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Human Molecular Genetics Advance Access published online on May 14, 2008

Human Molecular Genetics, doi:10.1093/hmg/ddn135
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© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Neurological deficits and glycosphingolipid accumulation in Saposin B deficient mice

Ying Sun1,4, David P. Witte3,5, Huimin Ran1, Matt Zamzow1, Sonya Barnes1, Hua Cheng6, Xianlin Han6, Michael T. Williams2,4, Matthew R. Skelton2,4, Charles V. Vorhees2,4 and Gregory A. Grabowski1,4,*

1 The Division of Human Genetics, University of Cincinnati College of Medicine, Cincinnati, OH 45229-3039 2 Division of Neurology, University of Cincinnati College of Medicine, Cincinnati, OH 45229-3039 3 Division of Pediatric Pathology, Cincinnati Children's Hospital Medical Center and Departments of Pediatrics, University of Cincinnati College of Medicine, Cincinnati, OH 45229-3039 4 Departments of Pediatrics, University of Cincinnati College of Medicine, Cincinnati, OH 45229-3039 5 Departments of Pathology, University of Cincinnati College of Medicine, Cincinnati, OH 45229-3039 6 Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110

* Correspondence to: Gregory A. Grabowski, M.D., Cincinnati Children's Hospital Medical Center, Division of Human Genetics, 3333 Burnet Avenue, MLC 4006, Cincinnati, OH 45229-3039, Phone: (513) 636-7290, Fax: (513) 636-2261, E-mail address: greg.grabowski{at}cchmc.org

Received March 13, 2008; Revised April 21, 2008; Accepted April 21, 2008

Saposin B derives from the multi-functional precursor, prosaposin, and functions as an activity enhancer for several glycosphingolipid (GSL) hydrolases. Mutations in saposin B present in humans with phenotypes resembling metachromatic leukodystrophy. To gain insight into saposin B's physiological functions, a specific deficiency was created in mice by a knock-in mutation of an essential cysteine in exon 7 of the prosaposin locus. No saposin B protein was detected in the homozygotes (B-/-) mice, while prosaposin, and saposins A, C, and D were at normal levels. B-/- mice exhibited slowly progressive neuromotor deterioration and minor head tremor by 15 months. Excess hydroxy and non-hydroxy fatty acid sulfatide levels were present in brain and kidney. Alcian blue positive (sulfatide) storage cells were found in the brain, spinal cord, and kidney. Ultrastructural analyses showed lamellar inclusion material in the kidney, sciatic nerve, brain and spinal cord tissues. Lactosylceramide (LacCer) and globotriaosylceramide (TriCer) were increased in various tissues of B-/- mice supporting the in vivo role of saposin B in the degradation of these lipids. CD68 positive microglial cells and activated GFAP positive astrocytes showed a proinflammatory response in the brains of B-/- mice. These findings delineate the roles of saposin B for the in vivo degradation of several GSLs and its primary function in maintenance of CNS function. Saposin B deficient mice provide a useful model for understanding the contributions of this saposin to GSL metabolism and homeostasis.


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