Tyrosine-rich acidic matrix protein (TRAMP) accelerates collagen fibril formation in vitro.

Macbeath, Jonathan R.E.; Shackleton, D. R.; Hulmes, David J.S.

doi:10.1016/s0021-9258(19)36588-3

Cited by 62 publications

(9 citation statements)

References 62 publications

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“…The cell adhesion activity of dermatopontin is completely inhibited by intact small dermatan sulfate proteoglycans (decorin and biglycan), but not by chondroitin sulfate/keratan sulfate proteoglycans (Lewandowska et al, 1991). Furthermore, dermatopontin accelerates small diameter collagen assembly (MacBeath et al, 1993), while decorin markedly delays fibril formation (Vogel et al, 1984). These findings suggest that the two molecules may help regulate the assembly and turnover of collagen in the extracellular matrix through their diverse effect.…”

Section: Discussionmentioning

confidence: 96%

Dermatopontin Expression is Decreased in Hypertrophic Scar and Systemic Sclerosis Skin Fibroblasts and is Regulated by Transforming Growth Factor-β1, Interleukin-4, and Matrix Collagen

Kuroda

Okamoto

Shinkai³

1999

Journal of Investigative Dermatology

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Dermatopontin is a recently discovered extracellular matrix protein with proteoglycan and cell-binding properties and is assumed to play important roles in cell-matrix interactions and matrix assembly. In this study we examined the expression of dermatopontin mRNA and protein in skin fibroblast cultures from patients with hypertrophic scar and patients with systemic sclerosis. Dermatopontin mRNA and protein levels were reduced in fibroblast cultures from hypertrophic scar lesional skin compared with fibroblasts from normal skin of the same hypertrophic scar patient. Fibroblast cultures from systemic sclerosis patient involved skin also showed significantly reduced expression of dermatopontin compared with normal skin fibroblasts from healthy individuals. We also investigated the effects of cytokines and matrix collagen on dermatopontin expression in normal cultured fibroblasts. Transforming growth factor-beta1 increased dermatopontin mRNA and protein levels, while interleukin-4 reduced dermatopontin expression. Substrate coated with type I collagen reduced dermatopontin mRNA levels, the reduction being more prominent in three-dimensional collagen matrices. Our results suggest that the decreased expression of dermatopontin is associated with the pathogenesis of fibrosis in hypertrophic scar and systemic sclerosis, and that the effect of the cytokines and matrix collagen on dermatopontin may have important implications for skin fibrosis.

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Section: Discussionmentioning

confidence: 96%

Dermatopontin Expression is Decreased in Hypertrophic Scar and Systemic Sclerosis Skin Fibroblasts and is Regulated by Transforming Growth Factor-β1, Interleukin-4, and Matrix Collagen

Kuroda

Okamoto

Shinkai³

1999

Journal of Investigative Dermatology

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“…A number of PGs affect collagen ®bril formation, which has been studied extensively (Vogel, 1994). Although most PGs delay the formation of collagen ®brils, DPT was observed to accelerate ®bril formation when the kinetics of ®bril formation were monitored by turbidity at 313 nm (MacBeath et al, 1993). These ®ndings, taken together, suggest that DPT would accelerate axial growth more extensively to form thinner ®brils in the deep dermis.…”

Section: Discussionmentioning

confidence: 99%

“…DPT promotes cell attachment and cytoplasmic spreading of dermal ®broblasts where, it is assumed, adhesion activity is mediated by cell surface integrin receptors (Lewandowska et al, 1991). Furthermore, addition of puri®ed DPT accelerated collagen ®bril formation in vitro (MacBeath et al, 1993). Therefore, we expected DPT to be involved in the process of collagen ®brillogenesis in vivo.…”

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confidence: 98%

Targeted Disruption of Dermatopontin Causes Abnormal Collagen Fibrillogenesis

Takeda

Utani

et al. 2002

Journal of Investigative Dermatology

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Gene targeting of a member of small leucine-rich repeat proteoglycans demonstrates that collagen fibrillogenesis is mediated by a set of extracellular matrix components, which interact with collagen. Collagen-associated protein dermatopontin knockout mice were generated in order to analyze the biologic involvement of dermatopontin in the formation of collagen fibrils. Although dermatopontin-null mice did not exhibit any obvious anatomical abnormality, skin elasticity was increased. Skin tensile tests revealed that the initial elastic modulus was 57% lower in dermatopontin-null mice than in wild-type mice, and that maximum tensile strength was similar. Remarkably, light microscopy study showed a significant decrease in the relative thickness of the dermis in dermatopontin-null mice compared with wild-type mice (45.2 +/- 3.09% and 57.8 +/- 4.25%, respectively). The skin collagen content was 40% lower in dermatopontin-null than in wild-type mice. Collagen fibrils in dermatopontin-null mice showed a great variety in diameter and irregular contours under the electron microscope. These data indicate that dermatopontin plays a critical role in elasticity of skin and collagen accumulation attributed to collagen fibrillogenesis in vivo.

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“…Interestingly, some accessory molecules function as modulators that regulate the early steps in the assembly of collagen monomers to fibrils. For example, it has been found that extracellular matrix proteins, such as the tyrosine-rich acidic matrix protein (18) and the cartilage oligomeric matrix protein, 6 accelerate the formation of collagen fibrils from monomers in vitro. Other molecules have the opposite effect and slow down fibril formation in vitro (e.g.…”

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confidence: 99%

Chondroitin Sulfate Perlecan Enhances Collagen Fibril Formation

Kvist

Johnson

Mörgelin

et al. 2006

Journal of Biological Chemistry

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Inactivation of the perlecan gene leads to perinatal lethal chondrodysplasia. The similarity to the phenotypes of the Col2A1 knock-out and the disproportionate micromelia mutation suggests perlecan involvement in cartilage collagen matrix assembly. We now present a mechanism for the defect in collagen type II fibril assembly by perlecan-null chondrocytes. Cartilage perlecan is a heparin sulfate or a mixed heparan sulfate/chondroitin sulfate proteoglycan. The latter form binds collagen and accelerates fibril formation in vitro, with more defined fibril morphology and increased fibril diameters produced in the presence of perlecan. Interestingly, the enhancement of collagen fibril formation is independent on the core protein and is mimicked by chondroitin sulfate E but neither by chondroitin sulfate D nor dextran sulfate. Furthermore, perlecan chondroitin sulfate contains the 4,6-disulfated disaccharides typical for chondroitin sulfate E. Indeed, purified glycosaminoglycans from perlecan-enriched fractions of cartilage extracts contain elevated levels of 4,6-disulfated chondroitin sulfate disaccharides and enhance collagen fibril formation. The effect on collagen assembly is proportional to the content of the 4,6-disulfated disaccharide in the different cartilage extracts, with growth plate cartilage glycosaminoglycan being the most efficient enhancer. These findings demonstrate a role for perlecan chondroitin sulfate side chains in cartilage extracellular matrix assembly and provide an explanation for the perlecan-null chondrodysplasia.

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Tyrosine-rich acidic matrix protein (TRAMP) accelerates collagen fibril formation in vitro.

Cited by 62 publications

References 62 publications

Dermatopontin Expression is Decreased in Hypertrophic Scar and Systemic Sclerosis Skin Fibroblasts and is Regulated by Transforming Growth Factor-β1, Interleukin-4, and Matrix Collagen

Dermatopontin Expression is Decreased in Hypertrophic Scar and Systemic Sclerosis Skin Fibroblasts and is Regulated by Transforming Growth Factor-β1, Interleukin-4, and Matrix Collagen

Targeted Disruption of Dermatopontin Causes Abnormal Collagen Fibrillogenesis

Chondroitin Sulfate Perlecan Enhances Collagen Fibril Formation

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