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Collagen XVII and BPAG1 expression in the retina: Evidence for an anchoring complex in the central nervous system
Author(s) -
Claudepierre Thomas,
Manglapus Mary K.,
Marengi Nathan,
Radner Stephanie,
Champliaud MarieFrance,
Tasanen Kaisa,
BrucknerTuderman Leena,
Hunter Dale D.,
Brunken William J.
Publication year - 2005
Publication title -
journal of comparative neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.855
H-Index - 209
eISSN - 1096-9861
pISSN - 0021-9967
DOI - 10.1002/cne.20549
Subject(s) - biology , microbiology and biotechnology , hemidesmosome , extracellular matrix , gene isoform , retina , anatomy , neuroscience , basement membrane , genetics , gene
The ectoderm gives rise not only to the skin but also to the entire CNS. This common embryonic lineage suggests that some molecular isoforms might serve analogous functions in both tissues. Indeed, not only are laminins important components of dermal adhesion mechanisms, but they also regulate some aspects of synaptic development in both the CNS and the PNS. In the skin, laminins are part of a hemidesmosome complex essential for basal keratinocyte adhesion that includes collagen XVII (BP180) and BPAG1 (dystonin/BP230). Here, we show that CNS neurons also express collagen XVII and BPAG1 and that these molecules are expressed in the adult and developing retina. In the retina, isoforms of collagen XVII and BPAG1 are colocalized with laminins at photoreceptor synapses and around photoreceptor outer segments; both molecules are expressed by rods, whereas cones express collagen XVII but not BPAG1. Moreover, biochemical data demonstrate that collagen XVII complexes with retinal laminins. We propose that collagen XVII and BPAG1 isoforms may help to anchor elements of the rod photoreceptor cytomatrix to the extracellular matrix. J. Comp. Neurol. 487:190–203, 2005. © 2005 Wiley‐Liss, Inc.