Modulation of collagen fibrillogenesis by tenascin-X and type VI collagen

Minamitani, Takeharu; Ikuta, Tomoki; Saito, Yoshinari; Takebe, Gen; Sato, Mami; Sawa, Hirofumi; Nishimura, Takanori; Nakamura, Fumio; Takahashi, Kazuhiko; Ariga, Hiroyoshi; Matsumoto, K.

doi:10.1016/j.yexcr.2004.04.030

Cited by 108 publications

(93 citation statements)

References 46 publications

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“…First, Lethias et al cloned bovine TNX as a fibril-associated protein in dermal collagen preparations [31]. Second, recent studies suggest that native TNX binds collagen in vitro and the native protein increased both the rate and extent of fibril formation [32]. Third, Lethias showed that TNX is also capable of binding decorin, a small leucine-rich proteoglycan that binds collagen avidly and regulates fibrillogenesis [33].…”

Section: Tenascin-x and The Collagen Fibrilmentioning

confidence: 99%

Tenascin‐X, collagen, elastin, and the Ehlers–Danlos syndrome

Bristow

Carey

Egging

et al. 2005

American J of Med Genetics Pt C

105

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Francisco. He was involved in the original cloning of tenascin-X and has spent the past decade using genetic approaches to understand the functions of tenascins in disease.2. William Carey is a neonatologist and Instructor in Pediatrics at the University of California, San Francisco. He is studying the role of tenascin-X and tenascin-C in pathologic fibrosis. Tenascin-X serves as a compelling example of how human "experiments of nature" can guide us to an understanding of genes whose function may not be evident from their sequence or in vitro studies of their encoded proteins.

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Section: Tenascin-x and The Collagen Fibrilmentioning

confidence: 99%

Tenascin‐X, collagen, elastin, and the Ehlers–Danlos syndrome

Bristow

Carey

Egging

et al. 2005

American J of Med Genetics Pt C

105

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“…Tn-X localization in both species was confined to the interstitial connective tissue in CP. Tn-X directly binds to type I collagen and regulates type VI collagen for collagen fibrillogenesis (Mao et al, 2002;Minamitani et al, 2004). Collagen fibril in the CP connective tissue has been clearly observed in monkeys (Ling 1981).…”

Section: Discussionmentioning

confidence: 99%

“…These symptoms are caused by the occurrence of abnormal irregular collagen fibres. Tn-X plays a role in collagen fibrillogenesis by directly binding to collagen (Mao et al 2002;Minamitani et al 2004). Mice with a Tn-X deficiency also showed skin symptoms comparable with those of EDS (Mao et al, 2002).…”

mentioning

confidence: 99%

Identification of the novel localization of tenascinX in the monkey choroid plexus and comparison with the mouse

Imura¹,

Sato²

2009

Eur J Histochem

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Tenascin-X (Tn-X) belongs to the tenascin family of glycoproteins and has been reported to be significantly associated with schizophrenia in a single nucleotide polymorphism analysis in humans. This finding indicates an important role of Tn-X in the central nervous system (CNS). However, details of Tn-X localization are not clear in the primate CNS. Using immunohistochemical techniques, we found novel localizations of Tn-X in the interstitial connective tissue and around blood vessels in the choroid plexus (CP) in macaque monkeys. To verify the reliability of Tn-X localization, we compared the Tn-X localization with the tenascin-C (Tn-C) localization in corresponding regions using neighbouring sections. Localization of Tn-C was not observed in CP. This result indicated consistently restricted localization of Tn-X in CP. Comparative investigations using mouse tissues showed equivalent results. Our observations provide possible insight into specific roles of Tn-X in CP for mammalian CNS function.

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“…Associated with fibrotic tissues is the increase in collagen type VI and is considered as an early marker for tissue fibrosis (Specks et.al, 1995;Hatamochi et.al., 1996;Gerling et.al, 1997;Groma 1998;Zeichen et.al., 1999). Increase in collagen VI has also been proposed to increase the rate of collagen type I fibril formation (Harumiya et al, 2002;Minamitani et al, 2004;), result in loss of elastic properties (Hatamochi et al, 1996) and contribute to migration of glioblastoma cells . Elevated IOP models of glaucoma have demonstrated, the deposition of collagen I and VI at the optic nerve head to be an early event and are correlated linearly to degree of IOP-induced injury (Johnson et al, 2000;Guo et al, 2005;Morrison et al, 2005;Johnson et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

Endothelin-1 mediated regulation of extracellular matrix collagens in cells of human lamina cribrosa

Rao

Krishnamoorthy

Yorio

2008

Experimental Eye Research

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Endothelin-1(ET-1), a potent vaso-active peptide, mediates extracellular matrix regulation resulting in an increase in collagen deposition in various cell types and tissues and has been proposed to play a key role in glaucoma pathology. The role of ET-1 in the regulation of extracellular matrix collagens at the level of optic nerve head is not known. In this study we have examined the role of ET-1 in extracellular matrix collagen regulation in primary cultures of human lamina cribrosa cells. Our hypothesis is that ET-1 increases remodeling of the ECM of cells of the lamina cribrosa. Such actions could contribute to the development of optic neuropathy. QPCR analysis revealed that ET-1 mediated an increase in mRNA levels of collagen type I alpha 1 and collagen type VI alpha 1 chains at all doses of ET-1 with a significant increase at 1nM and 10nM concentration in LC cells. A dose dependent increase in collagen type I and type VI protein deposition and secretion was also observed by Western blot in response to ET-1 and was significant at 10nM and 100nM concentrations of ET-1. ET-1 increased the [ 3 H] proline uptake in LC cells suggesting that ET-1 contributed to an increase in total collagen synthesis in LC cells. ET-1 -mediated increase in collagen type I, type VI and total collagen synthesis was significantly blocked by the ET A receptor antagonist, BQ610, as well as with the ET B receptor antagonist, BQ788, suggesting the involvement of both receptor subtypes in ET-1 mediated collagen synthesis in LC cells. These results suggest that ET-1 regulates extra cellular matrix-collagen synthesis in LC cells and may contribute to ECM remodeling at the level of LC of POAG subjects who have elevated plasma and aqueous humor levels of endothelin-1.

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Modulation of collagen fibrillogenesis by tenascin-X and type VI collagen

Cited by 108 publications

References 46 publications

Tenascin‐X, collagen, elastin, and the Ehlers–Danlos syndrome

Tenascin‐X, collagen, elastin, and the Ehlers–Danlos syndrome

Identification of the novel localization of tenascinX in the monkey choroid plexus and comparison with the mouse

Endothelin-1 mediated regulation of extracellular matrix collagens in cells of human lamina cribrosa

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