Immunolocalization of Types V and XI Collagen in Cartilage Using Monoclonal Antibodies

Furuto, Donald K.; Stewart, Tod E.; Miller, Edward J.

doi:10.1016/s0934-8832(11)80218-0

Cited by 14 publications

(6 citation statements)

References 24 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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“…However, we now know that articular cartilage is an extremely complex tissue not least in its collagen composition. Three types of collagen in addition to type II, namely types VI, IX and XI are certainly present (Mayne, 1986;Eyre et al, 1987b) and types I, V and X have also been reported (Duance, 1983;Furuto et al, 1991;Gannon et al, 1991;Eyre et aI., 1992;Wardale & Duance, 1993). These are 'minor' collagens in the sense that they are present in comparatively small amounts but they may have important functions; for example, type IX collagen appears to have a role in regulating the fibril diameter of type II collagen (Wotton et al, 1988) to which it is now known to be covalently cross-linked (Eyre et al, 1987a).…”

Section: Introductionmentioning

confidence: 99%

Type III collagen in normal human articular cartilage

Wotton

Duance

1994

Histochem J

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“…Of the antibodies raised to specific regions of the N-terminal region of the α1(XI) chain only one antibody, p8, to a 20 amino-acid region, was bound by developing articular cartilage in fetal rats (Morris et al 2000); the other antibodies were bound by diaphyseal and epiphyseal cartilage. A brief report suggests that both types V and XI collagens are located in the chondrocytes of articular cartilage of mature rats (Furuto et al 1991). Identification of the cells expressing the mRNAs for these collagens supports the immunohistochemical observations.…”

Section: Discussionmentioning

confidence: 57%

“…Type V collagen is very closely related to type XI collagen and some fibrils may be heterotypic associations of α-chains from both collagens (Fichard et al 1994). Type XI collagen has not been localized in articular cartilage, although it is known to be a constituent of the matrix (Eyre et al 1987, Furuto et al 1991, Thomas et al 1994. In epiphyseal cartilage it is found throughout the matrix (Petit et al 1993).…”

Section: Introductionmentioning

confidence: 99%