Results 141 to 150 of about 1,124 (173)
Archives of Biochemistry and Biophysics, 1997 Saposins A, B, C, and D, which are required for the enzymatic hydrolysis of sphingolipids by specific lysosomal hydrolases, are produced by proteolytic processing of their common precursor protein, prosaposin.
Shoji Tsuji +2 more
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Crystal Structures of Human Saposins C and D: Implications for Lipid Recognition and Membrane Interactions [PDF]
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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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.
J W Callahan, J S O'Brien, M Hiraiwa
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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.
Rosa Salvioli +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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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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Characterization of Human Saposins by NMR Spectroscopy†
Biochemistry, 2006Saposins are lipid-binding and membrane-perturbing glycoproteins of the mammalian lysosomes involved in sphingolipid and membrane digestion. Although the four human saposins (Saps), A-D, are sequence-related, they are responsible for the activation of different steps in the cascade of lysosomal glycosphingolipid degradation. Saposin activity is maximal
Michael John +2 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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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
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