Demonstration of lysosomal localization for the mammalian ependymin-related protein using classical approaches combined with a novel density shift method.

Demonstration of lysosomal localization for the mammalian ependymin-related protein using classical approaches combined with a novel density shift method. Research Abstract Details 

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Demonstration of lysosomal localization for the mammalian ependymin-related protein using classical approaches combined with a novel density shift method. Abstract Text:

Maria Cecilia Della Valle,David E Sleat,Istvan Sohar,Ting Wen,John E Pintar,Michel Jadot,Peter Lobel,

Most newly synthesized soluble lysosomal proteins are delivered to the lysosome via the mannose 6-phosphate (Man-6-P)-targeting pathway. The presence of the Man-6-P post-translational modification allows these proteins to be affinity-purified on immobilized Man-6-P receptors. This approach has formed the basis for a number of proteomic studies that identified multiple as yet uncharacterized Man-6-P glycoproteins that may represent new lysosomal proteins. Although the presence of Man-6-P is suggestive of lysosomal function, the subcellular localization of such candidates requires experimental verification. Here, we have investigated one such candidate, ependymin-related protein (EPDR). EPDR is a protein of unknown function with some sequence similarity to ependymin, a fish protein thought to play a role in memory consolidation and learning. Using classical subcellular fractionation on rat brain, EPDR co-distributes with lysosomal proteins, but there is significant overlap between lysosomal and mitochondrial markers. For more definitive localization, we have developed a novel approach based upon a selective buoyant density shift of the brain lysosomes in a mutant mouse lacking NPC2, a lysosomal protein involved in lipid transport. EPDR, in parallel with lysosomal markers, shows this density shift in gradient centrifugation experiments comparing mutant and wild type mice. This approach, combined with morphological analyses, demonstrates that EPDR resides in the lysosome. In addition, the lipidosis-induced density shift approach represents a valuable tool for identification and validation of both luminal and membrane lysosomal proteins that should be applicable to high throughput proteomic studies.

Demonstration of lysosomal localization for the mammalian ependymin-related protein using classical approaches combined with a novel density shift method. Publishing Authors By Initials

MC Della Valle,DE Sleat,I Sohar,T Wen,JE Pintar,M Jadot,P Lobel,

For similar proteins: membrane proteins: vesicular transport proteins research abstracts see: proteins: membrane proteins: vesicular transport proteins research

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Demonstration of lysosomal localization for the mammalian ependymin-related protein using classical approaches combined with a novel density shift method. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 281

Page Numbers: 35436-45

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 5

MONTH: 09

YEAR: 2006

Demonstration of lysosomal localization for the mammalian ependymin-related protein using classical approaches combined with a novel density shift method. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Demonstration of lysosomal localization for the mammalian ependymin-related protein using classical approaches combined with a novel density shift method. Keywords Mesh Terms:

KEYWORDS: Vesicular Transport Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Demonstration of lysosomal localization for the mammalian ependymin-related protein using classical approaches combined with a novel density shift method. Information

Substance Name: mannose-6-phosphate

Registry Number: 3672-15-9

Grant and Affiliation Information for Demonstration of lysosomal localization for the mammalian ependymin-related protein using classical approaches combined with a novel density shift method.

AFFILIATION: Center for Advanced Biotechnology and Medicine, Department of Pharmacology, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.

Country: United States

AGENCY: United States NIDDK

GRANT: DK054317

ACRONYM: DK

MEDLINETA: J Biol Chem

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