Osteoadherin, a Cell-binding Keratan Sulfate Proteoglycan in Bone, Belongs to the Family of Leucine-rich Repeat Proteins of the Extracellular Matrix

Sommarin, Yngve; Wendel, Mikael; Shen, Zhenxin; Hellman, Ulf; Heinegård, Dick

doi:10.1074/jbc.273.27.16723

Cited by 113 publications

(82 citation statements)

References 46 publications

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“…Osteomodulin or Osteoadherin (OMD or OSAD) is a keratan sulfate proteoglycan which belongs to the SLRP (Small Leucine-rich Repeat Proteoglycans) family 42,43) . It is found exclusively in mineralized tissues 44) , mouse osteoblasts, odontoblasts, ameloblasts 45) and human odontoblasts 46) .…”

Section: Discussionmentioning

confidence: 99%

Gene Expression of MC3T3-E1 Cells on Fibronectin-immobilized Titanium Using Tresyl Chloride Activation Technique

et al. 2007

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Fibronectin (FN) can be immobilized directly on titanium surfaces using tresyl chloride activation technique. The key advantage of tresyl chloride activation technique lies in its simplicity. In this study, we examined the cell attachment and gene expression of MC3T3-E1 cells on FN-immobilized titanium using GeneChip. Cells attached on FN-immobilized titanium at a higher rate than untreated titanium. FN altered the gene expression profile, whereby 62 genes were found to be up-regulated, while 56 genes were found to down-regulate to over twice the level on day 14. FN not only enhanced the expression levels of IBSP and OMD, but also decreased SULF1 mRNA level. Taken together, the immobilization of FN on tresylated titanium promoted early matrix mineralization and bone formation.

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Section: Discussionmentioning

confidence: 99%

Gene Expression of MC3T3-E1 Cells on Fibronectin-immobilized Titanium Using Tresyl Chloride Activation Technique

et al. 2007

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“…The class II members, fibromodulin (8), lumican (9), PRELP (10), keratocan (11), and osteoadherin (12), have a pairwise amino acid sequence identity between 37 and 55% and have a common gene structure composed of three exons. The cysteine spacing in the N-terminal region of class II SLRPs is identical (CX 3 CXCX 9 C) but different from the other SLRP classes.…”

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confidence: 99%

Expression Pattern and Gene Characterization ofAsporin

Henry

Takanosu

Boyd

et al. 2001

Journal of Biological Chemistry

149

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We have discovered a new member of the class I small leucine-rich repeat proteoglycan (SLRP) family which is distinct from the other class I SLRPs since it possesses a unique stretch of aspartate residues at its N terminus. For this reason, we called the molecule asporin. The deduced amino acid sequence is about 50% identical (and 70% similar) to decorin and biglycan. However, asporin does not contain a serine/glycine dipeptide sequence required for the assembly of O-linked glycosaminoglycans and is probably not a proteoglycan. The tissue expression of asporin partially overlaps with the expression of decorin and biglycan. During mouse embryonic development, asporin mRNA expression was detected primarily in the skeleton and other specialized connective tissues; very little asporin message was detected in the major parenchymal organs. The mouse asporin gene structure is similar to that of biglycan and decorin with 8 exons. The asporin gene is localized to human chromosome 9q22-9q21.3 where asporin is part of a SLRP gene cluster that includes extracellular matrix protein 2, osteoadherin, and osteoglycin. Further analysis shows that, with the exception of biglycan, all known SLRP genes reside in three gene clusters.The small leucine-rich repeat proteoglycans (or SLRPs) 1 are a group of extracellular proteins (ECM) that belong to the leucine-rich repeat (LRR) superfamily of proteins (1, 2). The LRR is a protein folding motif composed of 20 -30 amino acids with leucines in conserved positions. LRR-containing proteins are present in a broad spectrum of organisms and possess diverse cellular functions and localization (3). The members of the SLRP subfamily have core proteins of similar size (about 40 kilodaltons) that are dominated by a central domain composed of 6 -10 tandemly repeated LRRs. This domain is flanked by smaller, less conserved N-terminal and C-terminal regions containing cysteines in characteristic positions.Most of the SLRP proteins are proteoglycans, and the SLRP gene family has been subdivided into 3 classes based on similarities in overall amino acid sequence, spacing of cysteine residues in the N terminus, and gene structure. The previously identified class I members, decorin (4) and biglycan (5), are the most closely related SLRPs based on amino acid sequences; the human sequences are 57% identical. The core proteins contain 10 LRRs, and the N-terminal regions of decorin and biglycan are substituted with one and two chondroitin/dermatan sulfate chains, respectively. The cysteine-rich cluster in the N terminus of class I SLRPs has an amino acid spacing of CX 3 CXCX 6 C. The mouse decorin (6) and biglycan genes (7) contain 8 exons.The class II members, fibromodulin (8), lumican (9), PRELP (10), keratocan (11), and osteoadherin (12), have a pairwise amino acid sequence identity between 37 and 55% and have a common gene structure composed of three exons. The cysteine spacing in the N-terminal region of class II SLRPs is identical (CX 3 CXCX 9 C) but different from the other SLRP classes. The core pro...

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“…In fact, expression of osteoadherin mRNA has been detected by in situ hybridization in mature osteoblasts located superficially on trabecular bovine bone 15) .…”

Section: Discussionmentioning

confidence: 99%

Hydrogen Peroxide Reduced Osteomodulin Gene Expression in MC3T3-E1

Kamikawa

Abiko

2009

J. Hard Tissue Biology.

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: Bone formation steadily declines with age resulting in significant loss of bone mass, and reactive oxygen species (ROS) are thought to be a major contributor to the aging process. H2O2 treatment significantly reduced bone nodule formation rate in pre-osteoblastic cell, MC3T3E1. In this study, to identify which genes have an altered transcription level associated with bone loss by ageing, MC3T3-E1 cells were treated with H2O2, and monitored gene expression change using the Affymetrix GeneChip TM system (Mouse; 34,000 genes). H2O2 altered many gene expressions including reduction of osteomodulin (OMD) mRNA level. The reduction of OMD gene expression by H2O2 was successfully confirmed by reversed transcription polymerase chain reaction (RT-PCR) and real-time PCR. Since OMD was found in bone tissues and play an important role in biomineralization, the reduction of OMD gene expression by H2O2 may be involved in the decline of bone formation in the ageing process.

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Osteoadherin, a Cell-binding Keratan Sulfate Proteoglycan in Bone, Belongs to the Family of Leucine-rich Repeat Proteins of the Extracellular Matrix

Cited by 113 publications

References 46 publications

Gene Expression of MC3T3-E1 Cells on Fibronectin-immobilized Titanium Using Tresyl Chloride Activation Technique

Gene Expression of MC3T3-E1 Cells on Fibronectin-immobilized Titanium Using Tresyl Chloride Activation Technique

Expression Pattern and Gene Characterization ofAsporin

Hydrogen Peroxide Reduced Osteomodulin Gene Expression in MC3T3-E1

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