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Sommarin Y, Wendel M, Shen Z, Hellman U, Heinegard D (1998) Osteoadherin, a cell-binding keratan sulfate proteoglycan in bone, belongs to the family of leucine-rich repeat proteins of the extracellular matrix. J Biol Chem 273:16723–16729 PubMed CrossRef Google Scholar

Date: 2008-06-04. A small cell-binding proteoglycan for which we propose the name osteoadherin was extracted from bovine bone with guanidine hydrochloride–containing EDTA. It was purified to homogeneity using a combination of ion-exchange chromatography, hydroxyapatite chromatography, and gel filtration. The Mr of the proteoglycan was 85,000 as determined by Osteoadherin, fibromodulin, and chondroadherin, which bind C1q and activate complement, were found to cause significantly higher C9 deposition in C4BP-depleted serum compared with Igs, indicating that the level of complement activation initiated by SLRPs is regulated by simultaneous binding to C4BP. Bovine osteoadherin contains leucine-rich repeats (LRRs) and is also rich in aspartic acid and glutamic acid. It had an apparent molecular mass of 85 kD under reducing conditions by SDS-PAGE.

Osteoadherin

Osteoadherin is highly expressed in mineralized tissues, including bone and dentin; however, it's precise roles remain unknown. 1998-07-03 · Osteoadherin, a Cell-binding Keratan Sulfate Proteoglycan in Bone, Belongs to the Family of Leucine-rich Repeat Proteins of the Extracellular Matrix. *. Osteoadherin is a recently described bone proteoglycan containing keratan sulfate. It promotes integrin (α v β 3 )-mediated cell binding (Wendel, M., Sommarin, Y., and Heinegård, D. (1998) J. Cell Osteoadherin (OSAD), a keratan sulphate PG is a member of the small leucine-rich (SLRP) family of PGs and unlike other SLRPs, OSAD expression is restricted to mineralized tissues. It is proposed to have a high affinity for hydroxyapatite and has been shown to be expressed by mature osteoblasts but its exact role remains to be elucidated.

Short name: OSAD.

Super‐motifs and evolution of tandem leucine‐rich repeats within the small proteoglycans—biglycan, decorin, lumican, fibromodulin, PRELP, keratocan, osteoadherin, epiphycan, and osteoglycin

U Petersson, K Hultenby, M Wendel. European journal of oral sciences 111 (2), Osteoadherin is a recently described bone proteoglycan containing keratan sulfate. It promotes integrin (alphav beta3)-mediated cell binding (Wendel, M., Sommarin, Y., and Heinegârd, D. (1998) J. Cell Biol. 141, 839-847).

2017-02-28

141, 839-847). Osteoadherin (also termed osteomodulin) is encoded by the Omd gene and is a keratan sulfate proteoglycan of the class II subfamily of SLRPs. Osteoadherin is highly expressed in mineralized tissues, including bone and dentin; however, it's precise roles remain unknown. Osteoadherin is a recently described bone proteoglycan containing keratan sulfate. It promotes integrin (α v β 3)-mediated cell binding (Wendel, M., Sommarin, Y., and Heinegård, D. (1998) J. Cell Biol. 141, 839–847).

It was purified to homogeneity using a combination of ion-exchange chromatography, hydroxyapatite chromatography, and gel filtration. The Mr of the proteoglycan was 85,000 as determined by OSTEOADHERIN. From THE INSTITUTE OF ODONTOLOGY, CENTER FOR ORAL BIOLOGY Karolinska Institutet, Stockholm, Sweden REGULATION AND FUNCTION OF MINERALIZED TISSUE EXTRA-CELLULAR MATRIX PROTEINS: STUDIES OF ADAMTS-1 AND OSTEOADHERIN Anders Rehn Stockholm 2008 . 2008 Gårdsvägen 4, 169 70 Solna Osteoadherin also interacts with calcium phosphate mineral , suggesting that osteoadherin contributes to biomineralization and the control of mineral crystal nucleation, growth, and maturation. Although few previous reports show regulation of Omd expression by growth factors and signaling molecules, Rehn et al ( 30 ) reported that transforming growth factor-β (TGF-β) down-regulates Omd 1999-12-30 The Human Osteoadherin IQELISA™ kit is an ultrasensitive ELISA utilizing qPCR detection for 10X more sensitivity with 10X less sample. See more Osteoadherin/OSAD/OMD products: Catalog# EK2017: Storage & Handling: Store at 4˚C for 6 months, at -20˚C for 12 months. Avoid multiple freeze-thaw cycles (Shipped with wet ice.) Description: Sandwich High Sensitivity ELISA kit for Quantitative Detection of human Osteoadherin.
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OMD (Osteomodulin) is a Protein Coding gene. Diseases associated with OMD include Bladder Carcinoma In Situ and Anthracosilicosis . Among its related pathways are Diseases of glycosylation and HIV Life Cycle .

Accepted manuscript, Calcified Tissue International.
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Osteoadherin, fibromodulin, and chondroadherin, which bind C1q and activate complement, were found to cause significantly higher C9 deposition in C4BP-depleted serum compared with Igs, indicating that the level of complement activation initiated by SLRPs is regulated by simultaneous binding to C4BP.

The primary structure of bovine osteoadherin has now been determined by nucleotide sequencing of a cDNA clone Osteoadherin (OSAD), a keratan sulphate PG is a member of the small leucine-rich (SLRP) family of PGs and unlike other SLRPs, OSAD expression is restricted to mineralized tissues. It is proposed to have a high affinity for hydroxyapatite and has been shown to be expressed by mature osteoblasts but its exact role remains to be elucidated.

Osteoadherin (OSAD), a keratan sulphate PG is a member of the small leucine-rich (SLRP) family of PGs and unlike other SLRPs, OSAD expression is restricted to mineralized tissues. It is proposed to have a high affinity for hydroxyapatite and has been shown to be expressed by mature osteoblasts but its exact role remains to be elucidated.

It promotes integrin (α v β 3 )-mediated cell binding (Wendel, M., Sommarin, Y., and Heinegård, D. (1998) J. Cell Osteoadherin (OSAD), a keratan sulphate PG is a member of the small leucine-rich (SLRP) family of PGs and unlike other SLRPs, OSAD expression is restricted to mineralized tissues. It is proposed to have a high affinity for hydroxyapatite and has been shown to be expressed by mature osteoblasts but its exact role remains to be elucidated. Osteoadherin (OSAD), also known as Osteomodulin, is an extracellular matrix keratan sulfate proteoglycan that belongs to the class II subfamily of small leucine-rich proteoglycans (SLRP). Leucine-rich repeat (LRR) motifs consist of approximately 20 - 30 amino acids (aa) with conserved leucine spacing, folded into a structure with one beta-sheet and one alpha-helix. 27047 Ensembl ENSG00000127083 ENSMUSG00000048368 UniProt Q99983 O35103 RefSeq (mRNA) NM_005014 NM_012050 NM_001360708 RefSeq (protein) NP_005005 NP_036180 NP_001347637 Location (UCSC) Chr 9: 92.41 – 92.42 Mb Chr 13: 49.58 – 49.59 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Osteomodulin (also called osteoadherin or osteoadherin proteoglycan) is a protein that in humans is Listed are ELISA Kits for the detection of Osteoadherin, an alias name of osteomodulin. The human protein, encoded by the gene OMD, is 421 amino acid residues long and has a mass of 49,492 daltons.

The LRR‐containing proteins include a family of nine small proteoglycans, forming three distinct subfamilies: class I contains biglycan/PG‐I and decorin/PG‐II; class II: lumican, fibromodulin, PRELP, keratocan, and osteoadherin; and class III: epiphycan/PG The small leucine-rich repeat proteins (SLRPs), fibromodulin and osteoadherin, have N-terminal extensions with a variable number of O-sulfated tyrosine residues.