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Defects in tendon, ligament, and enthesis in response to genetic alterations in key proteoglycans and glycoproteins: a review.

Arthritis

Juneja SC, Veillette C.
PMID: 24324885
Arthritis. 2013;2013:154812. doi: 10.1155/2013/154812. Epub 2013 Nov 10.

This review summarizes the genetic alterations and knockdown approaches published in the literature to assess the role of key proteoglycans and glycoproteins in the structural development, function, and repair of tendon, ligament, and enthesis. The information was collected from...

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Juneja SC, Veillette C. Defects in tendon, ligament, and enthesis in response to genetic alterations in key proteoglycans and glycoproteins: a review. Arthritis. 2013;2013:154812doi: 10.1155/2013/154812.
Juneja, S. C., & Veillette, C. (2013). Defects in tendon, ligament, and enthesis in response to genetic alterations in key proteoglycans and glycoproteins: a review. Arthritis, 2013154812. https://doi.org/10.1155/2013/154812
Juneja, Subhash C, and Veillette, Christian. "Defects in tendon, ligament, and enthesis in response to genetic alterations in key proteoglycans and glycoproteins: a review." Arthritis vol. 2013 (2013): 154812. doi: https://doi.org/10.1155/2013/154812
Juneja SC, Veillette C. Defects in tendon, ligament, and enthesis in response to genetic alterations in key proteoglycans and glycoproteins: a review. Arthritis. 2013;2013:154812. doi: 10.1155/2013/154812. Epub 2013 Nov 10. PMID: 24324885; PMCID: PMC3842050.
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Re-expression of glucuronyl C5-epimerase in the mutant MEF cells increases heparan sulfate epimerization but has no influence on the Golgi localization and enzymatic activity of 2-O-sulfotransferase.

Glycobiology

Cui H, Wang Z, Zhang T, Li JP, Fang J.
PMID: 33755115
Glycobiology. 2021 Sep 09;31(8):1018-1025. doi: 10.1093/glycob/cwab019.

Heparan sulfate (HS) is a linear and complex polysaccharide that modulates the biological activities through protein recognition and interaction. Evidence indicates that protein-binding properties of HS are largely dependent on distinctive sulfation and epimerization patterns that are modified by...

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Cui H, Wang Z, Zhang T, et al. Re-expression of glucuronyl C5-epimerase in the mutant MEF cells increases heparan sulfate epimerization but has no influence on the Golgi localization and enzymatic activity of 2-O-sulfotransferase. Glycobiology. 2021;31(8):1018-1025doi: 10.1093/glycob/cwab019.
Cui, H., Wang, Z., Zhang, T., Li, J. P., & Fang, J. (2021). Re-expression of glucuronyl C5-epimerase in the mutant MEF cells increases heparan sulfate epimerization but has no influence on the Golgi localization and enzymatic activity of 2-O-sulfotransferase. Glycobiology, 31(8), 1018-1025. https://doi.org/10.1093/glycob/cwab019
Cui, Hao, et al. "Re-expression of glucuronyl C5-epimerase in the mutant MEF cells increases heparan sulfate epimerization but has no influence on the Golgi localization and enzymatic activity of 2-O-sulfotransferase." Glycobiology vol. 31,8 (2021): 1018-1025. doi: https://doi.org/10.1093/glycob/cwab019
Cui H, Wang Z, Zhang T, Li JP, Fang J. Re-expression of glucuronyl C5-epimerase in the mutant MEF cells increases heparan sulfate epimerization but has no influence on the Golgi localization and enzymatic activity of 2-O-sulfotransferase. Glycobiology. 2021 Sep 09;31(8):1018-1025. doi: 10.1093/glycob/cwab019. PMID: 33755115.
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Domain Mapping of Chondroitin/Dermatan Sulfate Glycosaminoglycans Enables Structural Characterization of Proteoglycans.

Molecular & cellular proteomics : MCP

Persson A, Nikpour M, Vorontsov E, Nilsson J, Larson G.
PMID: 33757834
Mol Cell Proteomics. 2021;20:100074. doi: 10.1016/j.mcpro.2021.100074. Epub 2021 Mar 20.

Of all posttranslational modifications known, glycosaminoglycans (GAGs) remain one of the most challenging to study, and despite the recent years of advancement in MS technologies and bioinformatics, detailed knowledge about the complete structures of GAGs as part of proteoglycans...

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Persson A, Nikpour M, Vorontsov E, et al. Domain Mapping of Chondroitin/Dermatan Sulfate Glycosaminoglycans Enables Structural Characterization of Proteoglycans. Mol Cell Proteomics. 2021;20:100074doi: 10.1016/j.mcpro.2021.100074.
Persson, A., Nikpour, M., Vorontsov, E., Nilsson, J., & Larson, G. (2021). Domain Mapping of Chondroitin/Dermatan Sulfate Glycosaminoglycans Enables Structural Characterization of Proteoglycans. Molecular & cellular proteomics : MCP, 20100074. https://doi.org/10.1016/j.mcpro.2021.100074
Persson, Andrea, et al. "Domain Mapping of Chondroitin/Dermatan Sulfate Glycosaminoglycans Enables Structural Characterization of Proteoglycans." Molecular & cellular proteomics : MCP vol. 20 (2021): 100074. doi: https://doi.org/10.1016/j.mcpro.2021.100074
Persson A, Nikpour M, Vorontsov E, Nilsson J, Larson G. Domain Mapping of Chondroitin/Dermatan Sulfate Glycosaminoglycans Enables Structural Characterization of Proteoglycans. Mol Cell Proteomics. 2021;20:100074. doi: 10.1016/j.mcpro.2021.100074. Epub 2021 Mar 20. PMID: 33757834.
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Synthesis and immunomodulatory activity of the sulfated tetrasaccharide motif of type B ulvanobiuronic acid 3-sulfate.

Organic & biomolecular chemistry

Zhang L, Wang X, Hua Q, Wang J, Liu J, Yang Y.
PMID: 33001123
Org Biomol Chem. 2020 Oct 14;18(39):7932-7935. doi: 10.1039/d0ob01852j.

Ulvan is a sulfated polysaccharide from green algae with potent antitumor, antiviral, and immunomodulatory activities. However, no chemical synthesis of ulvan saccharides has been reported to date. In this paper, we performed the first efficient synthesis of the unique...

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Zhang L, Wang X, Hua Q, et al. Synthesis and immunomodulatory activity of the sulfated tetrasaccharide motif of type B ulvanobiuronic acid 3-sulfate. Org Biomol Chem. 2020;18(39):7932-7935doi: 10.1039/d0ob01852j.
Zhang, L., Wang, X., Hua, Q., Wang, J., Liu, J., & Yang, Y. (2020). Synthesis and immunomodulatory activity of the sulfated tetrasaccharide motif of type B ulvanobiuronic acid 3-sulfate. Organic & biomolecular chemistry, 18(39), 7932-7935. https://doi.org/10.1039/d0ob01852j
Zhang, Liangliang, et al. "Synthesis and immunomodulatory activity of the sulfated tetrasaccharide motif of type B ulvanobiuronic acid 3-sulfate." Organic & biomolecular chemistry vol. 18,39 (2020): 7932-7935. doi: https://doi.org/10.1039/d0ob01852j
Zhang L, Wang X, Hua Q, Wang J, Liu J, Yang Y. Synthesis and immunomodulatory activity of the sulfated tetrasaccharide motif of type B ulvanobiuronic acid 3-sulfate. Org Biomol Chem. 2020 Oct 14;18(39):7932-7935. doi: 10.1039/d0ob01852j. PMID: 33001123.
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Structural characterization of ulvans extracted from blade (Ulva ohnoi) and filamentous (Ulva tepida and Ulva prolifera) species of cultivated Ulva.

International journal of biological macromolecules

Glasson CRK, Luiten CA, Carnachan SM, Daines AM, Kidgell JT, Hinkley SFR, Praeger C, Andrade Martinez M, Sargison L, Magnusson M, de Nys R, Sims IM.
PMID: 34813787
Int J Biol Macromol. 2022 Jan 01;194:571-579. doi: 10.1016/j.ijbiomac.2021.11.100. Epub 2021 Nov 20.

Ulvans from Ulva ohnoi, Ulva tepida and Ulva prolifera were extracted under mild acidic conditions, isolated and their composition and structure determined. The ulvans contained mostly rhamnose (31.6-46.7 mol%) and glucuronic acid (26.6-37.5 mol%), with smaller amounts of xylose...

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Glasson CRK, Luiten CA, Carnachan SM, et al. Structural characterization of ulvans extracted from blade (Ulva ohnoi) and filamentous (Ulva tepida and Ulva prolifera) species of cultivated Ulva. Int J Biol Macromol. 2021;194:571-579doi: 10.1016/j.ijbiomac.2021.11.100.
Glasson, C. R. K., Luiten, C. A., Carnachan, S. M., Daines, A. M., Kidgell, J. T., Hinkley, S. F. R., Praeger, C., Andrade Martinez, M., Sargison, L., Magnusson, M., de Nys, R., & Sims, I. M. (2022). Structural characterization of ulvans extracted from blade (Ulva ohnoi) and filamentous (Ulva tepida and Ulva prolifera) species of cultivated Ulva. International journal of biological macromolecules, 194571-579. https://doi.org/10.1016/j.ijbiomac.2021.11.100
Glasson, Christopher R K, et al. "Structural characterization of ulvans extracted from blade (Ulva ohnoi) and filamentous (Ulva tepida and Ulva prolifera) species of cultivated Ulva." International journal of biological macromolecules vol. 194 (2022): 571-579. doi: https://doi.org/10.1016/j.ijbiomac.2021.11.100
Glasson CRK, Luiten CA, Carnachan SM, Daines AM, Kidgell JT, Hinkley SFR, Praeger C, Andrade Martinez M, Sargison L, Magnusson M, de Nys R, Sims IM. Structural characterization of ulvans extracted from blade (Ulva ohnoi) and filamentous (Ulva tepida and Ulva prolifera) species of cultivated Ulva. Int J Biol Macromol. 2022 Jan 01;194:571-579. doi: 10.1016/j.ijbiomac.2021.11.100. Epub 2021 Nov 20. PMID: 34813787.
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Sulfation Code and Conformational Plasticity of l-Iduronic Acid Homo-Oligosaccharides Mimic the Biological Functions of Heparan Sulfate.

ACS chemical biology

Shanthamurthy CD, Gimeno A, Leviatan Ben-Arye S, Kumar NV, Jain P, Padler-Karavani V, Jiménez-Barbero J, Kikkeri R.
PMID: 34586794
ACS Chem Biol. 2021 Nov 19;16(11):2481-2489. doi: 10.1021/acschembio.1c00582. Epub 2021 Sep 29.

Recently, the activity of heparan sulfate (HS) has led to the discovery of many drug candidates that have the potential to impact both medical science and human health. However, structural diversity and synthetic challenges impede the progress of HS...

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Shanthamurthy CD, Gimeno A, Leviatan Ben-Arye S, et al. Sulfation Code and Conformational Plasticity of l-Iduronic Acid Homo-Oligosaccharides Mimic the Biological Functions of Heparan Sulfate. ACS Chem Biol. 2021;16(11):2481-2489doi: 10.1021/acschembio.1c00582.
Shanthamurthy, C. D., Gimeno, A., Leviatan Ben-Arye, S., Kumar, N. V., Jain, P., Padler-Karavani, V., Jiménez-Barbero, J., & Kikkeri, R. (2021). Sulfation Code and Conformational Plasticity of l-Iduronic Acid Homo-Oligosaccharides Mimic the Biological Functions of Heparan Sulfate. ACS chemical biology, 16(11), 2481-2489. https://doi.org/10.1021/acschembio.1c00582
Shanthamurthy, Chethan D, et al. "Sulfation Code and Conformational Plasticity of l-Iduronic Acid Homo-Oligosaccharides Mimic the Biological Functions of Heparan Sulfate." ACS chemical biology vol. 16,11 (2021): 2481-2489. doi: https://doi.org/10.1021/acschembio.1c00582
Shanthamurthy CD, Gimeno A, Leviatan Ben-Arye S, Kumar NV, Jain P, Padler-Karavani V, Jiménez-Barbero J, Kikkeri R. Sulfation Code and Conformational Plasticity of l-Iduronic Acid Homo-Oligosaccharides Mimic the Biological Functions of Heparan Sulfate. ACS Chem Biol. 2021 Nov 19;16(11):2481-2489. doi: 10.1021/acschembio.1c00582. Epub 2021 Sep 29. PMID: 34586794.
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The Heparan Sulfate Sulfotransferases HS2ST1 and HS3ST2 Are Novel Regulators of Breast Cancer Stem-Cell Properties.

Frontiers in cell and developmental biology

Teixeira FCOB, Vijaya Kumar A, Kumar Katakam S, Cocola C, Pelucchi P, Graf M, Kiesel L, Reinbold R, Pavão MSG, Greve B, Götte M.
PMID: 33102470
Front Cell Dev Biol. 2020 Sep 25;8:559554. doi: 10.3389/fcell.2020.559554. eCollection 2020.

Heparan sulfate (HS) is a glycosaminoglycan found mainly in its protein-conjugated form at the cell surface and the extracellular matrix. Its high sulfation degree mediates functional interactions with positively charged amino acids in proteins. 2-O sulfation of iduronic acid...

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Teixeira FCOB, Vijaya Kumar A, Kumar Katakam S, et al. The Heparan Sulfate Sulfotransferases HS2ST1 and HS3ST2 Are Novel Regulators of Breast Cancer Stem-Cell Properties. Front Cell Dev Biol. 2020;8:559554doi: 10.3389/fcell.2020.559554.
Teixeira, F. C. O. B., Vijaya Kumar, A., Kumar Katakam, S., Cocola, C., Pelucchi, P., Graf, M., Kiesel, L., Reinbold, R., Pavão, M. S. G., Greve, B., & Götte, M. (2020). The Heparan Sulfate Sulfotransferases HS2ST1 and HS3ST2 Are Novel Regulators of Breast Cancer Stem-Cell Properties. Frontiers in cell and developmental biology, 8559554. https://doi.org/10.3389/fcell.2020.559554
Teixeira, Felipe C O B, et al. "The Heparan Sulfate Sulfotransferases HS2ST1 and HS3ST2 Are Novel Regulators of Breast Cancer Stem-Cell Properties." Frontiers in cell and developmental biology vol. 8 (2020): 559554. doi: https://doi.org/10.3389/fcell.2020.559554
Teixeira FCOB, Vijaya Kumar A, Kumar Katakam S, Cocola C, Pelucchi P, Graf M, Kiesel L, Reinbold R, Pavão MSG, Greve B, Götte M. The Heparan Sulfate Sulfotransferases HS2ST1 and HS3ST2 Are Novel Regulators of Breast Cancer Stem-Cell Properties. Front Cell Dev Biol. 2020 Sep 25;8:559554. doi: 10.3389/fcell.2020.559554. eCollection 2020. PMID: 33102470; PMCID: PMC7546021.
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Synthesis of Conformationally Locked Carbohydrates: A Skew-Boat Conformation of L-Iduronic Acid Governs the Antithrombotic Activity of Heparin.

Angewandte Chemie (International ed. in English)

Das SK, Mallet JM, Esnault J, Driguez PA, Duchaussoy P, Sizun P, Hérault JP, Herbert JM, Petitou M, Sinaÿ P.
PMID: 11353474
Angew Chem Int Ed Engl. 2001 May 04;40(9):1670-1673.

No abstract available.

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Das SK, Mallet JM, Esnault J, et al. Synthesis of Conformationally Locked Carbohydrates: A Skew-Boat Conformation of L-Iduronic Acid Governs the Antithrombotic Activity of Heparin. Angew Chem Int Ed Engl. 2001;40(9):1670-1673
Das, S. K., Mallet, J. M., Esnault, J., Driguez, P. A., Duchaussoy, P., Sizun, P., Hérault, J. P., Herbert, J. M., Petitou, M., & Sinaÿ, P. (2001). Synthesis of Conformationally Locked Carbohydrates: A Skew-Boat Conformation of L-Iduronic Acid Governs the Antithrombotic Activity of Heparin. Angewandte Chemie (International ed. in English), 40(9), 1670-1673.
Das, Sanjoy K., et al. "Synthesis of Conformationally Locked Carbohydrates: A Skew-Boat Conformation of L-Iduronic Acid Governs the Antithrombotic Activity of Heparin." Angewandte Chemie (International ed. in English) vol. 40,9 (2001): 1670-1673.
Das SK, Mallet JM, Esnault J, Driguez PA, Duchaussoy P, Sizun P, Hérault JP, Herbert JM, Petitou M, Sinaÿ P. Synthesis of Conformationally Locked Carbohydrates: A Skew-Boat Conformation of L-Iduronic Acid Governs the Antithrombotic Activity of Heparin. Angew Chem Int Ed Engl. 2001 May 04;40(9):1670-1673. PMID: 11353474.
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Synthesis of l-Pyranosides by Hydroboration of Hex-5-enopyranosides Revisited.

The Journal of organic chemistry

Łopatkiewicz G, Mlynarski J.
PMID: 27504790
J Org Chem. 2016 Sep 02;81(17):7545-56. doi: 10.1021/acs.joc.6b01243. Epub 2016 Aug 18.

Extensive study of the diastereoselective synthesis of l-pyranosides utilizing hydroboration of substituted exo-glucals (5-enopyranosides) obtained from d-sugars is presented. On the basis of this study we present the empirical rules describing the reaction stereoselectivity and the correlation between the...

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Łopatkiewicz G, Mlynarski J. Synthesis of l-Pyranosides by Hydroboration of Hex-5-enopyranosides Revisited. J Org Chem. 2016;81(17):7545-56doi: 10.1021/acs.joc.6b01243.
Łopatkiewicz, G., & Mlynarski, J. (2016). Synthesis of l-Pyranosides by Hydroboration of Hex-5-enopyranosides Revisited. The Journal of organic chemistry, 81(17), 7545-56. https://doi.org/10.1021/acs.joc.6b01243
Łopatkiewicz, Grzegorz, and Mlynarski, Jacek. "Synthesis of l-Pyranosides by Hydroboration of Hex-5-enopyranosides Revisited." The Journal of organic chemistry vol. 81,17 (2016): 7545-56. doi: https://doi.org/10.1021/acs.joc.6b01243
Łopatkiewicz G, Mlynarski J. Synthesis of l-Pyranosides by Hydroboration of Hex-5-enopyranosides Revisited. J Org Chem. 2016 Sep 02;81(17):7545-56. doi: 10.1021/acs.joc.6b01243. Epub 2016 Aug 18. PMID: 27504790.
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Plasmatic and Urinary Glycosaminoglycans Characterization in Mucopolysaccharidosis II Patient Treated with Enzyme-Replacement Therapy with Idursulfase.

JIMD reports

Coppa GV, Buzzega D, Zampini L, Maccari F, Santoro L, Galeotti F, Galeazzi T, Gabrielli O, Volpi N.
PMID: 23430900
JIMD Rep. 2012;4:79-90. doi: 10.1007/8904_2011_75. Epub 2011 Nov 04.

We report the structural characterization of plasmatic and urinary GAGs in a patient affected by MPS II (Hunter syndrome) before and during the first 10 months of enzyme-replacement therapy (ERT). Plasmatic GAGs before ERT were rich in pathological DS...

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Coppa GV, Buzzega D, Zampini L, et al. Plasmatic and Urinary Glycosaminoglycans Characterization in Mucopolysaccharidosis II Patient Treated with Enzyme-Replacement Therapy with Idursulfase. JIMD Rep. 2011;4:79-90doi: 10.1007/8904_2011_75.
Coppa, G. V., Buzzega, D., Zampini, L., Maccari, F., Santoro, L., Galeotti, F., Galeazzi, T., Gabrielli, O., & Volpi, N. (2012). Plasmatic and Urinary Glycosaminoglycans Characterization in Mucopolysaccharidosis II Patient Treated with Enzyme-Replacement Therapy with Idursulfase. JIMD reports, 479-90. https://doi.org/10.1007/8904_2011_75
Coppa, Giovanni V, et al. "Plasmatic and Urinary Glycosaminoglycans Characterization in Mucopolysaccharidosis II Patient Treated with Enzyme-Replacement Therapy with Idursulfase." JIMD reports vol. 4 (2012): 79-90. doi: https://doi.org/10.1007/8904_2011_75
Coppa GV, Buzzega D, Zampini L, Maccari F, Santoro L, Galeotti F, Galeazzi T, Gabrielli O, Volpi N. Plasmatic and Urinary Glycosaminoglycans Characterization in Mucopolysaccharidosis II Patient Treated with Enzyme-Replacement Therapy with Idursulfase. JIMD Rep. 2012;4:79-90. doi: 10.1007/8904_2011_75. Epub 2011 Nov 04. PMID: 23430900; PMCID: PMC3509895.
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Domain Mapping of Chondroitin/Dermatan Sulfate Glycosaminoglycans Enables Structural Characterization of Proteoglycans.

Molecular & cellular proteomics : MCP

Persson A, Nikpour M, Vorontsov E, Nilsson J, Larson G.
PMID: 33757834
Mol Cell Proteomics. 2021;20:100074. doi: 10.1016/j.mcpro.2021.100074. Epub 2021 Mar 20.

Of all posttranslational modifications known, glycosaminoglycans (GAGs) remain one of the most challenging to study, and despite the recent years of advancement in MS technologies and bioinformatics, detailed knowledge about the complete structures of GAGs as part of proteoglycans...

Cite
Persson A, Nikpour M, Vorontsov E, et al. Domain Mapping of Chondroitin/Dermatan Sulfate Glycosaminoglycans Enables Structural Characterization of Proteoglycans. Mol Cell Proteomics. 2021;20:100074doi: 10.1016/j.mcpro.2021.100074.
Persson, A., Nikpour, M., Vorontsov, E., Nilsson, J., & Larson, G. (2021). Domain Mapping of Chondroitin/Dermatan Sulfate Glycosaminoglycans Enables Structural Characterization of Proteoglycans. Molecular & cellular proteomics : MCP, 20100074. https://doi.org/10.1016/j.mcpro.2021.100074
Persson, Andrea, et al. "Domain Mapping of Chondroitin/Dermatan Sulfate Glycosaminoglycans Enables Structural Characterization of Proteoglycans." Molecular & cellular proteomics : MCP vol. 20 (2021): 100074. doi: https://doi.org/10.1016/j.mcpro.2021.100074
Persson A, Nikpour M, Vorontsov E, Nilsson J, Larson G. Domain Mapping of Chondroitin/Dermatan Sulfate Glycosaminoglycans Enables Structural Characterization of Proteoglycans. Mol Cell Proteomics. 2021;20:100074. doi: 10.1016/j.mcpro.2021.100074. Epub 2021 Mar 20. PMID: 33757834; PMCID: PMC8724862.
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Inhibition of iduronic acid biosynthesis by ebselen reduces glycosaminoglycan accumulation in mucopolysaccharidosis type I fibroblasts.

Glycobiology

Maccarana M, Tykesson E, Pera EM, Gouignard N, Fang J, Malmström A, Ghiselli G, Li JP.
PMID: 34192316
Glycobiology. 2021 Nov 18;31(10):1319-1329. doi: 10.1093/glycob/cwab066.

Mucopolysaccharidosis type I (MPS-I) is a rare lysosomal storage disorder caused by deficiency of the enzyme alpha-L-iduronidase, which removes iduronic acid in both chondroitin/dermatan sulfate (CS/DS) and heparan sulfate (HS) and thereby contributes to the catabolism of glycosaminoglycans (GAGs)....

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Maccarana M, Tykesson E, Pera EM, et al. Inhibition of iduronic acid biosynthesis by ebselen reduces glycosaminoglycan accumulation in mucopolysaccharidosis type I fibroblasts. Glycobiology. 2021;31(10):1319-1329doi: 10.1093/glycob/cwab066.
Maccarana, M., Tykesson, E., Pera, E. M., Gouignard, N., Fang, J., Malmström, A., Ghiselli, G., & Li, J. P. (2021). Inhibition of iduronic acid biosynthesis by ebselen reduces glycosaminoglycan accumulation in mucopolysaccharidosis type I fibroblasts. Glycobiology, 31(10), 1319-1329. https://doi.org/10.1093/glycob/cwab066
Maccarana, Marco, et al. "Inhibition of iduronic acid biosynthesis by ebselen reduces glycosaminoglycan accumulation in mucopolysaccharidosis type I fibroblasts." Glycobiology vol. 31,10 (2021): 1319-1329. doi: https://doi.org/10.1093/glycob/cwab066
Maccarana M, Tykesson E, Pera EM, Gouignard N, Fang J, Malmström A, Ghiselli G, Li JP. Inhibition of iduronic acid biosynthesis by ebselen reduces glycosaminoglycan accumulation in mucopolysaccharidosis type I fibroblasts. Glycobiology. 2021 Nov 18;31(10):1319-1329. doi: 10.1093/glycob/cwab066. PMID: 34192316; PMCID: PMC8600295.
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