Results 1 to 10 of about 102 (92)
A Comparative Study of Human Saposins [PDF]
Molecules, 2018 Saposins are small proteins implicated in trafficking and loading of lipids onto Cluster of Differentiation 1 (CD1) receptor proteins that in turn present lipid antigens to T cells and a variety of T-cell receptors, thus playing a crucial role in innate ...
Luis F Pacios +2 more
exaly +5 more sources
Crystal structures of saposins A and C [PDF]
Protein Science, 2006 AbstractSaposins A and C are sphingolipid activator proteins required for the lysosomal breakdown of galactosylceramide and glucosylceramide, respectively. The saposins interact with lipids, leading to an enhanced accessibility of the lipid headgroups to their cognate hydrolases.
Gilbert Prive
exaly +3 more sources
The Immunological Functions of Saposins [PDF]
Advances in Immunology, 2010 Saposins or sphingolipid activator proteins (SAPs) are small, nonenzymatic glycoproteins that are ubiquitously present in lysosomes. SAPs comprise the five molecules saposins A-D and the GM2 activator protein. Saposins are essential for sphingolipid degradation and membrane digestion.
Florian Winau
exaly +3 more sources
Saposin B binds and transfers phospholipids [PDF]
Journal of Lipid Research, 2006 Saposin B (Sap B) is a member of a family of four small glycoproteins, Sap A, B, C, and D. Like the other three saposins, Sap B plays a physiological role in the lysosomal degradation of sphingolipids (SLs). Although the interaction of Sap B with SLs has
Fiorella Ciaffoni +6 more
doaj +5 more sources
Effect of saposins on acid sphingomyelinase [PDF]
Biochemical Journal, 1993 The effect of saposins (A, B, C and D) on acid sphingomyelinase activity was determined using a crude human kidney sphingomyelinase preparation and a purified sphingomyelinase preparation from human placenta. Saposin D stimulated the activity of the crude enzyme by increasing its apparent Km and Vmax. values for sphingomyelin hydrolysis.
Kishimoto Y
exaly +3 more sources
Saposins: structure, function, distribution, and molecular genetics.
Journal of Lipid Research, 1992 Saposins A, B, C, and D are small heat-stable glycoproteins derived from a common precursor protein, prosaposin. These mature saposins, as well as prosaposin, activate several lysosomal hydrolases involved in the metabolism of various sphingolipids.
M Hiraiwa
exaly +3 more sources
Journal of Biological Chemistry, 1994 Small (80-amino acid) glycoproteins or saposins are important for the in vivo function of several lysosomal hydrolases. Four saposins, A, B, C, and D, are encoded by a single locus termed prosaposin. Saposins C and A are thought to function in vivo as activators of acid beta-glucosidase.
Xiaoyang Qi, G A Grabowski
exaly +3 more sources
PLoS ONE, 2021 Prosaposin (PSAP), a highly conserved glycoprotein, is a precursor of saposins A-D. Accumulating evidence suggests that PSAP is a neurotrophic factor, as well as a regulator of lysosomal enzymes. Recently, the orphan G-protein-coupled receptors GPR37 and
Miho Taniguchi +10 more
doaj +2 more sources
Altered autophagy in the mice with a deficiency of saposin A and saposin B [PDF]
Autophagy, 2013 Combined saposin A and saposin B deficiency (AB(-/-)) was created in mice by knock-in of point mutations into the saposin A and B domains of the Psap (encoding prosaposin) locus. PSAP is the precursor of saposin A, saposin B and two other members, saposin C and saposin D.
Ying, Sun, Gregory A, Grabowski
openaire +2 more sources
A Tetrameric Assembly of Saposin A: Increasing Structural Diversity in Lipid Transfer Proteins
Contact, 2021 Saposins are lipid transfer proteins required for the degradation of sphingolipids in the lysosome. These small proteins bind lipids by transitioning from a closed, monomeric state to an open conformation exposing a hydrophobic surface that binds and ...
Maria Shamin +3 more
doaj +1 more source