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[Abstract Title]. - Society for Neuroscience

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ostral CC, while myelinated or demyelinated axons had respectively similar diameters within<br />

each region. Neurofilament dephosphorylation, an indictor of disrupted axonal cytoskeletal<br />

structure, was also more extensive in the caudal versus rostral CC. Our data in this cuprizone<br />

model demonstrate that the early progression of pathology is more advanced in the caudal CC.<br />

Furthermore, DTI axial diffusivity may be more sensitive to the disruption of neurofilament<br />

structural integrity and less indicative of axonal atrophy. Supported by NIH NS39293, NMSS<br />

RG3515 and DBSCIP F170TP.<br />

Disclosures: J.E. Tobin, None; M. Xie, None; S. Song, None; T.Q. Le, None; D. McDaniel,<br />

None; R.C. Armstrong, None.<br />

Poster<br />

251. Demyelinating Disorders: Animal Models and Human Studies I<br />

Time: Sunday, November 16, 2008, 1:00 pm - 5:00 pm<br />

Program#/Poster#: 251.14/W7<br />

Topic: C.08.b. Animal models<br />

Support: grant EU-NEST 1702<br />

SNSF Grant PP00A-106714<br />

Grant GM-28140<br />

Grant SSMBS1140<br />

<strong>Title</strong>: Phosphatidic acid mediates demyelination in Lpin1 mutant mice<br />

Authors: K. NADRA 1 , A.-S. DE PREUX CHARLES 1 , J.-J. MÉDARD 1 , W. T. HENDRIKS 2 ,<br />

G.-S. HAN 3 , S. GRÈS 4 , G. M. CARMAN 3 , J.-S. SAULNIER-BLACHE 4 , M. H. G.<br />

VERHEIJEN 2 , *R. CHRAST 1 ;<br />

1 Dept Med. Genet, Univ. Lausanne, Lausanne, Switzerland; 2 Dept. of Mol. and Cell. Neurobio.,<br />

Vrije Univ., Amsterdam, Netherlands; 3 Dept. of Food Sci., Rutgers Univ., New Brunswick, NJ;<br />

4 Dept. of Metabolism and Obesity, INSERM, U858/I2MR, Toulouse, France<br />

<strong>Abstract</strong>: Lipids play crucial roles in many aspects of glial cell biology, affecting processes<br />

ranging from myelin membrane biosynthesis to axo-glial interactions. In order to study the role<br />

of lipid metabolism in myelinating glial cells, we specifically deleted in Schwann cells the Lpin1<br />

gene, which encodes the Mg2+-dependent phosphatidate phosphatase (PAP1) enzyme necessary<br />

<strong>for</strong> normal triacylglycerol biosynthesis. The affected animals developed pronounced peripheral

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