Demonstration of fibronectin in human articular cartilage by an indirect immunoperoxidase technique

Clemmensen, Inge; Hølund, Berit; Johansen, Niklas Dyrby; Andersen, Rune

doi:10.1007/bf00493284

Cited by 33 publications

(4 citation statements)

References 16 publications

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“…Experimental evidence shows that ßig-h3 is a collagen-binding matrix protein [Hashimoto et al, 1997] whose expression increases during in vitro osteoblastic differentiation of bone mar- Yates/Forbes/Glowacki [Sandberg and Vuorio, 1987;Bland and Ashurst, 1996;Paulsen and Tillmann, 1999] COL5A2 (HUMCOLVA) [Furuto et al, 1991;Bland and Ashurst, 1996] COL6A3 (NM-004369) [Poole et al, 1988] COL11A1 (NM_001854) [Furuto et al, 1991;Bland and Ashurst, 1996;Paulsen and Tillmann, 1999] Other matrix Fibrillin 1 (HSFIBRMR) [Sakai et al, 1986] Fibronectin (HSU42594) [Clemmensen et al, 1982] Laminin ·2 (NM_000426) [Dürr et al, 1996] Thrombospondin-1 (NM_003246) [Pfander et al, 2000] Versican (NM_004385) [Rosenberg et al, 1985] ßig-h3 a (NM_000358) 1…”

Section: Discussionmentioning

confidence: 99%

New Chondrocyte Genes Discovered by Representational Difference Analysis of Chondroinduced Human Fibroblasts

Yates¹,

Forbes²,

Glowacki³

2004

Cells Tissues Organs

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This report includes a review of the potential for gene expression analyses to provide new information for solving problems in skeletal repair and regeneration. It focuses on two approaches: high-throughput gene array methods and representational difference analysis (RDA). The principles underlying these methods are presented with experimental tutorials and some applications. Second, this report includes a review of results from applying both approaches to an in vitro model of postnatal chondroinduction by demineralized bone powder (DBP). Human dermal fibroblasts (hDFs) cultured with DBP acquire a chondroblast phenotype and express cartilage-specific matrix proteins after 7 days. We used cDNA macroarrays and RDA to identify the genes that were altered prior to expression of the chondroblast phenotype, i.e., after only 3 days’ culture with DBP. Using a strategy of data management and reduction based upon biological functions, we reported several functional families of genes (cytoskeletal elements, protein synthesis/trafficking, and matrix molecules and their modifiers) that are upregulated during chondroinduction of hDFs. Together with histological and biochemical evidence of the chondroblast phenotype, the gene expression patterns indicate that there are specific stages of induced chondrocyte differentiation in this experimental system. Third, this report includes a new study, in which DBP-regulated genes were used as a data base to derive new information on the cell biology of chondrocytes. The objective was to determine whether a set of genes expressed during induction of chondrocyte differentiation is also expressed by mature articular chondrocytes. Our search of the literature for 59 of the DBP-regulated genes disclosed that expression of 20 of them (33%) had been documented in mature cartilage or chondrocytes. Of the 39 genes not previously documented in cartilage, 11 were tested by RT-PCR and all were found to be expressed in freshly isolated adult human chondrocytes. This review and these new data show how the strategy of high-throughput methods and functional data reduction can expand our knowledge of chondrocyte cell biology.

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Section: Discussionmentioning

confidence: 99%

New Chondrocyte Genes Discovered by Representational Difference Analysis of Chondroinduced Human Fibroblasts

Yates¹,

Forbes²,

Glowacki³

2004

Cells Tissues Organs

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“…Articular chondrocytes are embedded in a specialized extracellular matrix (ECM) in which there is preferential pericellular localization of molecules such as fibronectin and type VI collagen1, 2. Chondrocyte–matrix interactions, via a variety of cell adhesion molecules including members of the integrin superfamily, CD44 (hyaluronan receptor), NG2/HMPG, and annexin V, are important in the regulation of chondrocyte function.…”

Section: Introductionmentioning

confidence: 99%

NG2/HMPG modulation of human articular chondrocyte adhesion to type VI collagen is lost in osteoarthritis

Midwood

Salter

2001

The Journal of Pathology

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NG2/human melanoma proteoglycan (HMPG) is a chondroitin sulphate proteoglycan (CSPG), expressed by chondrocytes in fetal and in normal and osteoarthritic (OA) adult articular cartilage. NG2/HMPG is a receptor for extracellular matrix proteins, including type VI collagen, and regulates beta1 integrin binding to fibronectin. This study was undertaken to identify whether NG2/HMPG had similar activities in human articular chondrocytes (HACs). Normal and OA adult HAC adhesion to fibronectin, type II or type VI collagen was assessed using a methylene blue assay. The requirement for integrins, NG2/HMPG, and integrin-associated signalling molecules was investigated using anti-beta1 integrin and anti-HMPG antibodies and pharmacological inhibitors of signalling molecules. The adhesion of normal and OA HACs to fibronectin, type II and type VI collagen was beta1 integrin-dependent. Normal HAC adhesion to type VI collagen was stimulated by anti-HMPG antibodies. This effect was inhibited by pertussis toxin. Anti-HMPG antibodies had no effect on OA chondrocyte adhesion to type VI collagen, or on normal and OA cell adhesion to fibronectin and type II collagen. The results show that NG2/HMPG modulates integrin-mediated interactions of normal HACs with type VI collagen. Loss of this activity may be of importance in the progression of osteoarthritis.

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“…In recent years, considerable interest has been focused on the role of these glycoproteins during various process of cellular development and differentiation. Fibronectin is known to play an important role in cell-cell, cell-extracellular matrix binding and cellular migration, and has been found to be widely distributed in plasma, the extracellular matrix of connective tissues, blood vessels, cartilage, and osseous tissues [4][5][6][7][8][9][10]. Fibronectin has been localized in demineralized bone matrix when implanted in vivo, mesenchymal cells before and during cell proliferation, newly synthesized extracellular matrix, differentiating chondrocytes, and in cottony array around osteoblasts [9,11,19].…”

Section: Introductionmentioning

confidence: 99%

Laminin and fibronectin in bone formation induced by bone morphogenetic protein (BMP) in mouse muscle tissue

1994

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Abstract:The morphological features at the light and electron microscopic level and distribution of fibronectin and laminin using immunohistochemical methods were evaluated in chondro-osteogneic tissue induced by bone morphogenetic protein (BMP) in mouse skeletal muscle. Satellite cells were seen at the muscle fibers adjacent to the site of BMP implantation 3 days after BMP-implantation. At the ultrastructuraI level, the skeletal muscle had a continuous basal lamina, satellite cells were partially enveloped by basal lamina-like structure, and fibroblast-like cells with abundant mitochondria and endoplasmic reticulum were adjacent to the myofibrils. An enhanced immunoreactivity for laminin and fibronectin was observed at the basement membrane of muscle fibers and extracellular ~natrix of neighboring connective tissue on day 3. On the 7th day, the enhanced immunoreactivity of laminin was persistent on the muscle fibers adjacent to the BMP and myoblast-like satellite cells, however, fibronectin showed decreased reaction. On the 14th day specimen, the newly formed osteo-chondroid matrix with numerous chondroid cells and osteoblasts showed positive immunoreaction for laminin and fibronectin. During the process of resorption of the induced osteoid tissue, no immunoreactivity for laminin and fibronectin was observed. An enhanced immunoreactivity of these glycoproteins during the early stages of BMP induced chondro-ossification suggests that they play an important role in the differentiation of myo-fibroblasts and organization and integration of ground substances of connective tissue and chondro-osseous matrix.

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Demonstration of fibronectin in human articular cartilage by an indirect immunoperoxidase technique

Cited by 33 publications

References 16 publications

New Chondrocyte Genes Discovered by Representational Difference Analysis of Chondroinduced Human Fibroblasts

New Chondrocyte Genes Discovered by Representational Difference Analysis of Chondroinduced Human Fibroblasts

NG2/HMPG modulation of human articular chondrocyte adhesion to type VI collagen is lost in osteoarthritis

Laminin and fibronectin in bone formation induced by bone morphogenetic protein (BMP) in mouse muscle tissue

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