Mar 20, 2003 Osteoadherin (OSAD) is a keratan sulfate‐containing proteoglycan, belonging to the small leucine‐rich proteoglycan (SLRP) family. In bone
Osteoadherin is a recently described bone proteogly-can containing keratan sulfate. It promotes integrin (a vb 3)-mediated cell binding (Wendel, M., Sommarin, Y., and Heinegård, D. (1998) J. Cell Biol. 141, 839–847). The primary structure of bovine osteoadherin has now been determined by nucleotide sequencing of a cDNA clone
2017-02-28 Osteomodulin (also called osteoadherin or osteoadherin proteoglycan) is a protein that in humans is encoded by the OMD gene. References Further reading. This page was last edited on 12 October 2020, at 04:35 (UTC). Text is available under the Creative Commons Attribution 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 function of OSAD during mineralization remains to be fully elucidated; however it has been shown to have a high affinity for hydroxyapatite, via the large and acidic C-terminal [15] , [16] . Transforming growth factor beta 1 (TGF g 1) is generally considered to be a potent inducer of dentin formation. In order to further assess this role, we studied the influence of this factor in human dental pulp cells on the expression of osteoadherin (OSAD), a newly described proteoglycan found in bone and dentin and suspected to play a role in mineralization events. 1998-05-01 · In addition, pure osteoadherin was shown not to react with antisera against other acidic glycoproteins from bone matrix such as osteonectin, osteopontin, bone sialoprotein, decorin, or biglycan. Osteoadherin seems to be restricted to bone as assayed by an inhibition ELISA. Other proteins exclusively restricted to bone include osteocalcin and BSP. The small leucine-rich repeat proteins (SLRPs), fibromodulin and osteoadherin, have N-terminal extensions with a variable number of O-sulfated tyrosine residues. This modification combined with a number of aspartic and glutamic acid residues results in a highly negatively charged domain of less than 30 amino acids.
The assay will exclusively recognize both Glycoproteins, such as alkaline phosphatase, osteonectin, RGD-containing proteins (osteoadherin, thrombospondin, fibronectin, vitronectin, osteopontin, bone Apr 18, 2018 Bone matrix proteins: isolation and characterization of a novel cell-binding keratan sulfate proteoglycan (Osteoadherin) from bovine bone. J. Cell Jan 28, 2020 The tyrosine sulfate-rich domains of the LRR proteins fibromodulin and osteoadherin bind motifs of basic clusters in a variety of heparin-binding The regulation of osteoadherin by neurotrophins in both osteoblasts and dental pulp cells suggests that a complex signaling network occurs during the NP_005005.1 osteomodulin 229 OMD_HUMAN Osteomodulin precursor ( Osteoadherin) (OSAD) (Keratan sulfate. Q99983 proteoglycan osteomodulin) ( KSPG Osteoadherin is highly expressed in mineralized tissues, including bone and dentin; however, it's precise roles remain unknown.
Osteoadherin is a recently described bone proteogly-can containing keratan sulfate. It promotes integrin (a vb 3)-mediated cell binding (Wendel, M., Sommarin, Y., and Heinegård, D. (1998) J. Cell Biol. 141, 839–847). The primary structure of bovine osteoadherin has now been determined by nucleotide sequencing of a cDNA clone
Author: Rehn, Anders. 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.
KSPG osteomodulin antibody; OSAD antibody. Osteoadherin antibody; Osteoadherin proteoglycan antibody; Osteomodulin antibody; SLRR2C antibody.
An important paralog of this gene is KERA. Human Osteoadherin/Osteomodulin ELISA Kit from Invitrogen (96 Tests).
The primary structure of bovine osteoadherin has now been determined by nucleotide sequencing of a cDNA clone
1997-05-01
Osteoadherin, a cell-binding keratan sulfate proteoglycan in bone, belongs to the family of leucine-rich repeat proteins of the extracellular matrix. [Y Sommarin, M Wendel, Z Shen, U Hellman, D Heinegârd] PMID 9642227 . Abstract Osteoadherin is a recently described bone …
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. 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 .
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Osteoadherin (OSAD) is a bone proteoglycan containing keratan sulfate that belongs to the small leucine-rich proteoglycan (SLRP) family. Osteoadherin promotes Integrin αvβ3-mediated cell binding. The central region of Osteoadherin consists of eleven B-type, leucine-rich repeats ranging in length from 20 to 30 residues. 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.
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.
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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
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. 2017-02-28 Osteomodulin (also called osteoadherin or osteoadherin proteoglycan) is a protein that in humans is encoded by the OMD gene. References Further reading. This page was last edited on 12 October 2020, at 04:35 (UTC). Text is available under the Creative Commons Attribution 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. It is a member of the Small leucine-rich proteoglycan (SLRP) family, SLRP class II subfamily.