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Expression of a beta 1-related integrin by oligodendroglia in primary culture: evidence for a functional role in myelination.
We have investigated the expression of integrins by rat oligodendroglia grown in primary culture and the functional role of these proteins in myelinogenesis. Immunochemical analysis, using antibodies to a number of alpha and beta integrin subunits, revealed that oligodendrocytes express only one detectable integrin receptor complex (alpha OL beta OL). This complex is immunoprecipitated by a polyclonal anti-human beta 1 integrin subunit antibody. In contrast, astrocytes, the other major glial cell type in brain, express multiple integrins including alpha 1 beta 1, alpha 3 beta 1, and alpha 5 beta 1 complexes that are immunologically and electrophoretically indistinguishable from integrins expressed by rat fibroblasts. The beta subunit of the oligodendrocyte integrin (beta OL) and rat fibroblast beta 1 have different electrophoretic mobilities in SDS-PAGE. However, the two beta subunits appear to be highly related based on immunological cross-reactivity and one-dimensional peptide mapping. After removal of N-linked carbohydrate chains, beta OL and beta 1 comigrated in SDS-PAGE and peptide maps of the two deglycosylated subunits were identical, suggesting differential glycosylation of beta 1 and beta OL accounts entirely for their size differences. The oligodendrocyte alpha subunit, alpha OL, was not immunoprecipitated by antibodies against well characterized alpha chains which are known to associate with beta 1 (alpha 3, alpha 4, and alpha 5). However, an antibody to alpha 8, a more recently identified integrin subunit, did precipitate two integrin subunits with electrophoretic mobilities in SDS-PAGE identical to alpha OL and beta OL. Functional studies indicated that disruption of oligodendrocyte adhesion to a glial-derived matrix by an RGD-containing synthetic peptide resulted in a substantial decrease in the level of mRNAs for several myelin components including myelin basic protein (MBP), proteolipid protein (PLP), and cyclic nucleotide phosphodiesterase (CNP). These results suggest that integrin-mediated adhesion of oligodendrocytes may trigger signal(s) that induce the expression of myelin genes and thus influence oligodendrocyte differentiation
Optimal and efficient crossover designs for comparing test treatments with a control treatment
This paper deals exclusively with crossover designs for the purpose of
comparing t test treatments with a control treatment when the number of periods
is no larger than t+1. Among other results it specifies sufficient conditions
for a crossover design to be simultaneously A-optimal and MV-optimal in a very
large and appealing class of crossover designs. It is expected that these
optimal designs are highly efficient in the entire class of crossover designs.
Some computationally useful tools are given and used to build assorted small
optimal and efficient crossover designs. The model robustness of these newly
discovered crossover designs is discussed.Comment: Published at http://dx.doi.org/10.1214/009053604000000887 in the
Annals of Statistics (http://www.imstat.org/aos/) by the Institute of
Mathematical Statistics (http://www.imstat.org
A generalization of sum composition: Self orthogonal Latin square design with sub self orthogonal Latin square designs
AbstractA generalization of the theory of sum composition of Latin square designs is given. Via this generalized theory it is shown that a self orthogonal Latin square design of order (3pα − 1)2 with a subself orthogonal Latin square design of order (pα − 1)2 can be constructed for any prime p > 2 and any positive integer α as long as p ≠3, 5, 7 and 13 if α = 1. Additional results concerning sets of orthogonal Latin square designs are also provided
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