Results 131 to 140 of about 1,094 (157)
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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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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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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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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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Crystal structure of saposin D in an open conformation
Journal of Structural Biology, 2018Saposins are accessory proteins that aid in the degradation of sphingolipids by hydrolytic enzymes. Their structure usually comprises four α-helices arranged in various conformations including an open, V-shaped form that is generally associated with the ability to interact with membranes and/or enzymes to accentuate activity.
Ahmad, Gebai +2 more
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Phospholipid vesicle fusion induced by saposin C
Archives of Biochemistry and Biophysics, 2003Saposin C is a small Trp-free, multifunctional glycoprotein that enhances the hydrolytic activity of acid beta-glucosidase in lysosomes. Saposin C's functions have been shown to include neuritogenic/neuroprotection effects and membrane fusion induction.
Ying, Wang +2 more
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Saposins (sap) A and C activate the degradation of galactosylsphingosine
FEBS Letters, 2001Klaus Harzer, M Hiraiwa, B C Paton
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