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The glycosaminoglycan-binding domain of PRELP acts as a cell type-specific NF-kappa B inhibitor that impairs osteoclastogenesis

Rucci, Nadia ; Rufo, Anna ; Alamanou, Marina ; Capulli, Mattia ; Del Fattore, Andrea ; Åhrman, Emma LU ; Capece, Daria ; Iansante, Valeria ; Zazzeroni, Francesca and Alesse, Edoardo , et al. (2009) In Journal of Cell Biology 187(5). p.669-683
Abstract
Proline/arginine-rich end leucine-rich repeat protein (PRELP) is a glycosaminoglycan (GAG)- and collagen-binding anchor protein highly expressed in cartilage, basement membranes, and developing bone. We observed that PRELP inhibited in vitro and in vivo mouse osteoclastogenesis through its GAG-binding domain ((PRELP)-P-hbd), involving (a) cell internalization through a chondroitin sulfate-and annexin II-dependent mechanism, (b) nuclear translocation, (c) interaction with p65 nuclear factor. B (NF-kappa B) and inhibition of its DNA binding, and (d) impairment of NF-kappa B transcriptional activity and reduction of osteoclast-specific gene expression. hbdPRELP does not disrupt the mitogen-activated protein kinase signaling nor does it impair... (More)
Proline/arginine-rich end leucine-rich repeat protein (PRELP) is a glycosaminoglycan (GAG)- and collagen-binding anchor protein highly expressed in cartilage, basement membranes, and developing bone. We observed that PRELP inhibited in vitro and in vivo mouse osteoclastogenesis through its GAG-binding domain ((PRELP)-P-hbd), involving (a) cell internalization through a chondroitin sulfate-and annexin II-dependent mechanism, (b) nuclear translocation, (c) interaction with p65 nuclear factor. B (NF-kappa B) and inhibition of its DNA binding, and (d) impairment of NF-kappa B transcriptional activity and reduction of osteoclast-specific gene expression. hbdPRELP does not disrupt the mitogen-activated protein kinase signaling nor does it impair cell survival. hbdPRELP activity is cell type specific, given that it is internalized by the RAW264.7 osteoclast-like cell line but fails to affect calvarial osteoblasts, bone marrow macrophages, and epithelial cell lines. In vivo, hbdPRELP reduces osteoclast number and activity in ovariectomized mice, underlying its physiological and/or pathological importance in skeletal remodeling. (Less)
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Cell Biology
volume
187
issue
5
pages
669 - 683
publisher
Rockefeller University Press
external identifiers
  • wos:000272182900010
  • scopus:74049094448
  • pmid:19951916
ISSN
0021-9525
DOI
10.1083/jcb.200906014
language
English
LU publication?
yes
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Connective Tissue Biology (013230151), Biochemistry and Structural Biology (S) (000006142)
id
55b57b18-dd53-417f-b512-96ac56004c93 (old id 1517692)
date added to LUP
2016-04-01 12:27:34
date last changed
2022-01-27 05:21:05
@article{55b57b18-dd53-417f-b512-96ac56004c93,
  abstract     = {{Proline/arginine-rich end leucine-rich repeat protein (PRELP) is a glycosaminoglycan (GAG)- and collagen-binding anchor protein highly expressed in cartilage, basement membranes, and developing bone. We observed that PRELP inhibited in vitro and in vivo mouse osteoclastogenesis through its GAG-binding domain ((PRELP)-P-hbd), involving (a) cell internalization through a chondroitin sulfate-and annexin II-dependent mechanism, (b) nuclear translocation, (c) interaction with p65 nuclear factor. B (NF-kappa B) and inhibition of its DNA binding, and (d) impairment of NF-kappa B transcriptional activity and reduction of osteoclast-specific gene expression. hbdPRELP does not disrupt the mitogen-activated protein kinase signaling nor does it impair cell survival. hbdPRELP activity is cell type specific, given that it is internalized by the RAW264.7 osteoclast-like cell line but fails to affect calvarial osteoblasts, bone marrow macrophages, and epithelial cell lines. In vivo, hbdPRELP reduces osteoclast number and activity in ovariectomized mice, underlying its physiological and/or pathological importance in skeletal remodeling.}},
  author       = {{Rucci, Nadia and Rufo, Anna and Alamanou, Marina and Capulli, Mattia and Del Fattore, Andrea and Åhrman, Emma and Capece, Daria and Iansante, Valeria and Zazzeroni, Francesca and Alesse, Edoardo and Heinegård, Dick and Teti, Anna}},
  issn         = {{0021-9525}},
  language     = {{eng}},
  number       = {{5}},
  pages        = {{669--683}},
  publisher    = {{Rockefeller University Press}},
  series       = {{Journal of Cell Biology}},
  title        = {{The glycosaminoglycan-binding domain of PRELP acts as a cell type-specific NF-kappa B inhibitor that impairs osteoclastogenesis}},
  url          = {{http://dx.doi.org/10.1083/jcb.200906014}},
  doi          = {{10.1083/jcb.200906014}},
  volume       = {{187}},
  year         = {{2009}},
}