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  • Title: Structural and biochemical similarities reveal a family of proteins related to the MAL proteolipid, a component of detergent-insoluble membrane microdomains.
    Author: Pérez P, Puertollano R, Alonso MA.
    Journal: Biochem Biophys Res Commun; 1997 Mar 27; 232(3):618-21. PubMed ID: 9126323.
    Abstract:
    The MAL gene encodes a proteolipid protein displaying a cell type-specific pattern of expression, including T lymphocytes, myelin-forming cells, and epithelial renal MDCK cells, which has been recently identified as a component of detergent-insoluble membranes known to be enriched in glycolipids and cholesterol. Sequence alignment revealed a high degree of conservation of the MAL protein across species and evidenced the existence of a significant level of overall identity between MAL and two other proteins, BENE and the plasmolipin proteolipid. Moreover, using subcellular fractionation of transiently transfected COS-7 cells, both MAL and BENE were identified in detergent-resistant membranes. These results suggest the existence of a novel family of MAL-related proteins (including MAL, BENE, and plasmolipin) with primary structure homologies and with the distinctive features of having unusual biochemical properties such as lipid-like behaviour and/or the ability to reside in glycolipid-enriched membrane microdomains.
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