NDLI: Nfasc155H and MAG are Specifically Susceptible to Detergent Extraction in the Absence of the Myelin Sphingolipid Sulfatide

Content Provider	Springer Nature Link
Author	Pomicter, A. D. DeLoyht, J. M. Hackett, A. R. Purdie, N. Sato Bigbee, C. Henderson, S. C. Dupree, J. L.
Copyright Year	2013
Abstract	Mice incapable of synthesizing the myelin lipid sulfatide form paranodes that deteriorate with age. Similar instability also occurs in mice that lack contactin, contactin-associated protein or neurofascin155 (Nfasc155), the proteins that cluster in the paranode and form the junctional complex that mediates myelin-axon adhesion. In contrast to these proteins, sulfatide has not been shown to be enriched in the paranode nor has a sulfatide paranodal binding partner been identified; thus, it remains unclear how the absence of sulfatide results in compromised paranode integrity. Using an in situ extraction procedure, it has been reported that the absence of the myelin sphingolipids, galactocerebroside and sulfatide, increased the susceptibility of Nfasc155 to detergent extraction. Here, employing a similar approach, we demonstrate that in the presence of galactocerebroside but in the absence of sulfatide Nfasc155 is susceptible to detergent extraction. Furthermore, we use this in situ approach to show that stable association of myelin-associated glycoprotein (MAG) with the myelin membrane is sulfatide dependent while the membrane associations of myelin/oligodendrocyte glycoprotein, myelin basic protein and cyclic nucleotide phosphodiesterase are sulfatide independent. These findings indicate that myelin proteins maintain their membrane associations by different mechanisms. Moreover, the myelin proteins that cluster in the paranode and require sulfatide mediate myelin-axon adhesion. Additionally, the apparent dependency on sulfatide for maintaining Nfasc155 and MAG associations is intriguing since the fatty acid composition of sulfatide is altered and paranodal ultrastructure is compromised in multiple sclerosis. Thus, our findings present a potential link between sulfatide perturbation and myelin deterioration in multiple sclerosis.
Starting Page	2490
Ending Page	2502
Page Count	13
File Format	PDF
ISSN	03643190
Journal	Neurochemical Research
Volume Number	38
Issue Number	12
e-ISSN	15736903
Language	English
Publisher	Springer US
Publisher Date	2013-10-02
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Sulfatide Neurofascin Membrane rafts Myelin Neurosciences Neurochemistry Biochemistry Cell Biology Neurology
Content Type	Text
Resource Type	Article
Subject	Medicine Biochemistry Cellular and Molecular Neuroscience

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Nfasc155H and MAG are specifically susceptible to detergent extraction in the absence of the myelin sphingolipid sulfatide

The Role of 3-O-Sulfogalactosylceramide, Sulfatide, in the Lateral Organization of Myelin Membrane

White Matter Rafting––Membrane Microdomains in Myelin

Compromised Myelin and Axonal Molecular Organization Following Adult-Onset Sulfatide Depletion.

Remodeling of Sphingolipids by Plasma Membrane Associated Enzymes

Abnormal Gangliosides are Localized in Lipid Rafts in Sanfilippo (MPS3a) Mouse Brain

Essential Roles of Gangliosides in the Formation and Maintenance of Membrane Microdomains in Brain Tissues

Mini Review: Immune Response to Myelin-Derived Sulfatide and CNS-Demyelination

Regulatory Mechanisms of Nervous Systems with Glycosphingolipids

Nfasc155H and MAG are Specifically Susceptible to Detergent Extraction in the Absence of the Myelin Sphingolipid Sulfatide

Similar Documents

Nfasc155H and MAG are specifically susceptible to detergent extraction in the absence of the myelin sphingolipid sulfatide

The Role of 3-O-Sulfogalactosylceramide, Sulfatide, in the Lateral Organization of Myelin Membrane

White Matter Rafting––Membrane Microdomains in Myelin

Compromised Myelin and Axonal Molecular Organization Following Adult-Onset Sulfatide Depletion.

Remodeling of Sphingolipids by Plasma Membrane Associated Enzymes

Abnormal Gangliosides are Localized in Lipid Rafts in Sanfilippo (MPS3a) Mouse Brain

Essential Roles of Gangliosides in the Formation and Maintenance of Membrane Microdomains in Brain Tissues

Mini Review: Immune Response to Myelin-Derived Sulfatide and CNS-Demyelination

Regulatory Mechanisms of Nervous Systems with Glycosphingolipids

Nfasc155H and MAG are Specifically Susceptible to Detergent Extraction in the Absence of the Myelin Sphingolipid Sulfatide