PMID- 8996823
OWN - NLM
STAT- MEDLINE
DCOM- 19970529
LR  - 20190815
IS  - 0953-816X (Print)
IS  - 0953-816X (Linking)
VI  - 8
IP  - 12
DP  - 1996 Dec
TI  - Dystroglycan in the cerebellum is a laminin alpha 2-chain binding protein at the 
      glial-vascular interface and is expressed in Purkinje cells.
PG  - 2739-47
AB  - Dystroglycan is a core component of the dystrophin receptor complex in skeletal 
      muscle which links the extracellular matrix to the muscle cytoskeleton. 
      Dystrophin, dystrophin-related protein (DRP, utrophin) and dystroglycan are 
      present not only in muscles but also in the brain. Dystrophin is expressed in 
      certain neuronal populations while DRP is associated with perivascular 
      astrocytes. To gain insights into the function and molecular interactions of 
      dystroglycan in the brain, we examined the localization of alpha- and 
      beta-dystroglycan at the cellular and subcellular levels in the rat cerebellum. 
      In blood vessels, we find alpha-dystroglycan associated with the laminin alpha 
      2-chain-rich parenchymal vascular basement membrane and beta-dystroglycan 
      associated with the endfeet of perivascular astrocytes. We also show that 
      alpha-dystroglycan purified from the brain binds alpha 2-chain-containing 
      laminin-2. These observations suggest a dystroglycan-mediated linkage between DRP 
      in perivascular astrocytic endfeet and laminin-2 in the parenchymal basement 
      membrane similar to that described in skeletal muscle. This linkage of the 
      astrocytic endfeet to the vascular basement membrane is likely to be important 
      for blood vessel formation and stabilization and for maintaining the integrity of 
      the blood-brain barrier. In addition to blood vessel labelling, we show that 
      alpha-dystroglycan in the rat cerebellum is associated with the surface of 
      Purkinje cell bodies, dendrites and dendritic spines. Dystrophin has previously 
      been localized to the inner surface of the plasma membrane of Purkinje cells and 
      is enriched at postsynaptic sites. Thus, the present results also support the 
      hypothesis that dystrophin interacts with dystroglycan in cerebellar Purkinje 
      neurons.
FAU - Tian, M
AU  - Tian M
AD  - Gerontology Research Center, National Institute on Aging, National Institute of 
      Health, Baltimore, MD 21224, USA.
FAU - Jacobson, C
AU  - Jacobson C
FAU - Gee, S H
AU  - Gee SH
FAU - Campbell, K P
AU  - Campbell KP
FAU - Carbonetto, S
AU  - Carbonetto S
FAU - Jucker, M
AU  - Jucker M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - France
TA  - Eur J Neurosci
JT  - The European journal of neuroscience
JID - 8918110
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (Laminin)
RN  - 0 (Membrane Glycoproteins)
RN  - 146888-27-9 (Dystroglycans)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Blood Vessels/metabolism/ultrastructure
MH  - Cerebellum/blood supply/*metabolism/ultrastructure
MH  - Cytoskeletal Proteins/*metabolism
MH  - Dystroglycans
MH  - Immunohistochemistry
MH  - Laminin/*metabolism
MH  - Membrane Glycoproteins/*metabolism
MH  - Neuroglia/*metabolism
MH  - Purkinje Cells/*metabolism
MH  - Rats
MH  - Rats, Inbred F344
EDAT- 1996/12/01 00:00
MHDA- 1996/12/01 00:01
CRDT- 1996/12/01 00:00
PHST- 1996/12/01 00:00 [pubmed]
PHST- 1996/12/01 00:01 [medline]
PHST- 1996/12/01 00:00 [entrez]
AID - 10.1111/j.1460-9568.1996.tb01568.x [doi]
PST - ppublish
SO  - Eur J Neurosci. 1996 Dec;8(12):2739-47. doi: 10.1111/j.1460-9568.1996.tb01568.x.