Abstract
α-dystroglycan is a cell surface receptor that is expressed in many tissues including the nervous system. The study shows that a recombinant, non-glycosylated N-terminal fragment of α-dystroglycan comprising residues 30 to 315 [αDG (30-315)] bound to laminin-2/-4 and laminin-1, fibronectin and fibrinogen, all molecules highly upregulated in the regenerating peripheral nerve. The interaction was concentration dependent and saturable and could not be inhibited by heparin suggesting only minor involvement of sulfated carbohydrate moieties. In contrast to published data, addition of bivalent cations increased the binding affinity by only ten fold. αDG (30-315) promotes neurite extension of PC12 cells in a similar amount as described for laminin isoforms and could be inhibited in a concentration dependent manner by αDG (30-315) itself, soluble laminin-1, partially by heparin, EDTA, and an RGD-peptide. Furthermore, co-immunoprecipitations between α-dystroglycan and β1-integrin from PC12 cell surfaces suggested complex interactions between neuronal dystroglycan, integrins, and the ECM that induce neurite extension in vitro.
| Original language | English |
|---|---|
| Pages (from-to) | 1062-1073 |
| Number of pages | 12 |
| Journal | Molecular and Cellular Neuroscience |
| Volume | 24 |
| Issue number | 4 |
| DOIs | |
| State | Published - Dec 1 2003 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Molecular Biology
- Cellular and Molecular Neuroscience
- Developmental Neuroscience
Cite this
N-terminal α-dystroglycan binds to different extracellular matrix molecules expressed in regenerating peripheral nerves in a protein-mediated manner and promotes neurite extension of PC12 cells. / Hall, Heike; Bozic, Damir; Michel, Kathrin; Hubbell, Jeffrey A.
In: Molecular and Cellular Neuroscience, Vol. 24, No. 4, 01.12.2003, p. 1062-1073.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - N-terminal α-dystroglycan binds to different extracellular matrix molecules expressed in regenerating peripheral nerves in a protein-mediated manner and promotes neurite extension of PC12 cells
AU - Hall, Heike
AU - Bozic, Damir
AU - Michel, Kathrin
AU - Hubbell, Jeffrey A.
PY - 2003/12/1
Y1 - 2003/12/1
N2 - α-dystroglycan is a cell surface receptor that is expressed in many tissues including the nervous system. The study shows that a recombinant, non-glycosylated N-terminal fragment of α-dystroglycan comprising residues 30 to 315 [αDG (30-315)] bound to laminin-2/-4 and laminin-1, fibronectin and fibrinogen, all molecules highly upregulated in the regenerating peripheral nerve. The interaction was concentration dependent and saturable and could not be inhibited by heparin suggesting only minor involvement of sulfated carbohydrate moieties. In contrast to published data, addition of bivalent cations increased the binding affinity by only ten fold. αDG (30-315) promotes neurite extension of PC12 cells in a similar amount as described for laminin isoforms and could be inhibited in a concentration dependent manner by αDG (30-315) itself, soluble laminin-1, partially by heparin, EDTA, and an RGD-peptide. Furthermore, co-immunoprecipitations between α-dystroglycan and β1-integrin from PC12 cell surfaces suggested complex interactions between neuronal dystroglycan, integrins, and the ECM that induce neurite extension in vitro.
AB - α-dystroglycan is a cell surface receptor that is expressed in many tissues including the nervous system. The study shows that a recombinant, non-glycosylated N-terminal fragment of α-dystroglycan comprising residues 30 to 315 [αDG (30-315)] bound to laminin-2/-4 and laminin-1, fibronectin and fibrinogen, all molecules highly upregulated in the regenerating peripheral nerve. The interaction was concentration dependent and saturable and could not be inhibited by heparin suggesting only minor involvement of sulfated carbohydrate moieties. In contrast to published data, addition of bivalent cations increased the binding affinity by only ten fold. αDG (30-315) promotes neurite extension of PC12 cells in a similar amount as described for laminin isoforms and could be inhibited in a concentration dependent manner by αDG (30-315) itself, soluble laminin-1, partially by heparin, EDTA, and an RGD-peptide. Furthermore, co-immunoprecipitations between α-dystroglycan and β1-integrin from PC12 cell surfaces suggested complex interactions between neuronal dystroglycan, integrins, and the ECM that induce neurite extension in vitro.
UR - http://www.scopus.com/inward/record.url?scp=0345863398&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0345863398&partnerID=8YFLogxK
U2 - 10.1016/j.mcn.2003.08.007
DO - 10.1016/j.mcn.2003.08.007
M3 - Article
C2 - 14697669
AN - SCOPUS:0345863398
VL - 24
SP - 1062
EP - 1073
JO - Molecular and Cellular Neuroscience
JF - Molecular and Cellular Neuroscience
SN - 1044-7431
IS - 4
ER -