Cartilage Oligomeric Matrix Protein

Lawler, Jack; Chen, Hui

doi:10.1002/0471203076.emm0181

Cited by 7 publications

(3 citation statements)

References 25 publications

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“…In a tissue-engineering context, studies using an alginate hydrogel have demonstrated that static deformational loading increased the amount of GAG lost to the medium without altering the structure of the aggrecan core protein 50 . In addition to the size of aggregates and organization of the proteoglycan network, other extracellular matrix components (e.g., type IX collagen 51 , and cartilage oligomeric matrix protein (COMP) 52,53 ), which participate in the cross-linking of the type II collagen extracellular matrix, may be differentially regulated with deformational loading and thereby influence the functional properties of the ECM. Indeed, recent studies have shown that COMP gene expression is elevated in explants and alginate disks in response to deformational loading 54,55 .…”

Section: Discussionmentioning

confidence: 99%

The role of cell seeding density and nutrient supply for articular cartilage tissue engineering with deformational loading

Mauck

Wang

Oswald

et al. 2003

Osteoarthritis and Cartilage

276

253

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Section: Discussionmentioning

confidence: 99%

The role of cell seeding density and nutrient supply for articular cartilage tissue engineering with deformational loading

Mauck

Wang

Oswald

et al. 2003

Osteoarthritis and Cartilage

276

253

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“…COMP is principally expressed not only in cartilage, tendon Abbreviations: BM, basal membrane; BMP, bone morphogenic protein; CHH, Cartilage hair hypoplasia; COMP, cartilage oligomeric matrix protein; CTS, connective tissue sheath; DP, dermal papilla; ECM, extracellular matrix; EMI, epithelial-mesenchymal interactions; HF, hair follicle(s); ORS, outer root sheath; Shh, sonic hedgehog; TGFb, transforming growth factor, beta; THBS5, thrombospondin 5; Wnt, wingless. and synovium (27,32), but also found in ligaments produced by human foreskin fibroblasts in vitro (33) and cultured human vascular smooth muscle cells (31). However, its expression has not previously been reported for normal human skin or HF.…”

Section: Introductionmentioning

confidence: 99%

“…Complex interactions of each monomer with its neighbour result in the formation of a hydrophobic pore, which can bind retinol and vitamin D (21) and interact as a linker protein with several ECM molecules (22–28) and growth factors such as TGFβ ligands (29–31). COMP is principally expressed not only in cartilage, tendon and synovium (27,32), but also found in ligaments produced by human foreskin fibroblasts in vitro (33) and cultured human vascular smooth muscle cells (31). However, its expression has not previously been reported for normal human skin or HF.…”

Section: Introductionmentioning

confidence: 99%

Cartilage oligomeric matrix protein (COMP) forms part of the connective tissue of normal human hair follicles

Schellenberger

Horland

Rosowski

et al. 2011

Experimental Dermatology

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Hair follicle cycling is driven by epithelial-mesenchymal interactions (EMI), which require extracellular matrix (ECM) modifications to control the crosstalk between key epithelial-and mesenchymal-derived growth factors and cytokines. The exact roles of these ECM modifications in hair cycle-associated EMI are still unknown. Here, we used differential microarray analysis of laser capture-microdissected human scalp hair follicles (HF) to identify new ECM components that distinguish fibroblasts from the connective tissue sheath (CTS) from those of the follicular dermal papilla (DP). These analyses provide the first evidence that normal human CTS fibroblasts are characterized by the selective in situ-transcription of cartilage oligomeric matrix protein (COMP). Following this up on the protein level, COMP was found to be hair cycle-dependent, suggesting critical role in this process: COMP is expressed during telogen and early anagen at regions of EMI and is degraded during catagen (only the CTS adjacent to the bulge remains COMP+ during catagen). Notably, COMP gene expression in vitro suggests direct correlation with the expression of TGFb2 in CTS fibroblasts. This raises the question whether COMP expression undergoes regulation by transforming growth factor, beta (TGFb) signalling. The intrafollicular COMP expression suggests to be functionally important and deserves further scrutiny in hair biology as indicated by the fact that altered COMP expression might be associated with scant fine hair in the case of some chondrodysplasia and scleroderma patients. Together these results reveal for the first time that COMP is part of the ECM and suggests its important role in normal human HF biology.

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Comparison of long-term transgene expression after non-viral and adenoviral gene transfer into primary articular chondrocytes

Dinser

Kreppel

Zaucke

et al. 2001

Histochem Cell Biol

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Different gene transfer approaches to achieve long-term transgene expression in cultured primary bovine chondrocytes were compared using enhanced green fluorescent protein (EGFP) as a reporter. Transduction with a high-capacity adenoviral vector was 82% efficient when analysed by fluorescence microscopy, while up to 42% of plasmid-transfected cells were EGFP positive with FuGene as a transfection reagent. Rapid dominant marker selection of plasmid-transfected cells was achieved in monolayer culture. With either method of gene transfer, a high proportion of the chondrocytes remained transgene positive during prolonged alginate culture. Transgene transcription in single cells was quantified with a confocal laser scanning microscope. Detection of EGFP expression was more sensitive with this method, identifying more transgene-expressing cells than conventional fluorescence microscopy. Long-term EGFP expression was higher in adenovirally transduced chondrocytes embedded in alginate as compared to plasmidtransfected cells cultured in monolayer or in alginate. Both the adenoviral and the plasmid-based approach appear suited for studies of the molecular and cellular mechanisms by which mutations in cartilage matrix proteins cause disease.

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Cartilage Oligomeric Matrix Protein

Cited by 7 publications

References 25 publications

The role of cell seeding density and nutrient supply for articular cartilage tissue engineering with deformational loading

The role of cell seeding density and nutrient supply for articular cartilage tissue engineering with deformational loading

Cartilage oligomeric matrix protein (COMP) forms part of the connective tissue of normal human hair follicles

Comparison of long-term transgene expression after non-viral and adenoviral gene transfer into primary articular chondrocytes

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