Disease relevance of Arsa

• Thus, arylsulfatase A and not B was associated with the secretory granule released from the rat mast cell by reversed anaphylaxis or the calcium ionophore [1].
• Isolation and comparison of arylsulfatase A from rat liver and Morris hepatoma 7777 [2].
• The 3' end of PCK, arylsulfatase A and H1(0) mRNA exhibited strong binding of cytosolic protein(s) from diverse rat tissues such as heart, liver and lung as well as Fao rat hepatoma cells [3].

High impact information on Arsa

• Activities of lactate dehydrogenase, catalase, cyanide-insensitive palmitoyl-CoA oxidation, and arylsulfatase A in liver were not affected by HCCL treatment [4].
• Release of arylsulfatase A but not B from rat mast cells by noncytolytic secretory stimuli [1].
• It may be that arylsulfatase B resides in a minor second granule, whereas arylsulfatase A is loosely associated with the predominant secretory granule of the rat mast cell [1].
• Isoelectric focusing of the released and residual arylsulfatase activities demonstrated specific release of the A type without B and a net percentage of immunologic release of arylsulfatase A equivalent to that of histamine [1].
• Identification and characterization of arylsulfatase A and B of the rat basophil leukemia tumor [5].

Chemical compound and disease context of Arsa

• Rat liver and Morris hepatoma 7777 arylsulfatase A were isolated from the soluble lysosomal extract by a procedure involving blue-Sepharose affinity chromatography, DEAE-cellulose chromatography, hydrophobic chromatography on phenyl-Sepharose and preparative polyacrylamide gel electrophoresis [2].

Biological context of Arsa

• In clear cells, AS-A reactivity was found throughout the cytoplasmic machineries involved in endocytosis [6].
• Arylsulfatase A is 1 member of a family of sulfatases that is activated by a required co- or posttranslational modification with the oxidation of cysteine to formylglycine [7].
• The comparative studies revealed that the properties of arylsulfatase A from rat liver and Morris hepatoma 7777 are very similar, considering molecular weight of the native monomer and its subunits, the ability to form tetramers, isoelectric point, Michaelis constant and the anomalous kinetics of the reaction [2].
• Although arylsulfatase A alone was incapable of desulfating CS in either purified CS suspensions or the physiological membrane, activator-induced hydrolysis of myelin CS exhibited concentration dependency, pH optimum, and relative insensitivity to salts in a manner similar to purified lipid suspensions [8].

Anatomical context of Arsa

• Total specific activities of cathepsin D and of arylsulfatase A in the sedimentable and nonsedimentable subcellular fractions were at least 38% lower in LIG than in MIG and HIG [9].
• Effect of insulin-like growth factor II on uptake of arylsulfatase A by cultured rat hepatocytes and Kupffer cells [10].
• Background: Arylsulfatase A (ASA) is an enzyme that catalyzes the degradation of sulfatides, a glycosphingolipid found in many tissues, but predominantly in myelin and kidney [7].
• These results favored the adsorption of AS-A from epididymal fluid onto the sperm surface, rather than shunting from the acrosome as a consequence of capacitation-associated membrane priming [6].
• Rat sperm AS-A: subcellular localization in testis and epididymis and surface distribution in epididymal sperm [6].

Associations of Arsa with chemical compounds

• When the net percentage of histamine and arylsulfatase A release were nearly maximal (88 and 76%) in response to the calcium ionophore A23187, specific release of arylsulfatase B did not occur [1].
• Conclusion: Ethanol caused a tissue-specific decrease in hepatic ASA activity levels, but not hexosaminidase activity levels [7].
• Activator-dependent hydrolysis of myelin cerebroside sulfate by arylsulfatase A [8].
• We have demonstrated an increase in activity of arylsulfatase A and B during galactose induced cataract development in rats [11].
• Thiamine pyrophosphatase and arylsulfatase A (EC 3.1.6.1) activities also increased and stayed at higher levels for the duration of the experiment [12].

Other interactions of Arsa

• A purified myelin preparation containing [35S]-labeled cerebroside sulfate (CS) was biosynthesized in developing rat brain and tested as a model of a physiological substrate for CS hydrolysis by arylsulfatase A. Particular attention was directed to the involvement of the CS sulfatase activator protein in facilitating the catabolic process [8].
• Arylsulfatase A and B activities have been analysed in different areas of the CNS (olfactory bulbs, cerebral hemispheres, cerebellum, medulla oblongata and spinal cord) during methyl mercuric chloride (MMC), N-acetyl-DL-homocysteine thiolactone (NAHT) and glutathione (GSH) treatment [13].

Analytical, diagnostic and therapeutic context of Arsa

• 5. Microheterogeneity of rat liver arylsulfatase A was studied by affinity immunoelectrophoresis with 9 different lectins [14].
• Arylsulfatase A (arylsulfatase sulfohydrolase) EC 3.1.6.1 was purified from rat liver by a procedure consisting of differential centrifugation, Con A-Sepharose and Blue Sepharose chromatography, PBE 94 chromatofocusing, DEAE-cellulose and gel filtration chromatography followed by preparative electrophoresis [14].

References