Sulfates, desulfation

Stowell CL, Barvian KK, Young PC, et al. A role for sulfation desulfation in the uptake of bisphenol A into breast tumor cells. Chem Biol 2006 13(8) 891-7. 

Bollet et al. [11] demonstrated the presence of hyaluronidase activity in various mammalian tissues. They showed that this type of hyaluronidase differed from the testicular type concerning pH optimum and pH range of activity. Subsequent studies revealed that the enzyme was present in the lysosomal fraction of the tissues [12]. The liver is an especially rich source [13]. Degradation of hyaluronan leads to the same end products as testicular hyaluronidase [11]. Lysosomal hyaluronidase from rat liver degrades chondroitin-4- and -6-sulfate, but not dermatan sulfate, desulfated dermatan sulfate, heparan sulfate, keratan sulfate, or heparin [14], Lysosomal hyaluronidase has an acid pH optimum and a narrow pH range of activity [14]. This difference in pH profile of activity has commonly been used to differentiate between testicular and lysosomal hyaluronidase. A similar acid-active hyaluronidase is present in human serum [15]. 

DeSULF ALES-301] DeSULF ALES-302] DeSULF ALES-303. See Ammonium laureth sulfate DeSULF ALS-30] DeSULF ALS-30HV] DeSULF ALS-30LC. See Ammonium lauryl sulfate DeSULF DBS-40S. See Sodium dodecylbenzenesulfonate DeSULF DBS-60T. SeeTEA-dodecylbenzenesulfonate DeSULF GOS-P-60WCG. See Lauryl glucoside DeSULF GOS-P-70. See Caprylyl/capryl... 

DeSULF SLES-301] DeSULF SLES-302] DeSULF SLES-303. See Sodium laureth sulfate DeSULF SLS-30LC] DeSULF SLS-30LS. See Sodium lauryl sulfate... 

Residues of non-N-substituted 2-amino-2-deoxy-D-glucose constitute only a tiny fraction (if any) of the total amino sugar of heparin and heparan sulfate. Although free amino groups are produced in the biosynthesis20,23 of heparin (between stages 1 and 2, see Scheme 1), the small proportions occasionally found in heparin and heparan sulfate preparations are most probably the result of some N-desulfation during extraction, or purification, or both. 

Acid cleavage of reduced oxyheparins occurs at pH 1-3 during155 15 min at 100°, or151 with 5 mMH2S04 during 3 h at 60°. Some desulfation of fragments was reported for Smith-degraded heparan sulfate.151 Also, elimination at pH 12 for 30 min at 20° may cause some loss of sulfate.151... 

Dermatan sulfate, also termed chondroitin sulfate B, a related glycosaminoglycan constituent of connective tissue, was known to be composed of galactosamine and a uronic acid, originally believed to be glucuronic acid but then claimed to be iduronic acid based largely on color reactions and paper chromatography. However, the d or L-enantiomer status of the latter monosaccharide was not clear. Jeanloz and Stoffyn unequivocally characterized the monosaccharide as L-iduronic acid by consecutive desulfation, reduction, and hydrolysis of the polysaccharide, followed by isolation of the crystalline 2,3,4-tri-0-acetyl-l,6-anhydro-/ -L-idopyranose, which was shown to be identical to an authentic specimen synthesized from 1,2-0-isopropylidene-/ -L-idofuranose.34... 

The biologically inactive estrone sulfate (EIS) and dehydro-epiandrosterone-sulfate (DHEAS) are the most abundant circulating estrogenic precursors in the plasma of post-menopausal women [103]. Desulfation of inactive steroid-3-0-sulfates by estrone-sulfatase (STS) plays a key role in the regulation of levels of receptor-active estrogenic steroids (estradiol and androstenediol) in breast cancer cells (Fig. 9). There is strong evidence suggesting that estrone sulfatase (STS) and DHEA-sulfatase are the same enzyme [103]. 

For the analytical characterization of sulfated tyrosine peptides, spectroscopic methods as well as amino acid analysis and, more recently, mass spectrometry are employed. In Table 2 the spectroscopic data of tyrosine 0-sulfate are compared to those of the related sulfonic acid derivatives as possible byproducts in the chemical sulfation of the tyrosine or tyrosine peptides.[361 In the course of the synthesis of tyrosine 0-sulfate peptides and, particularly in the final deprotection step, desulfation may occur which limits the characterization of the final compounds in terms of quantitative identification of the tyrosine 0-sulfate. This is achieved by amino acid analyses of basic hydrolysates of the sulfated tyrosine peptides or preferably by analyses of the enzymatic hydrolysates with aminopeptidase M or leucine-aminopeptidase. 

To date, the O-sulfation of hydroxyamino acids as residues in proteins or as free amino acids has not been detected. Similarly, desulfation by sulfatases has been observed only for sulfated serine, but it could not be attributed unambiguously to a sulfatase.11301 This lack of natural occurrence explains why only marginal attention has been paid to the synthesis of sulfated hydroxyamino acid peptides. 

In 1921 Helferich [34J found that treatment of methyl a-D-glucopyranoside 18 with sulfuryl chloride in a mixture of pyridine and chloroform at 5°C afforded a compound, the structure of which was established several years later [37,38] to be that of methyl 4,6-dichloro-4,6-dideoxy-a-D-galactopyranoside 2,3-cyclic sulfate (19 Scheme 3). The cyclic sulfates are readily cleaved by dilute alkalis, or by methanolic ammonia, to give the salt of a monosulfate the hemi-ester is then desulfated by acid to yield the chlorodeoxy sugar [35,36]. Both of these reactions occur with retention of configuration [37]. 

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