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The role of osteoactivin and osteoac...

Selim, Abdulhafez A.

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The role of osteoactivin and osteoactivin-derived peptides in osteoblast differentiation.

Record Type:	Electronic resources : Monograph/item
Title/Author:	The role of osteoactivin and osteoactivin-derived peptides in osteoblast differentiation./
Author:	Selim, Abdulhafez A.
Description:	109 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-03, Section: B, page: 1116.
Contained By:	Dissertation Abstracts International65-03B.
Subject:	Biology, Cell. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3125554
ISBN:	0496728431

The role of osteoactivin and osteoactivin-derived peptides in osteoblast differentiation.
Selim, Abdulhafez A.

The role of osteoactivin and osteoactivin-derived peptides in osteoblast differentiation. - 109 p.

Source: Dissertation Abstracts International, Volume: 65-03, Section: B, page: 1116.

Thesis (Ph.D.)--Temple University, 2004.

Previously, our laboratory examined differential gene expression in bone from normal and osteopetrotic (op) rats, we isolated a novel cDNA, termed osteoactivin (OA) that was over-expressed in op when compared to normal bone. Using OA anti-sense oligonucleotides, we were able to block OA expression in primary osteoblast cultures resulting in decreased alkaline phosphatase activity, osteocalcin production, nodule formation and matrix mineralization. Using the Chariot transfection reagent as a vehicle to deliver the anti-OA antibody inside the cells, we demonstrated that anti-OA antibody treatment also showed inhibition of alkaline phosphatase activity, osteocalcin production, nodule formation and mineralization. Conversely, OA over-expression in osteoblast cells transiently transfected with CMV-OA increased alkaline phosphatase activity, osteocalcin production and matrix mineralization compared to cultures transfected with an empty vector. Based on the possibility that the region of the OA protein containing the RGD domain may be responsible, at least in part, in mediating the effects of OA on osteoblast development, we examined the functional role of OA-derived peptide containing the RGD motif (OA-D) in osteoblast differentiation. OA-D peptide treatment markedly induced osteoblast differentiation markers in vitro compared to cultures treated with negative control peptide (NCP). We next asked whether the effect of OA-D peptide on osteoblast differentiation is RGD dependent or not. For this purpose, we designed another peptide, termed OA-E, that has a sequence similar to OA-D but with glutamic acid (E) instead of aspartic acid (D). Interestingly, OA-E induced osteoblast differentiation in a manner similar to OA-D peptide. These data suggested that the effect of OA-derived peptides is RGD independent. Since phosphorylation of amino acid residues in proteins and peptides plays a major role in biological systems, the phosphorylation pattern of OA-derived peptides and OA protein family members were examined using bioinformatic analysis tools. OA-derived peptides and OA protein family members have conserved serine residues, close to the C-terminus and potentially phosphorylated with casein kinase II. Casein kinase II is known to phosphorylate many osteoblast-related proteins that regulate osteoblast differentiation. Collectively, these data indicated that OA and OA-derived peptides plays a key role in the regulation of osteoblast differentiation in vitro.

ISBN: 0496728431Subjects--Topical Terms:

1017686
Biology, Cell.

The role of osteoactivin and osteoactivin-derived peptides in osteoblast differentiation.
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245 1 4 $a The role of osteoactivin and osteoactivin-derived peptides in osteoblast differentiation.
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500 $a Chair: Fayez F. Safadi.
502 $a Thesis (Ph.D.)--Temple University, 2004.
520 $a Previously, our laboratory examined differential gene expression in bone from normal and osteopetrotic (op) rats, we isolated a novel cDNA, termed osteoactivin (OA) that was over-expressed in op when compared to normal bone. Using OA anti-sense oligonucleotides, we were able to block OA expression in primary osteoblast cultures resulting in decreased alkaline phosphatase activity, osteocalcin production, nodule formation and matrix mineralization. Using the Chariot transfection reagent as a vehicle to deliver the anti-OA antibody inside the cells, we demonstrated that anti-OA antibody treatment also showed inhibition of alkaline phosphatase activity, osteocalcin production, nodule formation and mineralization. Conversely, OA over-expression in osteoblast cells transiently transfected with CMV-OA increased alkaline phosphatase activity, osteocalcin production and matrix mineralization compared to cultures transfected with an empty vector. Based on the possibility that the region of the OA protein containing the RGD domain may be responsible, at least in part, in mediating the effects of OA on osteoblast development, we examined the functional role of OA-derived peptide containing the RGD motif (OA-D) in osteoblast differentiation. OA-D peptide treatment markedly induced osteoblast differentiation markers in vitro compared to cultures treated with negative control peptide (NCP). We next asked whether the effect of OA-D peptide on osteoblast differentiation is RGD dependent or not. For this purpose, we designed another peptide, termed OA-E, that has a sequence similar to OA-D but with glutamic acid (E) instead of aspartic acid (D). Interestingly, OA-E induced osteoblast differentiation in a manner similar to OA-D peptide. These data suggested that the effect of OA-derived peptides is RGD independent. Since phosphorylation of amino acid residues in proteins and peptides plays a major role in biological systems, the phosphorylation pattern of OA-derived peptides and OA protein family members were examined using bioinformatic analysis tools. OA-derived peptides and OA protein family members have conserved serine residues, close to the C-terminus and potentially phosphorylated with casein kinase II. Casein kinase II is known to phosphorylate many osteoblast-related proteins that regulate osteoblast differentiation. Collectively, these data indicated that OA and OA-derived peptides plays a key role in the regulation of osteoblast differentiation in vitro.
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