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PubMed2001

Isolation and structural determination of novel sulfated hexasaccharides from squid cartilage chondroitin sulfate E that exhibits neuroregulatory activities.

Squid cartilage chondroitin sulfate E (CS-E) exhibits various biological activities, including anticoagulant activities, lymphoid regulatory activities, and neuroregulatory activities [Ueoka, C., Kaneda, N., Okazaki, I., Nadanaka, S., Muramatsu, T., and Sugahara, K. (2000) J. Biol. Chem. 275, 37407-37413]. These activities are expressed through molecular interactions with specific proteins, including heparin cofactor II, selectins, CD44, chemokines, and the heparin-binding growth factor midkine. Hence, the sugar sequence information is essential for a better understanding of the CS-E functions. Previously, several novel tetrasaccharides containing the unreported 3-O-sulfated glucuronic acid (GlcA) were isolated after digestion of squid cartilage CS-E with testicular hyaluronidase. In this study, hexasaccharides were isolated to obtain more detailed sequence information, especially around the GlcA(3-O-sulfate) residue, and were characterized by fast atom bombardment mass spectrometry and 500 or 600 MHz (1)H NMR spectroscopy. The findings demonstrate one tetrasulfated and five pentasulfated hexasaccharide sequences, five of them being novel. They were composed of three disaccharide building units of either A [GlcA(beta1-3)GalNAc(4-O-sulfate)], E [GlcA(beta1-3)GalNAc(4,6-O-disulfate)], K [GlcA(3-O-sulfate)(beta1-3)GalNAc(4-O-sulfate)], L [GlcA(3-O-sulfate)(beta1-3)GalNAc(6-O-sulfate)], or M [GlcA(3-O-sulfate)(beta1-3)GalNAc(4,6-O-disulfate)], forming E-A-A, M-A-A, K-L-A, E-E-A, K-K-A, and A-M-A hexasaccharide sequences. The K-L tetrasaccharide sequence is to date unreported. The isolated sequences appear to indicate the occurrence of an unreported GlcA 3-O-sulfotransferase specific for chondroitin sulfate. The obtained sequence information will be useful for investigating the structure-function relationship and biosynthesis of CS-E.

Animals↗
PubMed1998

Selective reduction of 6-O-sulfation in heparan sulfate from transformed mammary epithelial cells.

Heparan sulfate at cell surfaces and in the extracellular matrix regulates cell proliferation and adhesion by binding to growth factors and matrix proteins via structurally specific oligosaccharide domains. We have used the hormonally regulated mouse mammary carcinoma cell line S115 as a model to elucidate the effect of malignant transformation on the structure of heparan sulfate. When cultured in the presence of testosterone, S115 cells form tumor cell colonies in soft agar and exhibit fibroblast-like morphology; withdrawal of testosterone results in a loss of the tumorigenic capacity and a switch towards epithelial morphology. Metabolically 35SO4-labeled heparan sulfate was isolated from testosterone-treated and non-treated S115 cells and subjected to structural analysis. We found that the testosterone-dependent malignant transformation was associated with reduced sulfation of heparan sulfate due to a approximately 40% decrease in the amount of GlcN6S units. By contrast, no significant differences were observed in the amounts of 2-O-sulfate or N-sulfate groups. The reduced 6-O-sulfation of GlcN units in heparan sulfate from transformed S115 cells led to a marked decrease in the amount of trisulfated IdoA2S-GlcNS6S units (IdoA, L-iduronic acid), implicated in many heparan sulfate-protein interactions.

Animals↗
PubMed2003

Identification of a third sulfate activation system in Sinorhizobium sp. strain BR816: the CysDN sulfate activation complex.

Sinorhizobium sp. strain BR816 possesses two nodPQ copies, providing activated sulfate (3'-phosphoadenosine-5'-phosphosulfate [PAPS]) needed for the biosynthesis of sulfated Nod factors. It was previously shown that the Nod factors synthesized by a nodPQ double mutant are not structurally different from those of the wild-type strain. In this study, we describe the characterization of a third sulfate activation locus. Two open reading frames were fully characterized and displayed the highest similarity with the Sinorhizobium meliloti housekeeping ATP sulfurylase subunits, encoded by the cysDN genes. The growth characteristics as well as the levels of Nod factor sulfation of a cysD mutant (FAJ1600) and a nodP1 nodQ2 cysD triple mutant (FAJ1604) were determined. FAJ1600 shows a prolonged lag phase only with inorganic sulfate as the sole sulfur source, compared to the wild-type parent. On the other hand, FAJ1604 requires cysteine for growth and produces sulfate-free Nod factors. Apigenin-induced nod gene expression for Nod factor synthesis does not influence the growth characteristics of any of the strains studied in the presence of different sulfur sources. In this way, it could be demonstrated that the "household" CysDN sulfate activation complex of Sinorhizobium sp. strain BR816 can additionally ensure Nod factor sulfation, whereas the symbiotic PAPS pool, generated by the nodPQ sulfate activation loci, can be engaged for sulfation of amino acids. Finally, our results show that rhizobial growth defects are likely the reason for a decreased nitrogen fixation capacity of bean plants inoculated with cysD mutant strains, which can be restored by adding methionine to the plant nutrient solution.

Bacterial Proteins↗
PubMed1992

Effect of complete sulfation of bile acids on bile formation: role of conjugation and number of sulfate groups.

The effect of complete sulfation of conjugated cholic, chenodeoxycholic and deoxycholic acids on bile formation was investigated in rats. The sulfated bile acids were infused intravenously in stepwise increasing doses (1, 2, 3 and 4 mumol/min/100 gm body wt) in rats after 90 min of bile acid pool depletion. The effects of these bile acids on bile flow, bile salt, biliary phospholipid and cholesterol secretion rates were determined. In addition, their choleretic activity and their effect on biliary lipid secretion were calculated. Appropriate controls infused with nonsulfated bile were also performed. The sulfated bile acids increased bile flow with increasing the infusion doses, and the maximum bile flow was significantly higher than nonsulfated bile acids. Although cholestasis was developed during the infusion of nonsulfated bile acids, no cholestatic effect was observed for sulfated bile acids. With the exception of cholic acid, sulfation significantly increased the bile acid secretory rate maximum. The sulfates of chenodeoxycholic and deoxycholic acids were further hydroxylated. The choleretic activities for all the sulfated bile acids were significantly higher than the nonsulfated bile acids. All the sulfated bile acids significantly reduced the biliary lipid secretion, and a significant correlation was found between the choleretic activity and the phospholipid-dependent bile acid secretion. The data also showed that infusion of sulfated taurine-conjugated bile acids produced higher bile flow and bile acid secretion rate and was less effective when biliary lipid secretion rates were reduced compared with glycine conjugates. It is concluded that sulfated conjugated bile acids may have a role in protection during cholestasis either by stimulation of bile flow or by reduction of biliary lipid secretion, thus protecting cell membranes from the detergent properties of high concentrations of nonsulfated bile acids.

Animals↗
PubMed1984

Sulfation in isolated enterocytes of guinea pig: dependence on inorganic sulfate.

Isolated intestinal epithelial cells of the guinea-pig were used to study uptake and metabolism of inorganic sulfate in the jejunum (proximal cells) and ileum (distal cells). Proximal enterocytes accumulated sulfate 1.5-fold and distal enterocytes 3.1-fold. Accumulation was almost linearly related to substrate concentrations up to 5 mM. In proximal cells, despite their lower intracellular sulfate levels, sulfate incorporation into acid-precipitable material and sulfate conjugation of 1-naphthol were faster than in distal cells. Formation of 1-naphthyl sulfate increased with extracellular sulfate concentrations up to 1 and 3 mM sulfate in distal and proximal enterocytes, respectively. The data suggest that the extent of intestinal sulfation of phenolic compounds may be enhanced by oral administration of sulfate.

Animals↗
PubMed1998

Regioselective syntheses of sulfated polysaccharides: specific anti-HIV-1 activity of novel chitin sulfates.

A novel and convenient method for the regioselective syntheses of sulfated analogs of chitin and chitosan is described in relation to studies on structure-biological activity. Fully protected, soluble derivatives of chitosan were found to be useful intermediates for the syntheses of a novel class of sulfated polysaccharides, 2-acetamido-2-deoxy-3-O-sulfo-(1-->4)-beta-D-glucopyranan (3-sulfate, 3S, 4) and (1-->4)-2-deoxy-2-sulfoamido-3-O-sulfo-(1-->4)-beta-D-glucopyranan (2,3-disulfate, 23-S, 3). These compounds were tested for their activities in (i) inhibiting HIV-1 replication in vitro and (ii) inhibiting blood coagulation. The results reveal that the selective sulfation at O-2 and/or O-3 affords potent antiretroviral agents showing a much higher inhibitory effect on the infection of AIDS virus in vitro than that by the known 6-O-sulfated derivative (6-sulfate, 6S). Moreover, the 23-S product completely inhibited the infection of AIDS virus to T lymphocytes at concentrations as low as 0.28 microgram/mL without significant cytotoxicity. The regioselective introduction of sulfate group(s) at O-2 and/or O-3 had little effect on generating anticoagulant activity, whereas 6-O-sulfated chitin strongly inhibits blood coagulation. These results suggest that the specific interaction of these new types of chitin sulfates with gp 120 of the AIDS virus depends significantly on the sites of sulfation rather than on the total degree of substitution on sugar residues.

Animals↗
PubMed1982

Proton-sulfate co-transport: mechanism of H+ and sulfate addition to the chloride transporter of human red blood cells.

Proton and sulfate inhibition of the obligatory chloride-chloride exchange of human erythrocytes was measured at 0 degrees C to determine their mechanism of reaction with the anion transporter. The proton and sulfate that are co-transported by this mechanism at higher temperatures behaved as nontransported inhibitors at 0 degrees C. We analyzed the data in terms of four molecular mechanisms: (1) HSO4- addition to the transporter; (2) ordered addition with the proton first; (3) ordered addition with the sulfate first; (4) random addition to the transporter. The Dixon plots of 1/MCl vs. [SO4] at different proton concentrations were not parallel. Thus protons and sulfate ions were not mutually exclusive inhibitors. The slope of these Dixon plots was independent of pH above 7.0, which indicates that sulfate could bind to the unprotonated carrier and excludes the first two mechanisms. Protons were inhibitors of chloride flux in the absence of sulfate, which indicates that protons could bind to the unloaded carrier and excludes mechanism 3. The KI for sulfate was 4.35 +/0 0.36 mM. The pK for the protonatable group was 5.03 +/- 0.02. The binding of either a proton or sulfate to the carrier decreased the KI of the other by ninefold. The only simple mechanism consistent with the data is a random-ordered mechanism with more transporters loaded with a sulfate than loaded with a proton at the pH and sulfate concentrations of plasma.

Biological Transport, Active↗
PubMed2005

Factor H is a dermatan sulfate-binding protein: identification of a dermatan sulfate-mediated protease that cleaves factor H.

Dermatan sulfate mediates the blood coagulation cascade by binding to heparin cofactor II and potentiating the antithrombin activity. In order to explore another function of dermatan sulfate, a dermatan sulfate affinity column was prepared from biotinylated dermatan sulfate and Streptavidin Sepharose. When human plasma was applied on the dermatan sulfate column, factor H was bound and cleaved. The cleavage products, a 30-kDa N-terminal fragment and a 120-kDa fragment, were eluted from the column with 500 mM NaCl and detected after Western blotting with anti-factor H. The bond between the tandem arginine residues in the sixth domain of factor H was cleaved. When purified factor H was applied on the column, the factor H was not cleaved and was recovered from the column as an intact 150-kDa fraction. The finding that dermatan sulfate-mediated cleavage of factor H was inhibited by (p-amidinophenyl) methanesulfonyl fluoride, but not N-ethylmaleimide or EDTA, indicates that a serine protease in the plasma was activated on the dermatan sulfate column and factor H was cleaved without intervention of the plasma protease inhibitors. Amidase activity was detected in the effluent from the dermatan sulfate column but was abolished by pretreatment of the plasma with dermatan sulfate. Therefore, dermatan sulfate participates in the activation of a protease as well as having the protease inhibitory action.

Amidohydrolases↗
PubMed2004

Root-to-shoot transport of sulfate in Arabidopsis. Evidence for the role of SULTR3;5 as a component of low-affinity sulfate transport system in the root vasculature.

Xylem transport of sulfate regulates distribution of sulfur in vascular plants. Here, we describe SULTR3;5 as an essential component of the sulfate transport system that facilitates the root-to-shoot transport of sulfate in the vasculature. In Arabidopsis (Arabidopsis thaliana), SULTR3;5 was colocalized with the SULTR2;1 low-affinity sulfate transporter in xylem parenchyma and pericycle cells in roots. In a yeast (Saccharomyces cerevisiae) expression system, sulfate uptake was hardly detectable with SULTR3;5 expression alone; however, cells coexpressing both SULTR3;5 and SULTR2;1 showed substantial uptake activity that was considerably higher than with SULTR2;1 expression alone. The V(max) value of sulfate uptake activity with SULTR3;5-SULTR2;1 coexpression was approximately 3 times higher than with SULTR2;1 alone. In Arabidopsis, the root-to-shoot transport of sulfate was restricted in the sultr3;5 mutants, under conditions of high SULTR2;1 expression in the roots after sulfur limitation. These results suggested that SULTR3;5 is constitutively expressed in the root vasculature, but its function to reinforce the capacity of the SULTR2;1 low-affinity transporter is only essential when SULTR2;1 mRNA is induced by sulfur limitation. Consequently, coexpression of SULTR3;5 and SULTR2;1 provides maximum capacity of sulfate transport activity, which facilitates retrieval of apoplastic sulfate to the xylem parenchyma cells in the vasculature of Arabidopsis roots and may contribute to the root-to-shoot transport of sulfate.

Anion Transport Proteins↗
PubMed1991

Structural studies on sulfated oligosaccharides derived from the carbohydrate-protein linkage region of chondroitin sulfate proteoglycans of whale cartilage.

From the carbohydrate-protein linkage region of whale cartilage proteoglycans, which bear predominantly chondroitin 4-sulfate, one nonsulfated, two monosulfated and one disulfated hexasaccharide alditols were isolated after exhaustive digestions with Actinase E and chondroitinase ABC, and subsequent beta-elimination. Their structures were analyzed by chondroitinase ACII digestion in conjunction with HPLC and by 500-MHz 1H-NMR spectroscopy. The nonsulfated compound (A) had the following conventional structure: delta GlcA(beta 1-3)-GalNAc(beta 1-4)GlcA(beta 1-3)Gal(beta 1-4)Xylol, where GlcA, delta GlcA and GalNAc are glucuronic acid; 4,5-unsaturated glucuronic acid and 2-deoxy-2-N-acetylamino-D-galactose, respectively. The other compounds were sulfated derivatives of compound A. Two monosulfated compounds (B and C) had an ester sulfate on C4 or C6 of the GalNAc residue, respectively and the disulfated compound (D) had two ester sulfate groups, namely, one on C4 of the GalNAc and the other on C4 of the Gal residue substituted by GlcA. The molar ratio of A/B/C/D was 0.21:0.16:0.36:0.27. The compound containing Gal-4-O-sulfate was previously isolated by us in the form of a sulfated glycoserine [delta GlcA(beta 1-3)GalNAc(4-O- sulfate)(beta 1-4)GlcA(beta 1-3)Gal(4-O-sulfate)(beta 1-3)-Gal(beta 1- 4)Xyl beta 1-O-Ser] from the carbohydrate-protein linkage region of rat chondrosarcoma chondroitin-4-sulfate proteoglycans [Sugahara K., Yamashina, I., DeWaard, P., Van Halbeek, H. & Vliegenthart, J.F.G. (1988) J. Biol. Chem. 263, 10,168-10,174]. The discovery of this structure in the carbohydrate-protein linkage region of chondroitin 4-sulfate proteoglycans from nontumorous cartilage indicates that it is not a tumor-associated product but rather a physiological biosynthetic product since it represents a significant proportion. The biological significance of this structure is discussed in relation to glycosaminoglycan biosynthesis.

Animals↗
PubMed1996

Specificity studies of bacterial sulfatases by means of structurally defined sulfated oligosaccharides isolated from shark cartilage chondroitin sulfate D.

Chondro-4-sulfatase and chondro-6-sulfatase from Proteus vulgaris and delta-hexuronate-2-sulfatase from Flavobacterium heparinum are potentially useful tools for structural studies of chondroitin sulfate and dermatan sulfate. Their substrate specificities were investigated with various structurally defined, sulfated hexasaccharides isolated from chondroitin sulfate as described in the accompanying report [Sugahara, K., Nadanaka, S., Takeda, K. & Kojima, T. (1996) Eur. J. Biochem. 239, 871-880]. The results indicated that delta-hexuronate-2-sulfatase released an ester sulfate from the C2 position of the delta-hexuronate residue located at the non-reducing terminus, while chondro-6-sulfatase removed an ester sulfate from the C6 position of the GalNAc residue at the reducing end of the hexasaccharides. Chondro-4-sulfatase acted preferentially on an ester sulfate on the C4 position of the GalNAc residue at the reducing end under mild incubation conditions, but also released a sulfate group under harsh conditions from the C4 position of the GalNAc residue at the internal positions of the hexasaccharide chains, unless the GalNAc residue had another ester sulfate on its C6 position. The results demonstrated the usefulness of the sulfatases as tools for the structural characterization of chondroitin sulfate oligosaccharides.

Animals↗
PubMed2006

Methane and sulfate profiles within the subsurface of a tidal flat are reflected by the distribution of sulfate-reducing bacteria and methanogenic archaea.

The anoxic layers of marine sediments are dominated by sulfate reduction and methanogenesis as the main terminal oxidation processes. The aim of this study was to analyze the vertical succession of microbial populations involved in these processes along the first 4.5 m of a tidal-flat sediment. Therefore, a quantitative PCR approach was applied using primers targeting the domains of Bacteria and Archaea, and key functional genes for sulfate reduction (dsrA) and methanogenesis (mcrA). The sampling site was characterized by an unusual sulfate peak at 250 cm depth resulting in separate sulfate-methane transition zones. Methane and sulfate profiles were diametrically opposed, with a methane maximum in the sulfate-depleted zone showing high numbers of archaea and methanogens. The methane-sulfate interfaces harbored elevated numbers of sulfate reducers, and revealed a slight increase in mcrA and archaeal 16S rRNA genes, suggesting sulfate-dependent anaerobic oxidation of methane. A diversity analysis of both functional genes by PCR-denaturing gradient gel electrophoresis revealed a vertical succession of subpopulations that were governed by geochemical and sedimentologic conditions. Along the upper 200 cm, sulfate-reducing populations appeared quite uniform and were dominated by the Deltaproteobacteria. In the layers beneath, an apparent increase in diversity and a shift to the Firmicutes as the predominant group was observed.

Anaerobiosis↗
PubMed1985

Decreases in ovine fetal cartilage sulfate uptake and serum sulfate during gestation.

In vitro assays for [35S]sulfate uptake by ovine fetal costal cartilage were used to assess gestational changes in cartilage metabolism. Addition of 20% normal human serum to the incubation medium increased fetal cartilage [35S]sulfate incorporation into glycosaminoglycans. Both basal and human serum-stimulated uptakes of [35S]sulfate by fetal sheep cartilage decreased from midgestation to full term. The incremental response in [35S]sulfate uptake that was stimulated by human serum decreased as gestation proceeded to full-term. Fetal serum sulfate concentration decreased logarithmically during gestation, raising the possibility that cartilage sulfate uptake might become substrate limited as full term is approached. Perfusion of seven late gestation sheep fetuses for 7 days with Na2SO4 to achieve serum sulfate concentrations similar to those observed earlier in gestation resulted in a 33% increase in mean cartilage [35S]sulfate uptake compared with that of control twin fetuses, but uptake was not increased to values that occurred spontaneously earlier in gestation. These results suggest that the decreasing rate of [35S]sulfate uptake by fetal cartilage during the last half of gestation is associated only minimally with decreasing serum sulfate levels and is most consistent with intrinsic change in resting chondrocyte metabolism during gestation.

Animals↗
PubMed1987

[Composition and degree of sulfation of glycosaminoglycans from tissues of different animal species: heterogeneity and tissue specificity of heparan sulfates].

The composition and degree of sulfation of glycosaminoglycans (GAG) in proteoglycans from various animal tissues were studied. It was shown that sulfated GAG contain chondroitin sulfates AC and B as well as heparan sulfates. The bulk of GAG in the majority of tissues under study is represented by 2-3 types of heparan sulfate molecules differing in the degree of sulfation. According to the degree of sulfation heparan sulfates from all tissues studied can be classified into three groups. Homologous tissues of various animal species are characterized by a similar composition and the degree of sulfation The data obtained are discussed in terms of the feasible role of proteoheparan sulfates in specific cell-to-cell interactions.

Animals↗
PubMed1978

Copolymers of chondroitin 4-sulfate and chondroitin 6-sulfate in chick embryo epiphyses and other cartilage.

Tetrasaccharides were prepared from chondroitin sulfate by means of a limited degradation with chondroitinase ABC. Tetrasaccharides containing one sulfate per disaccharide unit were isolated and were found to be of three types: a tetrasaccharide with two 6-sulfated disaccharide units, a tetrasaccharide with two 4-sulfated disaccharide units, and a tetrasaccharide with one 4-sulfated disaccharide unit and one 6-sulfated disaccharide unit. Samples of each of these three types of tetrasaccharides were obtained from chick embryo epiphyseal cartilage and from a mixture of bovine tracheal cartilage and shark cartilage. The presence of both a 4-sulfated disaccharide unit and a 6-sulfated disaccharide unit in the same tetrasaccharide molecule indicates the existence of mixed 4 and 6 sulfation on the same chondroitin sulfate chain.

Animals↗
PubMed1992

One- and two-dimensional 1H-NMR characterization of two series of sulfated disaccharides prepared from chondroitin sulfate and heparan sulfate/heparin by bacterial eliminase digestion.

The 1H-NMR spectra of eight unsaturated disaccharides obtained by bacterial eliminase digestion of chondroitin sulfate and of heparan sulfate/heparin were recorded in order to construct an NMR data base of sulfated oligosaccharides and to investigate the effects of sulfation on the proton chemical shifts. These shifts were assigned by two-dimensional HOHAHA (homonuclear Hartmann-Hahn) and COSY (correlation spectroscopy) methods. The results indicated the following. (1) Two sets of proton signals were observed, corresponding to the alpha and beta anomers of these disaccharides, except those containing N-sulfated GlcN (2-deoxy-2-amino-D-glucose), in which only one set of signals appeared, corresponding to the alpha anomer. (2) Signals of protons bound to an O-sulfated carbon atom and those bound to the immediately neighboring carbon atoms were shifted downfield by 0.4-0.7 and 0.07-0.3 ppm, respectively. (3) For the disaccharides containing the N-sulfated GlcN, the signals of the protons bound to C-2 and C-3 were shifted upfield by 0.6 and 0.15 ppm, respectively, but that of C-1 was shifted downfield by 0.25 ppm when compared with those of the corresponding N-acetylated disaccharides. (4) For the chondroitin sulfate disaccharides sulfated on the C-4 position of GalNAc (2-deoxy-2-N-acetylamino-D-galactose) or the C-2 position of delta GlcA (D-gluco-4-ene-pyranosyluronic acid), the signal of the H-3 proton of delta GlcA or the H-4 proton of GalNAc was shifted upfield by 0.1-0.15 ppm, indicating the steric interaction of the two sugar components. (5) These effects of sulfation on chemical shifts are additive.

Animals↗
PubMed1979

Solution properties of sulfated monohydroxy bile salts. Relative insolubility of the disodium salt of glycolithocholate sulfate.

Physical-chemical properties of the major sulfated monohydroxy bile salts of man are described. In general, the sulfates are significantly more water-soluble than the non-sulfated species as a result of lower critical micellar temperatures, high aqueous monomeric solubilities and critical micellar concentrations. Nevertheless, at 37 degrees C the disodium salt of glycolithocholate sulfate, the major monohydroxy bile salt of man is not more soluble than its non-sulfated form. Since aqueous solubility correlates inversely with the cholestatic potential of bile salts, our results suggest that this sulfate may be potentially hepatoxic. Micellar solubility of phosphatidylcholine and cholesterol by the majority of non-sulfated and sulfated monohydroxy bile salts is slight. Nonetheless, phosphatidylcholine is very well solubilized by taurolithocholate sulfate but cholesterol solubility is not increased appreciably. Cholesterol saturation in model bile systems of taurochenodeoxycholate and phosphatidylcholine is impaired by the addition of sulfated lithocholate conjugates but with physiological bile salt compositions this reduction is not significant.

Bile Acids and Salts↗
PubMed1994

Tyrosine sulfation of the glycoprotein Ib-IX complex: identification of sulfated residues and effect on ligand binding.

Here, we present evidence that glycoprotein (GP) Ib alpha, one of three polypeptides that make up the GP Ib--IX complex--the receptor for von Willebrand factor (vWf) on the surface of unactivated platelets--is modified by sulfation of tyrosine residues. Only GP Ib alpha was found to incorporate 35S when the GP Ib--IX complex was immunoprecipitated from [35S]sulfate metabolically labeled L and CHO cells that express the recombinant complex. The occurrence of sulfation on tyrosine residues of the polypeptide backbone was determined by removing O- and N-linked oligosaccharides. Limited proteolytic digestion of metabolically labeled GP Ib alpha revealed that sulfated tyrosine residues are located in the 45-kDa globular region containing the vWf binding site. By mutating potentially sulfated tyrosine residues to phenylalanine and comparing the stoichiometry of sulfate incorporation of these mutants to the incorporation in wild-type GP Ib alpha, three clustered tyrosine residues--Tyr-276, Tyr-278, and Tyr-279-were identified that undergo the modification. Culturing cells in sulfate-depleted medium containing sodium chlorate and guaiacol completely inhibited GP Ib alpha sulfation but did not decrease GP Ib-IX expression on the cell surface. Similarly, transiently transfected CHO cells expressed the mutant GP Ib alpha polypeptide on their surfaces at the same levels as they expressed wild-type GP Ib alpha. These results suggest that tyrosine sulfation of GP Ib alpha has little or no effect on the synthesis, assembly, and surface expression of the GP Ib-IX complex. Nevertheless, inhibiting sulfation of GP Ib alpha reduced the binding of 125I-labeled vWf in the presence of ristocetin by up to 37%.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗