently, a polymorphism in the complement regulator factor H (FH) gene has been associated with age-related macular degeneration. When histidine instead of tyrosine is present at position 384 in the seventh complement control protein (CCP) domain of FH, the risk for age-related macular degeneration is increased. It was recently shown that these allotypic variants of FH, in the context of a recombinant construct corresponding to CCPs 6 -8, recognize polyanionic structures differently, which may lead to altered regulation of the alternative pathway of complement. We show now that His-384, corresponding to the risk allele, binds C-reactive protein (CRP) poorly compared with the Tyr-384 form. We also found that C1q and phosphorylcholine do not compete with FH for binding to C-reactive protein. The interaction with extracellular matrix protein fibromodulin, which we now show to be mediated, at least in part, by CCP6 -8 of FH, occurs via the polypeptide of fibromodulin and not through its glycosaminoglycan modifications. The Tyr-384 variant of FH bound fibromodulin better than the His-384 form. Furthermore, we find that CCP6 -8 is able to interact with DNA and necrotic cells, but in contrast the His-384 allotype binds these ligands more strongly than the Tyr-384 variant. The variations in binding affinity of the two alleles indicate that complement activation and local inflammation in response to different targets will differ between His/His and Tyr/Tyr homozygotes.In the western world, age-related macular degeneration (AMD) 4 is the leading cause of natural blindness in the elderly (1), affecting 50 million individuals worldwide. As the mean age of the population increases it is expected that the incidence will rise even further (2). Epidemiology reveals a complex etiology with not only age but also sex, diet, and ethnic background as underlying factors for AMD predisposal. As with every multifactorial disease there are certainly also genetic predispositions. For example, C-reactive protein (CRP) levels appear to be higher in AMD patients (3), and recently attention has been drawn to a polymorphism in the factor H (FH) gene present in Caucasians (4). FH is the major soluble inhibitor of the alternative pathway of the complement system. Alternative pathway activation results from a failure to appropriately regulate the constant low level spontaneous turnover of the abundant complement component C3 to C3(H 2 O). Complement non-activating cells and other host surfaces are protected from alternative pathway complement attack through binding of FH, which is believed to have a strong affinity for polyanionic structures such as glycosaminoglycans as well as glycoproteins containing sialic acid residues (5-7). FH is therefore able to discriminate between self and non-self surfaces. FH inhibits the alternative pathway by binding C3b and reducing the formation and activity of the alternative pathway C3-convertase (C3bBb). It also accelerates the decay of this convertase and works as a cofactor for the serine proteinase fact...

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“…Fibromodulin, the most abundant member of the leucine-rich repeat protein family, has been shown to bind to type I collagen and to regulate fibrogenesis [8], and it has been also shown to be a constituent of tendons, cartilage, and sclera [33,35]. However, there are no reports on the localization and developmental changes of fibromodulin in the retina.…”

mentioning

confidence: 99%

Expression of Small Leucine-Rich Proteoglycans in the Developing Retina and Kainic Acid-Induced Retinopathy in ICR Mice

Ali

Hosaka

Uehara

2011

The Journal of Veterinary Medical Science

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ABSTRACT. The aim of this study was to determine the developmental changes of small leucine-rich proteoglycans (PGs), decorin, biglycan and fibromodulin, in ICR mouse retinas and to elucidate their role in the adult retina using kainic acid (KA)-induced retinal degeneration model. Retinas of prenatal, postnatal and adult mice were collected for histological and immunohistochemical staining to investigate the changes in distribution of these PGs. Decorin-and fibromodulin-immunostainings were diffusely distributed at prenatal and early postnatal stages and were stronger in the adult retina. However, biglycan was moderately distributed in the prenatal and early postnatal stages and was faint in the adult retina. Retinas were collected at 1, 3 and 7 days after intravitreal injection of KA. Retinas of KA injected eyes underwent shrinkage accompanied by serious damage in the inner layers. Decorin and fibromodulin were upregulated in the inner retinal layers of KA-injected eyes compared to the normal ones. Our results suggest that decorin and fibromodulin play key roles in retinal differentiation, and contribute to the retinal damage and repair process. However, biglycan may have no or only a limited role in the mouse retinal development or repair process.KEY WORDS: biglycan, decorin, fibromodulin, kainic acid, retinal development and damage.

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The small proteoglycans of cartilage matrix

Cited by 35 publications

References 110 publications

Fourier transform infrared imaging of focal lesions in Human osteoarthritic cartilage

Fourier transform infrared imaging of focal lesions in Human osteoarthritic cartilage

The Factor H Variant Associated with Age-related Macular Degeneration (His-384) and the Non-disease-associated Form Bind Differentially to C-reactive Protein, Fibromodulin, DNA, and Necrotic Cells

Expression of Small Leucine-Rich Proteoglycans in the Developing Retina and Kainic Acid-Induced Retinopathy in ICR Mice

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