Interaction of Biglycan with Type I Collagen

Schönherr, Elke; Witsch‐Prehm, Petra; Harrach, B.; Robenek, Horst; Rauterberg, Jürgen; Kresse, Hans

doi:10.1074/jbc.270.6.2776

Cited by 353 publications

(226 citation statements)

References 42 publications

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“…The accumulation of biglycan might interfere with proper collagen network remodeling as decorin and biglycan could compete for binding on collagen type I. 28 We observed earlier expression of Sox 9 and collagen type II in healing tendon fibroblasts and this preceded their expression in the chondrocyte-like cells and ossified area. The alteration of ECM composition and growth factors after injury might favor erroneous chondrogenic and osteogenic differentiation of tendon progenitor cells to chondrocytes and osteoblasts, respectively, and negatively affect the mechanical property of the regenerated tissue.…”

mentioning

confidence: 57%

Ectopic chondro‐ossification and erroneous extracellular matrix deposition in a tendon window injury model

Lui

Cheuk

Lee

et al. 2011

Journal Orthopaedic Research

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The acquisition of chondro-osteogenic phenotypes and erroneous matrix deposition may account for poor tissue quality after acute tendon injury. We investigated the presence of chondrocyte phenotype, ossification, and the changes in the expression of major collagens and proteoglycans in the window wound in a rat patellar tendon window injury model using histology, von Kossa staining and immunohistochemistry of Sox 9, major collagens, and proteoglycans. Our results showed that the repair tissue did not restore to normal after acute injury. Ectopic chondrogenesis was observed in 33% of samples inside wound at week 4 while ectopic ossification surrounded by chondrocyte-like cells were observed in the window wound in 50% of samples at week 12. There was sustained expression of biglycan and reduced expression of aggrecan and decorin in the tendon matrix in the repair tissue. The erroneous deposition of extracellular matrix and ectopic chondro-ossification in the repair tissue, both might influence each other, might account for the poor tissue quality after acute injury. Higher expression of biglycan and aggrecan were observed in the ectopic chondro-ossification sites in the repair tissue, suggesting that they might have roles in ectopic chondro-osteogenesis. Tendons regenerate and repair slowly and inefficiently after injury. The crimp pattern of collagen fibers and fibrils was smaller than that of the control 1 and the regenerated fibrotic scar tissue could not return to its original mechanical strength for a long time after injury. 1-3 It was known that collagens and proteoglycans in the extracellular matrix (ECM) have roles in modulating the activities of tenocytes in addition to their structural roles. 4 Despite studies about the tendon healing process, there is still limited and inconsistent understanding about the change in biochemical composition of ECM after tendon injury 5-7 and how does the ECM regulate cellular functions. On the other hand, ectopic ossification after midpoint tenotomy of rat or mouse Achilles tendon has been reported. [8][9][10][11][12] Clinical studies have occasionally reported ectopic calcification after Achilles tendon rupture 13,14 as well as calcification and tendinopathic-like changes in patellar tendon donor site after anterior cruciate ligament (ACL) reconstruction. [15][16][17][18][19][20][21] We hypothesized that chondro-osteogenesis and change in the ECM composition of the repair tissue after acute tendon injury might contribute to the poor tissue quality. This study therefore aimed to examine the presence of chondrocyte phenotype and ossification inside the window wound of the patellar tendon. The spatial-temporal changes of major collagens including collagen types I and III and major proteoglycans including decorin, biglycan, fibromodulin, and aggrecan in the window wound after tendon injury were also investigated. METHODOLOGY Tendon Injury ModelThis study was approved by the Animal Research Ethics Committee of the authors' institution. Eighteen SpragueDawley male ad...

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confidence: 57%

Ectopic chondro‐ossification and erroneous extracellular matrix deposition in a tendon window injury model

Lui

Cheuk

Lee

et al. 2011

Journal Orthopaedic Research

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“…[52][53][54] The interaction between decorin or biglycan and collagen type I has been studied extensively in vitro and in vivo. [55][56][57][58] Both proteoglycans colocalize with collagen types I and III in atherosclerotic plaques. 59 Furthermore, decorin and biglycan have chondroitin/dermatan sulfate GAG chains that can potentially bind both LDL and snpPLA 2 .…”

Section: Discussionmentioning

confidence: 99%

Ultrastructural Localization of Secretory Type II Phospholipase A ₂ in Atherosclerotic and Nonatherosclerotic Regions of Human Arteries

Romano¹,

Romano²,

Björkerud³

et al. 1998

ATVB

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Abstract-We recently reported on the immunolocalization of type II secretory nonpancreatic phospholipase A 2 (snpPLA 2 ) in human atherosclerotic lesions. In the present study, we present data on the distribution and ultrastructural localization of snpPLA 2 in adjacent nonatherosclerotic and atherosclerotic regions of human arteries. Electron microscopy (EM) of immunogold labeling techniques with a monoclonal antibody was used to analyze arterial tissue. The human specimens analyzed were obtained from autopsy and surgery cases. The results with EM showed a stronger snpPLA 2 immunoreactivity in regions of arteries with atherosclerotic lesions than in regions without lesions from the same individual. snpPLA 2 immunoreactivity was stronger in the arterial intima of atherosclerotic than of nonatherosclerotic tissue. EM-immunogold examination revealed that the majority of snpPLA 2 was localized along the extracellular matrix, associated with collagen fibers and other extracellular matrix structures. Intracellular snpPLA 2 was observed in electron-dense vesicles in intimal cells. snpPLA 2 was also found in contact with large, extracellular lipid droplets. These results support the hypothesis that extracellular snpPLA 2 is localized at sites where it may hydrolyze phospholipids from lipoproteins and lipid aggregates retained in the extracellular matrix of the arterial wall. This may be a mechanism for in situ release of proinflammatory lipids, free fatty acids, and lysophosphatidylcholine in regions of apolipoprotein B accumulation, which are abundant in atherosclerotic lesions. (Arterioscler Thromb Vasc Biol. 1998;18:519-525.)

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“…The answers still are incomplete, but it is known that collagen fibrils in situ comprise not only several types of collagens (1,3,13,14) but also additional macromolecules (4,(15)(16)(17)(18). As shown in animals with deficiencies in small leucine-rich proteins, fusion of fibrils into irregularly shaped aggregates is often observed (19,20) suggesting a decisive role of small leucine-rich proteins in fibrillar organizations at the level of tissue architecture.…”

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Macromolecular Specificity of Collagen Fibrillogenesis

Hansen

Brückner

2003

Journal of Biological Chemistry

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Suprastructures of the extracellular matrix, such as banded collagen fibrils, microfibrils, filaments, or networks, are composites comprising more than one type of macromolecule. The suprastructural diversity reflects tissue-specific requirements and is achieved by formation of macromolecular composites that often share their main molecular components alloyed with minor components. Both, the mechanisms of formation and the final macromolecular organizations depend on the identity of the components and their quantitative contribution. Collagen I is the predominant matrix constituent in many tissues and aggregates with other collagens and/or fibril-associated macromolecules into distinct types of banded fibrils. Here, we studied co-assembly of collagens I and XI, which co-exist in fibrils of several normal and pathologically altered tissues, including fibrous cartilage and bone, or osteoarthritic joints. Immediately upon initiation of fibrillogenesis, the proteins co-assembled into alloy-like stubby aggregates that represented efficient nucleation sites for the formation of composite fibrils. Propagation of fibrillogenesis occurred by exclusive accretion of collagen I to yield composite fibrils of highly variable diameters. Therefore, collagen I/XI fibrils strikingly differed from the homogeneous fibrillar alloy generated by collagens II and XI, although the constituent polypeptides of collagens I and II are highly homologous. Thus, the mode of aggregation of collagens into vastly diverse fibrillar composites is finely tuned by subtle differences in molecular structures through formation of macromolecular alloys.Extracellular matrix aggregates, despite their functional and morphological diversity, often contain the same type of macromolecules as their major constituent. In tendons, for example, large and strongly banded fibrils of variable width are aggregated into bundles that resist extreme tensile forces in one dimension. By contrast, thin fibrils with uniform diameter and spacing are organized into orthogonal sheets forming the translucent corneal stromal matrix that withstands high traction in two dimensions. However, the same protein, i.e. collagen I, is the quantitatively predominant component in both suprastructures (1, 2). The major cartilage collagen is type II, but this protein, too, is common to fibrils with different structures and functions (3, 4). Finally, collagens I and II occur together in fibrocartilage (5), a tissue characterized by a high resistance to both compressive and tensile forces and that contains fibrous bundles in addition to an amorphous extrafibrillar matrix rich in proteoglycans.Collagens I and II are very similar in their molecular structure. They both contain three polypeptides with a central sequence of 1014 amino acids in which strictly every third residue is glycine. In addition, these glycine residues are frequently preceded by hydroxyproline and/or followed by proline. The (Gly-Xaa-Yaa) n sequences are flanked at both ends by short non-periodic sequences, called telopeptide...

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Interaction of Biglycan with Type I Collagen

Cited by 353 publications

References 42 publications

Ectopic chondro‐ossification and erroneous extracellular matrix deposition in a tendon window injury model

Ectopic chondro‐ossification and erroneous extracellular matrix deposition in a tendon window injury model

Ultrastructural Localization of Secretory Type II Phospholipase A ₂ in Atherosclerotic and Nonatherosclerotic Regions of Human Arteries

Macromolecular Specificity of Collagen Fibrillogenesis

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Interaction of Biglycan with Type I Collagen

Cited by 353 publications

References 42 publications

Ectopic chondro‐ossification and erroneous extracellular matrix deposition in a tendon window injury model

Ectopic chondro‐ossification and erroneous extracellular matrix deposition in a tendon window injury model

Ultrastructural Localization of Secretory Type II Phospholipase A 2 in Atherosclerotic and Nonatherosclerotic Regions of Human Arteries

Macromolecular Specificity of Collagen Fibrillogenesis

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Ultrastructural Localization of Secretory Type II Phospholipase A ₂ in Atherosclerotic and Nonatherosclerotic Regions of Human Arteries