Antisense Suppression of Collagen VI Synthesis Results in Reduced Expression of Collagen I in Normal Human Osteoblast-like Cells

Harumiya, Satoru; Gibson, Mark; Koshihara, Yasuko

doi:10.1271/bbb.66.2743

Cited by 21 publications

(21 citation statements)

References 22 publications

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“…Antisense suppression of collagen VI synthesis in human osteoblast-like cells results in reduced expression of type I collagen, suggesting that type VI collagen may regulate type I collagen expression in osteoblasts in vitro (Harumiya et al 2002). Some literature from cultured fibroblast studies also indicates that type VI collagen may mediate the three dimensional organization of fibronectin (Sabatelli et al 2002); this work used fibroblasts from Col6a1 mutant mice.…”

Section: Discussionmentioning

confidence: 96%

Morphologic complexity of the pericellular matrix in the annulus of the human intervertebral disc

Ingram

Hanley

2007

Biotechnic & Histochemistry

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The pericellular region of the extracellular matrix (ECM) contains collagens, proteoglycans and other noncollagenous matrix proteins. Although such specialized pericellular ECM has been well studied in articular cartilage, little is known about the pericellular matrix in the disc. In the study reported here, pericellular matrix was studied in annulus tissue from 52 subjects ranging in age from 17-74 years. In aging/degenerating intervertebral discs, cells were identified that formed a distinctive cocoon of encircling pericellular ECM. Immunohistochemical studies identified types I, II, III and VI collagen in these pericellular sites with diverse morphological features. Similar types of changes in the pericellular matrix were observed in both surgical specimens and control donor discs. Results indicate the need for future studies to address why such specialized matrix regions form around certain disc cells and to determine the consequences of these unusual matrix regions on annular lamellar organization and function.

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Section: Discussionmentioning

confidence: 96%

Morphologic complexity of the pericellular matrix in the annulus of the human intervertebral disc

Ingram

Hanley

2007

Biotechnic & Histochemistry

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“…Collagen I comprises 90-95% of the organic matrix of bone, (Datta et al, 2006), is absolutely essential for bone formation (Plotkin, 2004), and associates tightly with collagen VI. Collagen VI is necessary for collagen I production in osteoblast like cells (Harumiya et al, 2002) and interlukin-4-dependent mineralization of human periosteal cells (Ishibashi et al, 1999). Likewise fibronectin, which supports attachment and spreading of hMSC and osteoblasts (Salasznyk et al, 2004b;Ogura et al, 2004;Pistone et al, 1996), is secreted by osteoblasts early in development, and may act to help organize the osteoid matrix by binding to collagen I in mature bone tissue (Nordahl et al, 1995).…”

Section: Discussionmentioning

confidence: 99%

Laminin-5 activates extracellular matrix production and osteogenic gene focusing in human mesenchymal stem cells

et al. 2007

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We recently reported that laminin-5, expressed by human mesenchymal stem cells (hMSC), stimulates osteogenic gene expression in these cells in the absence of any other osteogenic stimulus. Here we employ two dimensional liquid chromatography and tandem mass spectrometry, along with the Database for Annotation, Visualization and Integrated Discovery (DAVID), to obtain a more comprehensive profile of the protein (and hence gene) expression changes occurring during laminin-5-induced osteogenesis of hMSC. Specifically, we compare the protein expression profiles of undifferentiated hMSC, hMSC cultured on laminin-5 (Ln-5 hMSC), and fully differentiated human osteoblasts (hOST) with profiles from hMSC treated with well-established osteogenic stimuli (collagen I, vitronectin, or dexamethazone). We find a marked reduction in the number of proteins (e.g., those involved with calcium signaling and cellular metabolism) expressed in Ln-5 hMSC compared to hMSC, consistent with our previous finding that hOST express far fewer proteins than do their hMSC progenitors, a pattern we call "osteogenic gene focusing." This focused set, which resembles an intermediate stage between hMSC and mature hOST, mirrors the expression profiles of hMSC exposed to established osteogenic stimuli and includes osteogenic extracellular matrix proteins (collagen, vitronectin) and their integrin receptors, calcium signaling proteins, and enzymes involved in lipid metabolism. These results provide direct evidence that laminin-5 alone stimulates global changes in gene/protein expression in hMSC that lead to commitment of these cells to the osteogenic phenotype, and that this commitment correlates with extracellular matrix production.

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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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Antisense Suppression of Collagen VI Synthesis Results in Reduced Expression of Collagen I in Normal Human Osteoblast-like Cells

Cited by 21 publications

References 22 publications

Morphologic complexity of the pericellular matrix in the annulus of the human intervertebral disc

Morphologic complexity of the pericellular matrix in the annulus of the human intervertebral disc

Laminin-5 activates extracellular matrix production and osteogenic gene focusing in human mesenchymal stem cells

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

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