The modulation of collagen fibril assembly and its structure by decorin: An electron microscopic study

Iwasaki, S.; Hosaka, Yoshinao Z.; Iwasaki, Tomohito; Yamamoto, Katsuhiro; Nagayasu, Aya; Ueda, Hiromi; Kokai, Yasuo; Takehana, Kazushige

doi:10.1679/aohc.71.37

Cited by 40 publications

(40 citation statements)

References 33 publications

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“…52 The significant and consistent enhancement of DEC gene expression by exogenous CTGF confirms our speculation because of DEC's role in assisting collagen fibril assembly. 53,54 In the case of ELA, the activity of ELA post-translational enzymes (for example, lysal oxidase) may have been activated by CTGF in our particular culture system. 52 In addition to structural proteins, amorphous GAG molecules in connective tissues establish a highly hydrated network facilitating the rapid diffusion of nutrients, metabolites, and hormones.…”

Section: Discussionmentioning

confidence: 99%

Controlling the Fibroblastic Differentiation of Mesenchymal Stem Cells Via the Combination of Fibrous Scaffolds and Connective Tissue Growth Factor

Tong

Sant

Khademhosseini

et al. 2011

Tissue Engineering Part A

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Controlled differentiation of multi-potent mesenchymal stem cells (MSCs) into vocal fold-specific, fibroblast-like cells in vitro is an attractive strategy for vocal fold repair and regeneration. The goal of the current study was to define experimental parameters that can be used to control the initial fibroblastic differentiation of MSCs in vitro. To this end, connective tissue growth factor (CTGF) and micro-structured, fibrous scaffolds based on poly(glycerol sebacate) (PGS) and poly(e-caprolactone) (PCL) were used to create a three-dimensional, connective tissue-like microenvironment. MSCs readily attached to and elongated along the microfibers, adopting a spindleshaped morphology during the initial 3 days of preculture in an MSC maintenance medium. The cell-laden scaffolds were subsequently cultivated in a conditioned medium containing CTGF and ascorbic acids for up to 21 days. Cell morphology, proliferation, and differentiation were analyzed collectively by quantitative PCR analyses, and biochemical and immunocytochemical assays. F-actin staining showed that MSCs maintained their fibroblastic morphology during the 3 weeks of culture. The addition of CTGF to the constructs resulted in an enhanced cell proliferation, elevated expression of fibroblast-specific protein-1, and decreased expression of mesenchymal surface epitopes without markedly triggering chondrogenesis, osteogenesis, adipogenesis, or apoptosis. At the mRNA level, CTGF supplement resulted in a decreased expression of collagen I and tissue inhibitor of metalloproteinase 1, but an increased expression of decorin and hyaluronic acid synthesase 3. At the protein level, collagen I, collagen III, sulfated glycosaminoglycan, and elastin productivity was higher in the conditioned PGS-PCL culture than in the normal culture. These findings collectively demonstrate that the fibrous mesh, when combined with defined biochemical cues, is capable of fostering MSC fibroblastic differentiation in vitro.

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Section: Discussionmentioning

confidence: 99%

Controlling the Fibroblastic Differentiation of Mesenchymal Stem Cells Via the Combination of Fibrous Scaffolds and Connective Tissue Growth Factor

Tong

Sant

Khademhosseini

et al. 2011

Tissue Engineering Part A

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“…The reasons for these differences between the chicken and crow are unknown. Some proteoglycans, which are involved in the process of the assembly and formation of collagen fibrils [2,16,28,29], may be different quantitatively and qualitatively between these two species.…”

Section: Discussionmentioning

confidence: 99%

“…Light scattering in the cornea increases if order in the spatial arrangement of the fibrils is destroyed, or if fibril diameters and fibril number density increase [28]. The process of the assembly and formation of collagen fibrils involves the activity of some proteoglycans [2,16,28,29].…”

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confidence: 99%

Microstructure Characteristics of the Cornea in Birds and Mammals

Tsukahara

Tani

Lee

et al. 2010

The Journal of Veterinary Medical Science

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ABSTRACT. In this study, the microstructure of the cornea was compared among chickens (Gallus gallus), jungle crows (Corvus macrorhynchos), rats (Rattus norvegicus) and rabbits (Oryctolagus cuniculus). The density of keratocytes in the mammals was over 3 times that in the birds. The size of the keratocytes in the birds and rat were significantly lower than those in the rabbit. Using scanning and transmission electron microscopy, the bundles of collagen fibers in the birds were found to be well arranged, while those in the mammals were arranged randomly. The collagen lamellae of the birds were significantly thicker than those of the mammals, and the numbers of collagen lamellae in the birds were significantly smaller than in the mammals. The center-to-center distances between the collagen fibrils of the chicken and rabbit were significantly larger than those of the crow and rat. The densities of collagen fibrils in the chicken and rabbit were significantly less than those of the crow and rat.

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“…Furthermore, the amount and types of proteoglycans could affect the arrangement and density of collagen fibrils [8,9]. Collagen from both corneal portions was therefore extracted and sitedependent difference in the composition ratio of collagen molecular species was determined.…”

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confidence: 99%

Site-Dependent Differences in Collagen Lamellae in the Corneal Substantia Propria of Beagle Dogs

Nagayasu

Hirayanagi

Tanaka

et al. 2009

The Journal of Veterinary Medical Science

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ABSTRACT. The fine structure in the center and periphery of the cornea of 16 beagle dogs were characterized and compared. The central cornea (about 540 m) was apparently thinner than the peripheral cornea (about 720 m). Thickness ratios of the corneal substantia propria to the entire cornea were approximately 86% in both portions. In addition, number of collagen lamellae, collagen fibril diameter, and collagen fibril index of the central substantia propria are different from those of the periphery (253 vs 236 lamellae, 29.1 vs 32.0 nm, and 39.0 vs 41.6%, respectively). These differences are thought to be due to site-dependent accumulation of proteoglycans (decorin and lumican) which are responsible for production of thin fibrils. The central portion with higher proteoglycans would have abundant thin fibrils with less slippage but better elasticity to buffer against the direct impact of intraocular pressure on the cornea. In contrast, thick fibrils in the peripheral substantia propria would contribute to the maintenance of tensile strength acting on the transition zone between the cornea and sclera.KEY WORDS: canine, collagen fibrils, collagen lamellae, cornea, corneal substantia propria.J. Vet. Med. Sci. 71(9): 1229-1231, 2009 The general structure of the cornea has been described in many textbooks [1,6,17,18]. With the recent development of technology in regenerative medicine, biomedical studies on the cornea of dogs and other animals have been increasing [11,19,21]. An understanding of the fine structure of the normal canine cornea is essential for the development of corneal tissue engineering for treatment of corneal diseases. The fine structure of the corneal substantia propria, which occupies approximately 90% of the entire thickness of the cornea, has not yet been completely determined. The objective of this study was to characterize and compare the fine structures in the central portion and peripheral portion of the normal corneal substantia propria of beagle dogs.The use of experimental animals was approved by the Ethics Committee of Rakuno Gakuen University, Japan, and compliance with the NIH Guide for the Care and Sixteen male beagles at the age of 16.8  7.0 months with body weight of 10.7  1.1 kg were used. After anesthesia with 25 mg/kg of pentobartital sodium, IV (Kyoritsu Seiyaku Corporation, Tokyo, Japan), these animals were euthanized by exsanguination. Then, the left eyeball was surgically removed from each dog. Twelve eyeballs were perfused with 10% formalin, and bisected in the median plane by using a razor blade for measurements of central and peripheral corneal thicknesses at ten sites for each sample. Four eyeballs were fixed in 3.0% glutaraldehyde in 0.1 M phosphate buffer (pH 7.4) for 24 hr at room temperature. Then, 2-mm 2 corneal samples were excised from the center and periphery of the eyeballs and post-fixed in 1.0% osmium tetroxide in 0.1 M phosphate buffer for 1 hr at room temperature. Thereafter, the samples were washed with 0.1 M phosphate buffer (pH 7.4), dehydrated in a grad...

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The modulation of collagen fibril assembly and its structure by decorin: An electron microscopic study

Cited by 40 publications

References 33 publications

Controlling the Fibroblastic Differentiation of Mesenchymal Stem Cells Via the Combination of Fibrous Scaffolds and Connective Tissue Growth Factor

Controlling the Fibroblastic Differentiation of Mesenchymal Stem Cells Via the Combination of Fibrous Scaffolds and Connective Tissue Growth Factor

Microstructure Characteristics of the Cornea in Birds and Mammals

Site-Dependent Differences in Collagen Lamellae in the Corneal Substantia Propria of Beagle Dogs

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