Document Detail


Thrombospondin 1 binding to calreticulin-LRP1 signals resistance to anoikis.
MedLine Citation:
PMID:  18653767     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Anoikis, apoptotic cell death due to loss of cell adhesion, is critical for regulation of tissue homeostasis in tissue remodeling. Fibrogenesis is associated with reduced fibroblast apoptosis. The matricellular protein thrombospondin 1 (TSP1) regulates cell adhesion and motility during tissue remodeling and in fibrogenesis. The N-terminal domain of TSP1 binds to the calreticulin-LRP1 receptor co-complex to signal down-regulation of cell adhesion and increased cell motility through focal adhesion disassembly. TSP1 signaling through calreticulin-LRP1 activates cell survival signals such as PI3-kinase. Therefore, we tested the hypothesis that TSP1 supports cell survival under adhesion-independent conditions to facilitate tissue remodeling. Here, we show that platelet TSP1, its N-terminal domain (NoC1) as a recombinant protein, or a peptide comprising the calreticulin-LRP1 binding site [amino acids 17-35 (hep I)] in the N-terminal domain promotes fibroblast survival under anchorage-independent conditions. TSP1 activates Akt and decreases apoptotic signaling through caspase 3 and PARP1 in suspended fibroblasts. Inhibition of PI3K/Akt activity blocks TSP1-mediated anchorage-independent survival. Fibroblasts lacking LRP1 or expressing calreticulin lacking the TSP1 binding site do not respond to TSP1 with anchorage-independent survival. These data define a novel role for TSP1 signaling through the calreticulin/LRP1 co-complex in tissue remodeling and fibrotic responses through stimulation of anoikis resistance.-Pallero, M. A., Elzie, C. A., Chen, J., Mosher, D. F., Murphy-Ullrich, J. E. Thrombospondin 1 binding to calreticulin-LRP1 signals resistance to anoikis.
Authors:
Manuel A Pallero; Carrie A Elzie; Jiping Chen; Deane F Mosher; Joanne E Murphy-Ullrich
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2008-07-24
Journal Detail:
Title:  FASEB journal : official publication of the Federation of American Societies for Experimental Biology     Volume:  22     ISSN:  1530-6860     ISO Abbreviation:  FASEB J.     Publication Date:  2008 Nov 
Date Detail:
Created Date:  2008-10-31     Completed Date:  2008-11-18     Revised Date:  2012-02-15    
Medline Journal Info:
Nlm Unique ID:  8804484     Medline TA:  FASEB J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3968-79     Citation Subset:  IM    
Affiliation:
Department of Pathology, VH 668 1530 3rd Ave., South, Birmingham, AL 35294-0019, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Anoikis / physiology*
Binding Sites / physiology
Calreticulin / agonists*,  metabolism
Caspase 3 / metabolism
Cell Adhesion / drug effects,  physiology
Cell Survival / drug effects,  physiology
Fibroblasts / cytology,  metabolism*
Humans
Mice
Mice, Knockout
Peptides / metabolism,  pharmacology*
Phosphatidylinositol 3-Kinases / metabolism
Poly(ADP-ribose) Polymerases / metabolism
Protein Structure, Tertiary / physiology
Proto-Oncogene Proteins c-akt / metabolism
Receptors, LDL / agonists*,  metabolism
Signal Transduction / drug effects*,  physiology
Thrombospondin 1 / metabolism,  pharmacology*
Tumor Suppressor Proteins / agonists*,  metabolism
Grant Support
ID/Acronym/Agency:
C06 RR 15490/RR/NCRR NIH HHS; HL079644/HL/NHLBI NIH HHS; T32AR47512-01A1/AR/NIAMS NIH HHS; T32DE014300/DE/NIDCR NIH HHS
Chemical
Reg. No./Substance:
0/Calreticulin; 0/Lrp1 protein, mouse; 0/Peptides; 0/Receptors, LDL; 0/Thrombospondin 1; 0/Tumor Suppressor Proteins; EC 2.4.2.30/PARP1 protein, human; EC 2.4.2.30/Parp1 protein, mouse; EC 2.4.2.30/Poly(ADP-ribose) Polymerases; EC 2.7.1.-/Phosphatidylinositol 3-Kinases; EC 2.7.11.1/Proto-Oncogene Proteins c-akt; EC 3.4.22.-/CASP3 protein, human; EC 3.4.22.-/Casp3 protein, mouse; EC 3.4.22.-/Caspase 3
Comments/Corrections

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