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Lysyl oxidase regulates transforming...

The University of North Carolina at Chapel Hill., Dentistry: Oral Biology.

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Lysyl oxidase regulates transforming growth factor-beta1 function in bone.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Lysyl oxidase regulates transforming growth factor-beta1 function in bone./
Author:	Atsawasuwan, Phimon.
Description:	137 p.
Notes:	Adviser: Mitsuo Yamauchi.
Contained By:	Dissertation Abstracts International69-04B.
Subject:	Biology, Cell. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=3304272
ISBN:	9780549532811

Lysyl oxidase regulates transforming growth factor-beta1 function in bone.
Atsawasuwan, Phimon.

Lysyl oxidase regulates transforming growth factor-beta1 function in bone. - 137 p.

Adviser: Mitsuo Yamauchi.

Thesis (Ph.D.)--The University of North Carolina at Chapel Hill, 2008.

Lysyl oxidase (LOX), an amine oxidase critical for the initiation of collagen and elastin cross-linking, has recently been shown to regulate cellular activities possibly by modulating growth factor activity. In this study, we discovered that osteoblastic (MC3T3-E1) cell-derived clones expressing higher (S) levels of LOX exhibited smaller collagen fibrils and lower collagen production than controls (MC, EV) while the clones expressing lower (AS) levels of LOX exhibited larger collagen fibrils and higher amount of collagen leading to subsequent defective mineralization. In order to elucidate the mechanisms by which collagen synthesis is controlled through LOX, we investigated the potential role of LOX in regulating growth factors. We further investigated the interaction of LOX with TGF-beta1, a potent growth factor abundant in bone, and evaluated the effect of this interaction. The specific binding between LOX and TGF-beta1 was demonstrated both by immunoprecipitation and glutathione-S-transferase pull down assay. Both molecules were co-localized in the extracellular matrix in culture and the binding complex was identified in the mineral-associated fraction of bone matrix. Furthermore, LOX suppressed TGF-beta1 induced Smad3 phosphorylation and collagen (I/V) expression but the effects were nullified by beta-aminopropionitrile. The suppression of Smad3 phosphorylation was not affected by the presence of catalase. The data indicate that LOX may bind to mature TGF-beta1 and regulate its signaling via its amine oxidase activity in bone, thus, may play an important role in bone remodeling and mineralization.

ISBN: 9780549532811Subjects--Topical Terms:

1017686
Biology, Cell.

Lysyl oxidase regulates transforming growth factor-beta1 function in bone.
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020 $a 9780549532811
035 $a (UMI)AAI3304272
035 $a AAI3304272
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100 1 $a Atsawasuwan, Phimon. $3 1025235
245 1 0 $a Lysyl oxidase regulates transforming growth factor-beta1 function in bone.
300 $a 137 p.
500 $a Adviser: Mitsuo Yamauchi.
500 $a Source: Dissertation Abstracts International, Volume: 69-04, Section: B, page: 2197.
502 $a Thesis (Ph.D.)--The University of North Carolina at Chapel Hill, 2008.
520 $a Lysyl oxidase (LOX), an amine oxidase critical for the initiation of collagen and elastin cross-linking, has recently been shown to regulate cellular activities possibly by modulating growth factor activity. In this study, we discovered that osteoblastic (MC3T3-E1) cell-derived clones expressing higher (S) levels of LOX exhibited smaller collagen fibrils and lower collagen production than controls (MC, EV) while the clones expressing lower (AS) levels of LOX exhibited larger collagen fibrils and higher amount of collagen leading to subsequent defective mineralization. In order to elucidate the mechanisms by which collagen synthesis is controlled through LOX, we investigated the potential role of LOX in regulating growth factors. We further investigated the interaction of LOX with TGF-beta1, a potent growth factor abundant in bone, and evaluated the effect of this interaction. The specific binding between LOX and TGF-beta1 was demonstrated both by immunoprecipitation and glutathione-S-transferase pull down assay. Both molecules were co-localized in the extracellular matrix in culture and the binding complex was identified in the mineral-associated fraction of bone matrix. Furthermore, LOX suppressed TGF-beta1 induced Smad3 phosphorylation and collagen (I/V) expression but the effects were nullified by beta-aminopropionitrile. The suppression of Smad3 phosphorylation was not affected by the presence of catalase. The data indicate that LOX may bind to mature TGF-beta1 and regulate its signaling via its amine oxidase activity in bone, thus, may play an important role in bone remodeling and mineralization.
590 $a School code: 0153.
650 4 $a Biology, Cell. $3 1017686
650 4 $a Health Sciences, Dentistry. $3 1019378
690 $a 0379
690 $a 0567
710 2 $a The University of North Carolina at Chapel Hill. $b Dentistry: Oral Biology. $3 1025234
773 0 $t Dissertation Abstracts International $g 69-04B.
790 $a 0153
790 1 0 $a Mishina, Yuji $e committee member
790 1 0 $a Mochida, Yoshiyuki $e committee member
790 1 0 $a Trackman, Phillip C. $e committee member
790 1 0 $a Wright, John T. $e committee member
790 1 0 $a Yamauchi, Mitsuo, $e advisor
791 $a Ph.D.
792 $a 2008
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=3304272