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PMID: 9634556 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

rMAL is a glycosphingolipid-associated protein of myelin and apical membranes of epithelial cells in kidney and stomach.

The Journal of neuroscience : the official journal of the Society for Neuroscience ·Vol. 18 ·No. 13 ·1998-07-01 ·Pages 4901-13

Frank M, van der Haar ME, Schaeren-Wiemers N, Schwab ME

Abstract

rMAL, the rat myelin and lymphocyte protein, is a small hydrophobic protein of 17 kDa with four putative transmembrane domains and is expressed in oligodendrocytes and Schwann cells, the myelinating cells of the nervous system. In addition, transcript expression has been found in kidney, spleen, and intestine. Confocal microscopy and immunoelectron microscopy with an affinity-purified antibody localized rMAL to compact myelin in a pattern similar to the structural myelin proteins: myelin basic protein and proteolipid protein. In kidney and stomach epithelia, rMAL is located almost exclusively on the apical (luminal) membranes of the cells lining distal tubuli in kidney and the glandular part of the stomach. Biochemical analysis of plasma membranes isolated from spinal cord and kidney demonstrated that rMAL is a proteolipid that is present in detergent insoluble complexes typical for proteins associated with glycosphingolipids. Lipid and protein analysis showed a co-enrichment of glycosphingolipids and rMAL protein within these complexes, indicating a close association of rMAL to glycosphingolipids in myelin and in kidney in vivo. We conclude that specific rMAL-glycosphingolipid interactions may lead to the formation and maintenance of stable protein-lipid microdomains in myelin and apical epithelial membranes. They may contribute to specific properties of these highly specialized plasma membranes.

MeSH Terms
Animals Antibody Specificity Brain Chemistry/physiology Detergents Epithelial Cells/chemistry Galactosylceramides/analysis Gene Expression/physiology Glycosphingolipids/analysis Kidney/chemistry,cytology Lymphocytes/chemistry Membrane Proteins/analysis Myelin Sheath/chemistry Nerve Tissue Proteins/analysis,genetics,immunology Peripheral Nervous System/chemistry RNA, Messenger/analysis Rats Rats, Inbred Lew Solubility Spinal Cord/chemistry Spleen/chemistry Stomach/chemistry,cytology Sulfoglycosphingolipids/analysis Thymus Gland/chemistry
Chemicals
Detergents Galactosylceramides Glycosphingolipids Membrane Proteins Nerve Tissue Proteins RNA, Messenger Sulfoglycosphingolipids
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Frank M
Research Institute, University of Zurich and Swiss Federal Institute of Technology Zurich, CH-8029 Zurich, Switzerland.
van der Haar M E
Schaeren-Wiemers N
Schwab M E
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Article Info
Journal
The Journal of neuroscience : the official journal of the Society for Neuroscience
Abbr.
J Neurosci
ISSN
0270-6474
Published
1998-07-01
Pages
4901-13
Language
English
Region
United States
NLM ID
8102140
PMCID
PMC6792556
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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