Disease relevance of Mal

• SAR and pharmacokinetic studies on phenethylamide inhibitors of the hepatitis C virus NS3/NS4A serine protease [1].

High impact information on Mal

• We have isolated a rat cDNA, initially denominated NS 3, that is mainly expressed in the myelinating cells of the nervous system, the oligodendrocytes and Schwann cells [2].
• The putative NS 3 protein lacks a N-terminal hydrophobic leader sequence and has no consensus sequence for N-linked glycosylation [2].
• Sequence analysis showed that NS 3 is the rat homolog of a human gene called MAL that was cloned from, and is expressed in various T-cell lines [2].
• The expression of Mal mRNA is highly restricted to the brain and testis [3].
• Probing of a human complementary DNA library with anti-Ma serum resulted in the cloning of a gene that encodes a novel 37 kDa protein (Mal) [3].

Biological context of Mal

• The corresponding MVP17 cDNA was isolated from an oligodendrocyte cDNA library [4].
• These data suggest that MVP17 is involved in myelin biogenesis and/or myelin function [4].
• We previously identified the presence of DIGCEMs in oligodendrocytes in culture and purified myelin and characterized a novel DIGCEM-associated tetraspan protein, MVP17/rMAL (Kim et al. (1995) Journal of Neuroscience Research 42, 413-422) [5].

Anatomical context of Mal

• A developmentally regulated protein, MVP17 (myelin vesicular protein of 17 kDa), was identified [4].
• Expression of full-length constructs of MVP17/rMAL in COS-7 cells resulted in an enlargement of transfected COS-7 cells, consistent with a proposed role of rMAL in vesicular trafficking [6].

Other interactions of Mal

• The MAL (MAL, MVP17, VIP17) proteolipid, an integral membrane protein present in DIGs in mature oligodendrocytes, has been proposed as a component of the machinery for DIG-mediated transport in a restricted pattern of cell types including myelinating cells [7].

References