Advanced

Ultrastructural distribution of osteoadherin in rat bone shows a pattern similar to that of bone sialoprotein

Ramstad, VE; Franzén, Ahnders LU ; Heinegård, Dick LU ; Wendel, M and Reinholt, FP (2003) In Calcified Tissue International 72(1). p.57-64
Abstract
Osteoadherin (OSAD) is a keratan sulfate proteoglycan recently isolated from bovine and rat bone. Based on results obtained from in vitro experiments, the protein was shown to bind osteoblasts via the integrin receptor alpha(v)beta(3). Due to OSAD's capacity to bind hydroxyapatite crystals, a role for the protein in the mineralization process has also been suggested. To test these hypotheses in an in vivo model, the ultrastructural localization of OSAD in bone, tibial (metaphyses and diaphyses). and calvarial samples from normal 10 to 12-day-old rats were examined by immunohistochemical techniques at the ultrastructural level. In addition to the qualitative studies, quantitative measurements of OSAD marker density were performed in... (More)
Osteoadherin (OSAD) is a keratan sulfate proteoglycan recently isolated from bovine and rat bone. Based on results obtained from in vitro experiments, the protein was shown to bind osteoblasts via the integrin receptor alpha(v)beta(3). Due to OSAD's capacity to bind hydroxyapatite crystals, a role for the protein in the mineralization process has also been suggested. To test these hypotheses in an in vivo model, the ultrastructural localization of OSAD in bone, tibial (metaphyses and diaphyses). and calvarial samples from normal 10 to 12-day-old rats were examined by immunohistochemical techniques at the ultrastructural level. In addition to the qualitative studies, quantitative measurements of OSAD marker density were performed in relevant compartments. Immunolabeling for OSAD was located to the mineralized bone matrix, with highest concentration of marker at the border between bone and cartilage remnants in the metaphyseal trabeculi. Intracellular labeling was low and no systemic accumulation of OSAD markers was observed at the cell-matrix interface. The observed distribution pattern of OSAD is strikingly similar to that of bone sialoprotein (BSP), confirmed by double labeling. The results of the current study support a role for OSAD in the mineralization process. In this process BSP is assumed to be a nucleator of hydroxyapatite crystals, and OSAD could work in concert with BSP to regulate nucleation. However, the mechanisms involved remain to be elucidated. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
immunohistochemistry, ultrastructure, bone sialoprotein, bone matrix, osteoadherin
in
Calcified Tissue International
volume
72
issue
1
pages
57 - 64
publisher
Springer
external identifiers
  • wos:000180548900009
  • pmid:12384815
  • scopus:0043211869
ISSN
1432-0827
DOI
language
English
LU publication?
yes
id
59f4290a-d820-434c-939d-62782697d2b9 (old id 319622)
date added to LUP
2007-09-20 12:11:39
date last changed
2018-05-29 10:48:48
@article{59f4290a-d820-434c-939d-62782697d2b9,
  abstract     = {Osteoadherin (OSAD) is a keratan sulfate proteoglycan recently isolated from bovine and rat bone. Based on results obtained from in vitro experiments, the protein was shown to bind osteoblasts via the integrin receptor alpha(v)beta(3). Due to OSAD's capacity to bind hydroxyapatite crystals, a role for the protein in the mineralization process has also been suggested. To test these hypotheses in an in vivo model, the ultrastructural localization of OSAD in bone, tibial (metaphyses and diaphyses). and calvarial samples from normal 10 to 12-day-old rats were examined by immunohistochemical techniques at the ultrastructural level. In addition to the qualitative studies, quantitative measurements of OSAD marker density were performed in relevant compartments. Immunolabeling for OSAD was located to the mineralized bone matrix, with highest concentration of marker at the border between bone and cartilage remnants in the metaphyseal trabeculi. Intracellular labeling was low and no systemic accumulation of OSAD markers was observed at the cell-matrix interface. The observed distribution pattern of OSAD is strikingly similar to that of bone sialoprotein (BSP), confirmed by double labeling. The results of the current study support a role for OSAD in the mineralization process. In this process BSP is assumed to be a nucleator of hydroxyapatite crystals, and OSAD could work in concert with BSP to regulate nucleation. However, the mechanisms involved remain to be elucidated.},
  author       = {Ramstad, VE and Franzén, Ahnders and Heinegård, Dick and Wendel, M and Reinholt, FP},
  issn         = {1432-0827},
  keyword      = {immunohistochemistry,ultrastructure,bone sialoprotein,bone matrix,osteoadherin},
  language     = {eng},
  number       = {1},
  pages        = {57--64},
  publisher    = {Springer},
  series       = {Calcified Tissue International},
  title        = {Ultrastructural distribution of osteoadherin in rat bone shows a pattern similar to that of bone sialoprotein},
  url          = {http://dx.doi.org/},
  volume       = {72},
  year         = {2003},
}