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Structure, 2008 SummaryHuman saposins are essential proteins required for degradation of sphingolipids and lipid antigen presentation. Despite the conserved structural organization of saposins, their distinct modes of interaction with biological membranes are not fully ...
Maxim Rossmann +2 more
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Saposins utilize two strategies for lipid transfer and CD1 antigen presentation [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 2012 Transferring lipid antigens from membranes into CD1 antigen-presenting proteins represents a major molecular hurdle necessary for T-cell recognition. Saposins facilitate this process, but the mechanisms used are not well understood. We found that saposin
Luis Leon +2 more
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Combined saposin deficiency: A rare occurrence
Medical Journal Armed Forces India, 2023Combined saposin deficiency (OMIM #611721), an exceedingly rare lysosomal storage disorder, is caused by a mutation in the gene PSAP. This gene encodes a protein, prosaposin, that cleaves into four constituent proteins, each of which has a role as a cofactor for the enzymes whose deficiency results in Krabbe disease, metachromatic leukodystrophy ...
Vivek Bhat +3 more
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Saposins and Their Interaction with Lipids
Neurochemical Research, 1999The lysosomal degradation of several sphingolipids requires the presence of four small glycoproteins called saposins, generated by proteolytic processing of a common precursor, prosaposin. Saposins share several structural properties, including six similarly located cysteines forming three disulfide bridges with the same cysteine pairings.
A M, Vaccaro +3 more
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The primary structure of mouse saposin
Biochemical and Biophysical Research Communications, 1992The primary structure of mouse sphingolipid activator protein (saposin) was determined by cDNA sequencing. The amino acid sequence predicted by the cDNA sequence revealed that mouse saposin was highly homologous to human saposin and also to rat sertoli cell glycoprotein.
M, Tsuda +3 more
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Fusogenic domain and lysines in saposin C
Archives of Biochemistry and Biophysics, 2004Saposin C, a sphingolipid activator protein with fusogenic activity, interacts specifically with the membrane containing negatively charged, unsaturated phospholipids. The kinetics and mechanism of saposin C-induced membrane fusion were previously investigated using acidic phospholipid liposomes. A hypothetic clip-on model for such a fusion process was
Xiaoyang, Qi, Zhengtao, Chu
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Characterizing the Size and Composition of Saposin A Lipoprotein Picodiscs
Analytical Chemistry, 2016Saposin A (SapA) lipoprotein discs, also known as picodiscs (PDs), represent an attractive method to solubilize glycolipids for protein interaction studies in aqueous solution. Recent electrospray ionization mass spectrometry (ESI-MS) data suggest that the size and composition of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC)-containing PDs at
Richards, Michele R. +7 more
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Structural and membrane‐binding properties of saposin D
European Journal of Biochemistry, 1999Saposin D is generated together with three similar proteins, saposins A, B and C, from a common precursor, called prosaposin, in acidic organelles such as late endosomes and lysosomes. Although saposin D has been reported to stimulate the enzymatic hydrolysis of sphingomyelin and ceramide, its physiological role has not yet been clearly established. In
TATTI M. +6 more
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Expression and Characterization of Saposin-Like Proteins
2000The 79 residue mature surfactant protein B is formed by proteolytic cleavage from a larger precursor. SP-B belongs to the family of saposin-like proteins and has unique functional roles in pulmonary surfactant. The 381-residue human proSP-B fused to an N-terminal poly-His tag was expressed in E.
S, Zaltash, J, Johansson
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Direct Visualization of Saposin Remodelling of Lipid Bilayers
Journal of Molecular Biology, 2006Saposins A, B, C and D are soluble, non-enzymatic proteins that interact with lysosomal membranes to activate the breakdown and transfer of glycosphingolipids. The mechanisms of hydrolase activation and lipid transfer by saposins remain unknown. We have used in situ atomic force microscopy (AFM) with simultaneous confocal fluorescence microscopy to ...
Jean-René, Alattia +3 more
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