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<title>Enzyme assay of sulfotransferases for keratan sulfate - Glycoscience Protocols (GlycoPODv2) - NCBI Bookshelf</title>
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<div class="pre-content"><div><div class="bk_prnt"><p class="small">NCBI Bookshelf. A service of the National Library of Medicine, National Institutes of Health.</p><p>Nishihara S, Angata K, Aoki-Kinoshita KF, et al., editors. Glycoscience Protocols (GlycoPODv2) [Internet]. Saitama (JP): Japan Consortium for Glycobiology and Glycotechnology; 2021-. </p></div></div></div>
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<div class="main-content lit-style" itemscope="itemscope" itemtype="http://schema.org/CreativeWork"><div class="meta-content fm-sec"><h1 id="_NBK593949_"><span class="title" itemprop="name">Enzyme assay of sulfotransferases for keratan sulfate</span></h1><div class="contrib half_rhythm"><span itemprop="author">Akira Seko</span>, Ph.D.<div class="affiliation small">Japan Agency for Medical Research and Development (AMED)<div><span class="email-label">Email: </span><a href="mailto:dev@null" data-email="pj.og.dema@okes-arikA" class="oemail">pj.og.dema@okes-arikA</a></div></div><div class="small">Corresponding author.</div></div><p class="small">Created: <span itemprop="datePublished">September 7, 2021</span>; Last Revision: <span itemprop="dateModified">March 23, 2022</span>.</p></div><div class="body-content whole_rhythm" itemprop="text"><div id="g85-assaystks.Introduction"><h2 id="_g85-assaystks_Introduction_">Introduction</h2><p>Keratan sulfate is a major glycosaminoglycan and comprises poly-<i>N</i>-acetyllactosamine backbone structure [(Galβ1-4GlcNAcβ1-3)<sub>n</sub>] with modification of sulfates at the 6-OH of Gal and GlcNAc residues. Based on the substrate specificities of glycosyl/sulfotransferases involved in keratan sulfate biosynthesis, keratan sulfate can be elongated as follows (<a class="figpopup" href="/books/NBK593949/figure/g85-assaystks.F1/?report=objectonly" target="object" rid-figpopup="figg85assaystksF1" rid-ob="figobg85assaystksF1">Figure 1</a>):</p><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">Nonreducing terminal GlcNAc residues on specific branches of <i>N</i>-linked/<i>O</i>-linked glycan chains are 6-<i>O</i>-sulfated by CHST2 (also known as GlcNAc 6-<i>O</i>-sulfotransferase-1 and GlcNAc6ST1), CHST5 (GlcNAc 6-<i>O</i>-sulfotransferase-3, GlcNAc6ST3, I-GlcNAc6ST, and GST4α), or CHST6 (GlcNAc 6-<i>O</i>-sulfotransferase-5, GlcNAc6ST5, CGn6ST, and GST4β) (<i>see</i>
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<b>Notes 1</b> and <b>2</b>).</p></dd><dt>2.</dt><dd><p class="no_top_margin">GlcNAc 6-<i>O</i>-sulfate residues are next galactosylated by B4GALT4 (also known as β4GalT-IV), which is only the β4GalT specific for GlcNAc 6-<i>O</i>-sulfate.</p></dd><dt>3.</dt><dd><p class="no_top_margin">6-<i>O</i>-Sulfated LacNAc, Galβ1-4(SO<sub>3</sub><sup>−</sup>-6)GlcNAc, is elongated by B3GNT7 (β3Gn-T7), which is specific for the sulfated moiety.</p></dd><dt>4.</dt><dd><p class="no_top_margin">Repeating 1, 2, and 3 results in the formation of [Galβ1-4(SO<sub>3</sub><sup>−</sup>-6)GlcNAcβ1-3]<sub>n</sub>.</p></dd><dt>5.</dt><dd><p class="no_top_margin">CHST1 (also known as Gal6ST, KSGal6ST, and GST-1) catalyzes 6-<i>O</i>-sulfation of both the nonreducing terminal and internal Gal residues.</p></dd></dl><p>As described above, at least four sulfotransferases, CHST1, 2, 5, and 6, are involved in the biosynthesis of keratan sulfate. The enzymatic activities of these enzymes can be measured using a donor substrate, adenosine 3’-phosphate 5’-phospho[<sup>35</sup>S]sulfate ([<sup>35</sup>S]PAPS) and acceptor substrates bearing appropriate nonreducing terminal sugar residues.</p><p>The first step, GlcNAc 6-<i>O</i>-sulfation, can be catalyzed using CHST2, 5, or 6. So far, CHST2, 5, and 6 mainly work on GlcNAc 6-<i>O</i>-sulfation in the developmental stage of the brain in mice, in the adult brain in mice, and in the cornea in mice and humans, respectively (<b>Note 2</b>). The difference in the substrate specificities for glycan or protein moieties in each organ is not fully understood.</p></div><div id="g85-assaystks.Protocol"><h2 id="_g85-assaystks_Protocol_">Protocol</h2><p>In this chapter, the methods for assaying CHST6 and CHST1 activities and preparing the acceptor substrate for CHST6 are shown (<a class="bk_pop" href="#g85-assaystks.REF.1">1</a>-<a class="bk_pop" href="#g85-assaystks.REF.3">3</a>).</p><div id="g85-assaystks.Materials"><h3>Materials</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">Adenosine 3’-phosphate 5’-phospho[<sup>35</sup>S]sulfate (PerkinElmer, Waltham, MA)</p></dd><dt>2.</dt><dd><p class="no_top_margin">Keratan sulfate (from bovine cornea, Seikagaku Corp., Tokyo, Japan)</p></dd><dt>3.</dt><dd><p class="no_top_margin">UDP-GlcNAc and GlcNAc (Sigma-Aldrich Co., St. Louis, MO)</p></dd><dt>4.</dt><dd><p class="no_top_margin">L2L2 [Galβ1-4(SO<sub>3</sub><sup>−</sup>-6)GlcNAcβ1-3Galβ1-4(SO<sub>3</sub><sup>−</sup>-6)GlcNAc] (prepared from bovine articular cartilage KS according to Ref. <a class="bk_pop" href="#g85-assaystks.REF.4">4</a>)</p></dd><dt>5.</dt><dd><p class="no_top_margin">RCA-I agarose (4 mg/mL of gel, J-OIL MILLS, Inc., Tokyo, Japan)</p></dd><dt>6.</dt><dd><p class="no_top_margin">Recombinant B3GNT7 (prepared according to Ref. <a class="bk_pop" href="#g85-assaystks.REF.5">5</a>) (<b>Note 3</b>)</p></dd></dl></div><div id="g85-assaystks.Instruments"><h3>Instruments</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">High-voltage paper electrophoresis unit (Advantec, Co., Ltd., Ehime, Japan) (<b>Note 4</b>)</p></dd><dt>2.</dt><dd><p class="no_top_margin">Radiochromatogram scanner (RITA, Raytest, Straubenhardt, Germany)</p></dd><dt>3.</dt><dd><p class="no_top_margin">Whatman No.1 paper (Cytiva, Boston, MA)</p></dd><dt>4.</dt><dd><p class="no_top_margin">Vacuum evaporator (Sakuma Co. Ltd., Tokyo, Japan)</p></dd><dt>5.</dt><dd><p class="no_top_margin">Sephadex G-25 and Sephadex G-50 (superfine, Cytiva, Boston, MA)</p></dd></dl></div><div id="g85-assaystks.Methods"><h3>Methods</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">Preparation of an intermediate analog of keratan sulfate, GlcNAcβ1-3Galβ1-4(SO<sub>3</sub><sup>-</sup>-6)GlcNAcβ1-3Galβ1-4(SO<sub>3</sub><sup>−</sup>-6)GlcNAc (GlcNAcβ1-3L2L2)</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">0.1 mL of the reaction mixture containing 50 mM of HEPES-NaOH (pH 7.2), 10 mM of MnCl<sub>2</sub>, 0.05%(v/v) Triton X-100, 50 μg/mL of protamine chloride, 1 mM of L2L2, 0.1 M GlcNAc, 1.25 mM of UDP-GlcNAc, and recombinant B3GNT7 (5 nmol/h. The activity is assayed using 0.5 mM of L2L2 and 0.5 mM of UDP-GlcNAc), is incubated at 37°C for 1 d.</p></dd><dt>b.</dt><dd><p class="no_top_margin">The mixture is applied to a Sephadex G-50 gel filtration (1.3 × 68 cm, equilibrated and eluted with 0.1 M NaCl).</p></dd><dt>c.</dt><dd><p class="no_top_margin">The hexose-positive fractions (phenol-sulfuric acid method) are applied to RCA-I-agarose lectin chromatography to remove residual L2L2.</p></dd><dt>d.</dt><dd><p class="no_top_margin">The pass-through fractions are desalted using Sephadex G-25 gel filtration (1.3 × 68 cm, equilibrated and eluted with EtOH/water 1:19). Finally, 27 nmol of GlcNAcβ1-3L2L2 is obtained.</p></dd></dl></dd><dt>2.</dt><dd><p class="no_top_margin">Assay of CHST6</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">A total of 20 μL of the reaction mixture containing 50 mM of sodium cacodylate (pH 6.8), 10 mM of MnCl<sub>2</sub>, 0.1% (w/v) digitonin (if enzyme sources are membrane fractions), 50 μg/mL of protamine chloride, 2 mM of dithiothreitol, 0.1 M NaF, 2 mM of ATP-Na<sub>2</sub>, 6.5 μM of [<sup>35</sup>S]PAPS (4.9 × 10<sup>5</sup> dpm), 0.1 mM of GlcNAcβ1-3L2L2, and the enzyme fractions [in 20 mM of HEPES-NaOH (pH 7.2); prepared according to Ref. <a class="bk_pop" href="#g85-assaystks.REF.3">3</a>], is incubated at 37°C for 1 h.</p></dd><dt>b.</dt><dd><p class="no_top_margin">Add 0.5 mL of 0.01 N HCl and heat at 100°C for 10 min to destroy residual [<sup>35</sup>S]PAPS. After cooling, the mixture is neutralized and concentrated by vacuum evaporator.</p></dd><dt>c.</dt><dd><p class="no_top_margin">Spot the mixture and bromophenol blue as a marker on a Whatman No. 1 paper (46 × 57 cm).</p></dd><dt>d.</dt><dd><p class="no_top_margin">Wet the paper with pyridine/acetic acid/water = 3:1:387 (pH 5.4).</p></dd><dt>e.</dt><dd><p class="no_top_margin">Set the paper into the high-voltage paper electrophoresis unit and perform electrophoresis at 4,000 V with the same solvent as Step 2d), until the marker moves 10 cm from the origin.</p></dd><dt>f.</dt><dd><p class="no_top_margin">Dry the paper in the draft, and measure the radioactivity using a radiochromatogram scanner. Generally, [<sup>35</sup>S]-labeled reaction product moves near the marker, while free sulfate moves about 2.5-fold forward from the marker.</p></dd></dl></dd><dt>3.</dt><dd><p class="no_top_margin">Assay of CHST1</p><dl class="temp-labeled-list"><dt>a.</dt><dd><p class="no_top_margin">Prepare the reaction mixture as above, except for adding 50 mM of sodium cacodylate (pH 6.4), 0.1% (v/v) Triton X-100, and 0.5 mg/mL of keratan sulfate in place of sodium cacodylate (pH 6.8), digitonin, and GlcNAcβ1-3L2L2, respectively.</p></dd><dt>b.</dt><dd><p class="no_top_margin">Same as Steps 2b-f. [<sup>35</sup>S]-labeled reaction products move as a smear profile between the origin and the marker.</p></dd></dl></dd></dl></div><div id="g85-assaystks.Notes"><h3>Notes</h3><dl class="temp-labeled-list"><dt>1.</dt><dd><p class="no_top_margin">CHST6 and CHST1 belong to the GlcNAc6ST family, which comprises 7 members in humans. If enzyme fractions to be analyzed are crude, it is difficult to determine the individual enzymatic activities of CHST6 and CHST1 because some of the other members can utilize keratan sulfate or GlcNAcβ1-3L2L2 as a donor substrate. For example, not only CHST1 but also CHST3 (C6ST-1) can act on keratan sulfate. Similarly, GlcNAcβ1-3L2L2 can be utilized by CHST1, CHST2 (GlcNAc6ST1), CHST6, and CHST7 (GlcNAc6ST4). CHST2, 7, and 6 can catalyze the sulfation of the 6-OH of nonreducing terminal GlcNAc of GlcNAcβ1-3L2L2, although the ratio of Vmax/Km values of the three enzymes for the substrate is 26:4:100, indicating the preference of CHST6 for the substrate. CHST1 can catalyze the sulfation of internal Gal residues of the substrate.</p></dd><dt>2.</dt><dd><p class="no_top_margin">Akama et al. showed that CHST6 is a cause gene of macular corneal dystrophy and responsible for keratan sulfate biosynthesis in the human cornea (<a class="bk_pop" href="#g85-assaystks.REF.6">6</a>). Conversely, Zhang et al. showed that the deficiency of CHST2 causes loss of keratan sulfate in the mouse brain (<a class="bk_pop" href="#g85-assaystks.REF.7">7</a>). Recently, Narentuya et al. showed that CHST5 is a major enzyme as KS sulfotransferase in oligodendrocytes in adult mice (<a class="bk_pop" href="#g85-assaystks.REF.8">8</a>).</p></dd><dt>3.</dt><dd><p class="no_top_margin">Their recombinant enzymes produced in <i>E. coli</i> would be generally inactive, probably due to their insolubility or improper folding. Other hosts, such as <i>Pichia pastoris</i> or culture cells (CHO, COS, and so on), are recommended.</p></dd><dt>4.</dt><dd><p class="no_top_margin">There is a danger of electric shock when using a high-voltage paper electrophoresis unit. The power source must be turned off when papers would be placed into the unit or taken out from it.</p></dd></dl></div></div><div id="g85-assaystks.References"><h2 id="_g85-assaystks_References_">References</h2><dl class="temp-labeled-list"><dt>1.</dt><dd><div class="bk_ref" id="g85-assaystks.REF.1">Torii T, Fukuta M, Habuchi O. Sulfation of sialyl N-acetyllactosamine oligosaccharides and fetuin oligosaccharides by keratan sulfate Gal-6-sulfotransferase. <span><span class="ref-journal">Glycobiology. </span>2000 Feb;<span class="ref-vol">10</span>(2):203–11.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/10642612" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 10642612</span></a>] [<a href="http://dx.crossref.org/10.1093/glycob/10.2.203" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>2.</dt><dd><div class="bk_ref" id="g85-assaystks.REF.2">Akama TO, Misra AK, Hindsgaul O, Fukuda MN. Enzymatic synthesis in vitro of the disulfated disaccharide unit of corneal keratin sulfate. <span><span class="ref-journal">J Biol Chem. </span>2002 Nov 8;<span class="ref-vol">277</span>(45):42505–13.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/12218059" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 12218059</span></a>] [<a href="http://dx.crossref.org/10.1074/jbc.M207412200" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>3.</dt><dd><div class="bk_ref" id="g85-assaystks.REF.3">Seko A, Nagata K, Yonezawa S, Yamashita K. Ectopic expression of a GlcNAc 6-O-sulfotransferase, GlcNAc6ST-2, in colonic mucinous adenocarcinoma. <span><span class="ref-journal">Glycobiology. </span>2002 Jun;<span class="ref-vol">12</span>(6):379–88.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/12107080" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 12107080</span></a>] [<a href="http://dx.crossref.org/10.1093/glycob/12.6.379" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>4.</dt><dd><div class="bk_ref" id="g85-assaystks.REF.4">Brown GM, Huckerby TN, Nieduszynski IA. Oligosaccharides derived by keratanase II digestion of bovine articular cartilage keratin sulphates. <span><span class="ref-journal">Eur J Biochem. </span>1994 Sep 1;<span class="ref-vol">224</span>(2):281–308.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/7925342" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 7925342</span></a>] [<a href="http://dx.crossref.org/10.1111/j.1432-1033.1994.00281.x" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>5.</dt><dd><div class="bk_ref" id="g85-assaystks.REF.5">Seko A, Yamashita K. β1,3-N-Acetylglucosaminyltransferase-7 (β3Gn-T7) acts efficiently on keratan sulfate-related glycans. <span><span class="ref-journal">FEBS Lett. </span>2004 Jan 2;<span class="ref-vol">556</span>(1-3):216–20.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/14706853" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 14706853</span></a>] [<a href="http://dx.crossref.org/10.1016/s0014-5793(03)01440-6" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>6.</dt><dd><div class="bk_ref" id="g85-assaystks.REF.6">Akama TO, Nishida K, Nakayama J, Watanabe H, Ozaki K, Nakamura T, Dota A, Kawasaki S, Inoue Y, Maeda N, Yamamoto S, Fujiwara T, Thonar EJ, Shimomura Y, Kinoshita S, Tanigami A, Fukuda MN. Macular corneal dystrophy type I and type II are caused by distinct mutations in a new sulphotranseferase gene. <span><span class="ref-journal">Nat Genet. </span>2000 Oct;<span class="ref-vol">26</span>(2):237–41.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/11017086" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 11017086</span></a>] [<a href="http://dx.crossref.org/10.1038/79987" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>7.</dt><dd><div class="bk_ref" id="g85-assaystks.REF.7">Zhang H, Muramatsu T, Murase A, Yuasa S, Uchimura K, Kadomatsu K. N-acetylglucosamine 6-O-sulfotransferase-1 is required for brain keratan sulfate biosynthesis and glial scar formation after brain injury. <span><span class="ref-journal">Glycobiology. </span>2006 Aug;<span class="ref-vol">16</span>(8):702–10.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/16624895" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 16624895</span></a>] [<a href="http://dx.crossref.org/10.1093/glycob/cwj115" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd><dt>8.</dt><dd><div class="bk_ref" id="g85-assaystks.REF.8">Narentuya Takeda-Uchimura Y, Foyez T, Zhang Z, Akama TO, Yagi H, Kato K, Komatsu Y, Kadomatsu K, Uchimura K. GlcNAc6ST3 is a keratan sulfate sulfotransferase for the protein-tyrosine phosphatase PTPRZ in the adult brain. <span><span class="ref-journal">Sci Rep. </span>2019 Mar 13;<span class="ref-vol">9</span>(1):4387.</span> [<a href="/pmc/articles/PMC6416290/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC6416290</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/30867513" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 30867513</span></a>] [<a href="http://dx.crossref.org/10.1038/s41598-019-40901-2" ref="pagearea=cite-ref&targetsite=external&targetcat=link&targettype=uri">CrossRef</a>]</div></dd></dl></div><h2 id="NBK593949_footnotes">Footnotes</h2><dl class="temp-labeled-list small"><dt></dt><dd><div id="g85-assaystks.FN1"><p class="no_top_margin">The authors declare no competing or financial interests.</p></div></dd></dl><div class="bk_prnt_sctn"><h2>Figures</h2><div class="whole_rhythm bk_prnt_obj bk_first_prnt_obj"><div id="g85-assaystks.F1" class="figure bk_fig"><div class="graphic"><img src="/books/NBK593949/bin/g85-assaystks-Image001.jpg" alt="Figure 1. . Biosynthesis of keratan sulfate." /></div><h3><span class="label">Figure 1. </span></h3><div class="caption"><p>Biosynthesis of keratan sulfate.</p><p>See Introduction for each step in detail.</p></div></div></div></div><div id="bk_toc_contnr"></div></div></div>
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