Results 231 to 240 of about 2,765,821 (261)
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Journal of Neurochemistry, 2007
AbstractWe have generated specific saposin A and D deficient mouse mutants by the gene targeting technology. Saposin A deficient mice showed the clinical, biochemical and pathological phenotype of a chronic form of globoid cell leukodystrophy (Krabbe disease) establishing that saposin A is essential for in vivo degradation of galactosylceramide ...
Junko, Matsuda +2 more
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AbstractWe have generated specific saposin A and D deficient mouse mutants by the gene targeting technology. Saposin A deficient mice showed the clinical, biochemical and pathological phenotype of a chronic form of globoid cell leukodystrophy (Krabbe disease) establishing that saposin A is essential for in vivo degradation of galactosylceramide ...
Junko, Matsuda +2 more
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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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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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[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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[Lysosomal enzymes, sphingolipid activator proteins, and protective protein].
Nihon rinsho. Japanese journal of clinical medicine, 1996The lysosome is an intracytoplasmic acidic vacuole containing more than 60 hydrolytic enzymes for digestion of macromolecules, such as nucleic acids, proteins, lipids and complex carbohydrates. Expression of lysosomal enzyme activities is regulated by various intracellular environmental factors.
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Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus.
Science, 1988J. S. O'Brien +5 more
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