Results 211 to 220 of about 1,668,301 (239)
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Journal of molecular neuroscience : MN, 1990
Mixed oligonucleotide primers complementary to the translation product of the sphingolipid activator protein (SAP)-2 were used to generate a 144-base pair (bp) complementary DNA (cDNA). This cDNA probe was used to isolate a 2,649-nucleotide-long cDNA that was sequenced and found to contain coding sequences for two known activators of lysosomal enzymes,
O, Reiner, O, Dagan, M, Horowitz
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Mixed oligonucleotide primers complementary to the translation product of the sphingolipid activator protein (SAP)-2 were used to generate a 144-base pair (bp) complementary DNA (cDNA). This cDNA probe was used to isolate a 2,649-nucleotide-long cDNA that was sequenced and found to contain coding sequences for two known activators of lysosomal enzymes,
O, Reiner, O, Dagan, M, Horowitz
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Biochemical, immunological, and structural studies on a sphingolipid activator protein (SAP-1)
Archives of Biochemistry and Biophysics, 1984Sphingolipid activator protein-1 (SAP-1) is a glycoprotein found in human tissue extracts that stimulates the enzymatic hydrolysis of at least two glycosphingolipids, including GM1 ganglioside and sulfatide. The ability of purified SAP-1 to stimulate GM1 ganglioside hydrolysis by extracts of cultured fibroblasts from patients with beta-galactosidase ...
K, Inui, D A, Wenger
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The Histochemical Journal, 1996
Congenital nephrotic syndrome of the Finnish type is a recessively inherited renal disease with glomerular deposits of the disialoganglioside O-acetyl-GD3. Sphingolipid activator proteins (saposins) stimulate the degradation of glycosphingolipids by lysosomal enzymes, and defects in saposins cause accumulation of substrate lipids in the affected ...
A, Haltia +5 more
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Congenital nephrotic syndrome of the Finnish type is a recessively inherited renal disease with glomerular deposits of the disialoganglioside O-acetyl-GD3. Sphingolipid activator proteins (saposins) stimulate the degradation of glycosphingolipids by lysosomal enzymes, and defects in saposins cause accumulation of substrate lipids in the affected ...
A, Haltia +5 more
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Biochemical and Biophysical Research Communications, 1986
A cDNA coding for SAP-1 was isolated from a lambda gt11 human hepatoma expression library using polyclonal antibodies raised against human SAP-1. Three positive clones were isolated with inserts of approximately 0.3 Kb (S1.1), 2 Kb (S1.2) and 2.2 Kb (S-1.3). The latter 2 contained an internal EcoRI site.
N, Dewji +6 more
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A cDNA coding for SAP-1 was isolated from a lambda gt11 human hepatoma expression library using polyclonal antibodies raised against human SAP-1. Three positive clones were isolated with inserts of approximately 0.3 Kb (S1.1), 2 Kb (S1.2) and 2.2 Kb (S-1.3). The latter 2 contained an internal EcoRI site.
N, Dewji +6 more
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12 Activator Proteins for Sphingolipid Hydrolysis
1983Publisher Summary This chapter focuses on the various activator proteins used for the sphingolipid hydrolysis. Mraz et al. found that human hepatic activator protein that was specific for stimulating the hydrolysis of galactosylceramide sulfate by human enzyme could also stimulate the same reaction catalyzed by acidic sulfatases isolated from various
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[Disorders of sphingolipid activator proteins].
Nihon rinsho. Japanese journal of clinical medicine, 1996Small-molecular nonenzymatic glycoproteins are necessary for degradation of sphingolipids in lysosomes. GM2 activator encoded by a gene on chromosome 5 is essential for hydrolysis of ganglioside GM2 and its asialo derivative. Mutations of this gene cause Tay-Sachs disease-like clinical phenotype (GM2-gangliosidosis AB variant).
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The gene coding for a sphingolipid activator protein, SAP-1, is on human chromosome 10
Human Genetics, 1985SAP-1 is a sphingolipid activator protein found in human tissues required for the enzymatic hydrolysis of GM1 ganglioside and sulfatide. It appears to be missing in patients who have a genetic lipidosis resembling juvenile metachromatic leukodystrophy.
K, Inui +6 more
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Journal of Molecular Neuroscience, 1992
Saposins are a group of small glycoproteins derived from a single precursor protein, prosaposin. Each of the four saposins are involved in lysosomal hydrolysis of various sphingolipids. Our recent investigations have shown that saposins accumulate in tissues of several lysosomal storage diseases patients, including those with Tay-Sachs disease and ...
M, Tayama, J S, O'Brien, Y, Kishimoto
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Saposins are a group of small glycoproteins derived from a single precursor protein, prosaposin. Each of the four saposins are involved in lysosomal hydrolysis of various sphingolipids. Our recent investigations have shown that saposins accumulate in tissues of several lysosomal storage diseases patients, including those with Tay-Sachs disease and ...
M, Tayama, J S, O'Brien, Y, Kishimoto
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Expression of Sphingolipid Activator Protein Gene in Brain and Systemic Organs of Developing Mice
Developmental Neuroscience, 1994The sphingolipid activator proteins (SAPs) are a family of small, heat-stable glycoproteins, proven or postulated to be required for in vivo degradation of some sphingolipids by hydrolytic enzymes. Four of them are coded by a single gene, which generates a transcript including the four saps in tandem.
S M, Kreda, N, Fujita, K, Suzuki
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Biochemical and Biophysical Research Communications, 1988
The sphingolipid activator protein 1 (SAP-1) increases the rate of hydrolysis of sphingolipids in the lysosome by apparently bringing together the substrate and the corresponding hydrolytic enzyme. This implies specific recognition of both the substrate and enzyme by SAP-1.
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The sphingolipid activator protein 1 (SAP-1) increases the rate of hydrolysis of sphingolipids in the lysosome by apparently bringing together the substrate and the corresponding hydrolytic enzyme. This implies specific recognition of both the substrate and enzyme by SAP-1.
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