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Involvement of heparan sulfate 3-O-sulfotransferase isoform-1 in the insulin secretion pathway.

Journal of diabetes investigation

Takahashi I, Ohashi K, Nata K.
PMID: 24843591
J Diabetes Investig. 2012 Aug 20;3(4):362-70. doi: 10.1111/j.2040-1124.2012.00205.x.

UNLABELLED: Aims/Introduction:  Heparan sulfate (HS) mediates a variety of molecular recognition events that are essential for differentiation, morphogenesis and homeostasis through various HS forms that result from differential sulfate modification. Recently, we found that HS is localized exclusively around...

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Takahashi I, Ohashi K, Nata K. Involvement of heparan sulfate 3-O-sulfotransferase isoform-1 in the insulin secretion pathway. J Diabetes Investig. 2012;3(4):362-70doi: 10.1111/j.2040-1124.2012.00205.x.
Takahashi, I., Ohashi, K., & Nata, K. (2012). Involvement of heparan sulfate 3-O-sulfotransferase isoform-1 in the insulin secretion pathway. Journal of diabetes investigation, 3(4), 362-70. https://doi.org/10.1111/j.2040-1124.2012.00205.x
Takahashi, Iwao, et al. "Involvement of heparan sulfate 3-O-sulfotransferase isoform-1 in the insulin secretion pathway." Journal of diabetes investigation vol. 3,4 (2012): 362-70. doi: https://doi.org/10.1111/j.2040-1124.2012.00205.x
Takahashi I, Ohashi K, Nata K. Involvement of heparan sulfate 3-O-sulfotransferase isoform-1 in the insulin secretion pathway. J Diabetes Investig. 2012 Aug 20;3(4):362-70. doi: 10.1111/j.2040-1124.2012.00205.x. PMID: 24843591; PMCID: PMC4019256.
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Carbohydrate sulfotransferases: novel therapeutic targets for inflammation, viral infection and cancer.

Drug discovery today

Hemmerich S.
PMID: 11165170
Drug Discov Today. 2001 Jan 01;6(1):27-35. doi: 10.1016/s1359-6446(00)01581-6.

Effective direct inhibition of adhesion receptors by small molecules has been hampered by extended receptor-ligand interfaces as well as the entropic penalties often associated with inhibition of cell adhesion. Therefore, alternative strategies have targeted enzymes that are centrally involved...

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Hemmerich S. Carbohydrate sulfotransferases: novel therapeutic targets for inflammation, viral infection and cancer. Drug Discov Today. 2001;6(1):27-35doi: 10.1016/s1359-6446(00)01581-6.
Hemmerich, S. (2001). Carbohydrate sulfotransferases: novel therapeutic targets for inflammation, viral infection and cancer. Drug discovery today, 6(1), 27-35. https://doi.org/10.1016/s1359-6446(00)01581-6
Hemmerich, S. "Carbohydrate sulfotransferases: novel therapeutic targets for inflammation, viral infection and cancer." Drug discovery today vol. 6,1 (2001): 27-35. doi: https://doi.org/10.1016/s1359-6446(00)01581-6
Hemmerich S. Carbohydrate sulfotransferases: novel therapeutic targets for inflammation, viral infection and cancer. Drug Discov Today. 2001 Jan 01;6(1):27-35. doi: 10.1016/s1359-6446(00)01581-6. PMID: 11165170.
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Dose- and time-dependent changes in tissue levels of tetrabromobisphenol A (TBBPA) and its sulfate and glucuronide conjugates following repeated administration to female Wistar Han Rats.

Toxicology reports

Borghoff SJ, Wikoff D, Harvey S, Haws L.
PMID: 28959539
Toxicol Rep. 2016 Jan 12;3:190-201. doi: 10.1016/j.toxrep.2016.01.007. eCollection 2016.

Tetrabromobisphenol A (TBBPA), a nongenotoxic flame retardant, causes uterine tumors in female rats. A proposed mode of action (MoA) for these tumors involves an increase in the bioavailability of estradiol as a result of TBBPA inhibiting estrogen sulfotransferases (ES),...

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Borghoff SJ, Wikoff D, Harvey S, et al. Dose- and time-dependent changes in tissue levels of tetrabromobisphenol A (TBBPA) and its sulfate and glucuronide conjugates following repeated administration to female Wistar Han Rats. Toxicol Rep. 2016;3:190-201doi: 10.1016/j.toxrep.2016.01.007.
Borghoff, S. J., Wikoff, D., Harvey, S., & Haws, L. (2016). Dose- and time-dependent changes in tissue levels of tetrabromobisphenol A (TBBPA) and its sulfate and glucuronide conjugates following repeated administration to female Wistar Han Rats. Toxicology reports, 3190-201. https://doi.org/10.1016/j.toxrep.2016.01.007
Borghoff, S J, et al. "Dose- and time-dependent changes in tissue levels of tetrabromobisphenol A (TBBPA) and its sulfate and glucuronide conjugates following repeated administration to female Wistar Han Rats." Toxicology reports vol. 3 (2016): 190-201. doi: https://doi.org/10.1016/j.toxrep.2016.01.007
Borghoff SJ, Wikoff D, Harvey S, Haws L. Dose- and time-dependent changes in tissue levels of tetrabromobisphenol A (TBBPA) and its sulfate and glucuronide conjugates following repeated administration to female Wistar Han Rats. Toxicol Rep. 2016 Jan 12;3:190-201. doi: 10.1016/j.toxrep.2016.01.007. eCollection 2016. PMID: 28959539; PMCID: PMC5615791.
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The Important Roles of Steroid Sulfatase and Sulfotransferases in Gynecological Diseases.

Frontiers in pharmacology

Rižner TL.
PMID: 26924986
Front Pharmacol. 2016 Feb 18;7:30. doi: 10.3389/fphar.2016.00030. eCollection 2016.

Gynecological diseases such as endometriosis, adenomyosis and uterine fibroids, and gynecological cancers including endometrial cancer and ovarian cancer, affect a large proportion of women. These diseases are estrogen dependent, and their progression often depends on local estrogen formation. In...

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Rižner TL. The Important Roles of Steroid Sulfatase and Sulfotransferases in Gynecological Diseases. Front Pharmacol. 2016;7:30doi: 10.3389/fphar.2016.00030.
Rižner, T. L. (2016). The Important Roles of Steroid Sulfatase and Sulfotransferases in Gynecological Diseases. Frontiers in pharmacology, 730. https://doi.org/10.3389/fphar.2016.00030
Rižner, Tea Lanišnik. "The Important Roles of Steroid Sulfatase and Sulfotransferases in Gynecological Diseases." Frontiers in pharmacology vol. 7 (2016): 30. doi: https://doi.org/10.3389/fphar.2016.00030
Rižner TL. The Important Roles of Steroid Sulfatase and Sulfotransferases in Gynecological Diseases. Front Pharmacol. 2016 Feb 18;7:30. doi: 10.3389/fphar.2016.00030. eCollection 2016. PMID: 26924986; PMCID: PMC4757672.
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Syndecans and Enzymes for Heparan Sulfate Biosynthesis and Modification Differentially Correlate With Presence of Inflammatory Infiltrate in Periodontitis.

Frontiers in physiology

Duplancic R, Roguljic M, Puhar I, Vecek N, Dragun R, Vukojevic K, Saraga-Babic M, Kero D.
PMID: 31611818
Front Physiol. 2019 Sep 25;10:1248. doi: 10.3389/fphys.2019.01248. eCollection 2019.

Periodontitis is a common degenerative disease initiated by the bacteria in subgingival biofilm. The exposure to bacterial biofilm triggers host inflammatory response whose dysregulation is ultimately responsible for the destruction of hard and soft periodontal tissues resulting in tooth...

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Duplancic R, Roguljic M, Puhar I, et al. Syndecans and Enzymes for Heparan Sulfate Biosynthesis and Modification Differentially Correlate With Presence of Inflammatory Infiltrate in Periodontitis. Front Physiol. 2019;10:1248doi: 10.3389/fphys.2019.01248.
Duplancic, R., Roguljic, M., Puhar, I., Vecek, N., Dragun, R., Vukojevic, K., Saraga-Babic, M., & Kero, D. (2019). Syndecans and Enzymes for Heparan Sulfate Biosynthesis and Modification Differentially Correlate With Presence of Inflammatory Infiltrate in Periodontitis. Frontiers in physiology, 101248. https://doi.org/10.3389/fphys.2019.01248
Duplancic, Roko, et al. "Syndecans and Enzymes for Heparan Sulfate Biosynthesis and Modification Differentially Correlate With Presence of Inflammatory Infiltrate in Periodontitis." Frontiers in physiology vol. 10 (2019): 1248. doi: https://doi.org/10.3389/fphys.2019.01248
Duplancic R, Roguljic M, Puhar I, Vecek N, Dragun R, Vukojevic K, Saraga-Babic M, Kero D. Syndecans and Enzymes for Heparan Sulfate Biosynthesis and Modification Differentially Correlate With Presence of Inflammatory Infiltrate in Periodontitis. Front Physiol. 2019 Sep 25;10:1248. doi: 10.3389/fphys.2019.01248. eCollection 2019. PMID: 31611818; PMCID: PMC6773826.
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Syndecans and Enzymes Involved in Heparan Sulfate Biosynthesis and Degradation Are Differentially Expressed During Human Odontogenesis.

Frontiers in physiology

Kero D, Bilandzija TS, Arapovic LL, Vukojevic K, Saraga-Babic M.
PMID: 29962964
Front Physiol. 2018 Jun 14;9:732. doi: 10.3389/fphys.2018.00732. eCollection 2018.

Syndecans belong to a four-member family of cell surface heparan sulfate proteoglycans (HSPGs) abundantly present in various tissues. They are primarily recognized as extracellular matrix (ECM) receptors able to bind various ECM components and form gradients of morphogens and...

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Kero D, Bilandzija TS, Arapovic LL, et al. Syndecans and Enzymes Involved in Heparan Sulfate Biosynthesis and Degradation Are Differentially Expressed During Human Odontogenesis. Front Physiol. 2018;9:732doi: 10.3389/fphys.2018.00732.
Kero, D., Bilandzija, T. S., Arapovic, L. L., Vukojevic, K., & Saraga-Babic, M. (2018). Syndecans and Enzymes Involved in Heparan Sulfate Biosynthesis and Degradation Are Differentially Expressed During Human Odontogenesis. Frontiers in physiology, 9732. https://doi.org/10.3389/fphys.2018.00732
Kero, Darko, et al. "Syndecans and Enzymes Involved in Heparan Sulfate Biosynthesis and Degradation Are Differentially Expressed During Human Odontogenesis." Frontiers in physiology vol. 9 (2018): 732. doi: https://doi.org/10.3389/fphys.2018.00732
Kero D, Bilandzija TS, Arapovic LL, Vukojevic K, Saraga-Babic M. Syndecans and Enzymes Involved in Heparan Sulfate Biosynthesis and Degradation Are Differentially Expressed During Human Odontogenesis. Front Physiol. 2018 Jun 14;9:732. doi: 10.3389/fphys.2018.00732. eCollection 2018. PMID: 29962964; PMCID: PMC6010574.
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An activity-based fluorescent sensor for the detection of the phenol sulfotransferase SULT1A1 in living cells.

RSC chemical biology

Baglia RA, Mills KR, Mitra K, Tutol JN, Ball D, Page KM, Kallu J, Gottipolu S, D'Arcy S, Nielsen SO, Dodani SC.
PMID: 34212150
RSC Chem Biol. 2021 Mar 15;2(3):830-834. doi: 10.1039/d0cb00231c.

Human phenol sulfotransferases mediate the transfer of a sulfuryl moiety from the activated sulfate donor PAPS to hydroxy-containing substrates, altering substrate solubility and charge to affect phase II metabolism and cell signaling. Here, we present the development, computational modeling,

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Baglia RA, Mills KR, Mitra K, et al. An activity-based fluorescent sensor for the detection of the phenol sulfotransferase SULT1A1 in living cells. RSC Chem Biol. 2021;2(3):830-834doi: 10.1039/d0cb00231c.
Baglia, R. A., Mills, K. R., Mitra, K., Tutol, J. N., Ball, D., Page, K. M., Kallu, J., Gottipolu, S., D'Arcy, S., Nielsen, S. O., & Dodani, S. C. (2021). An activity-based fluorescent sensor for the detection of the phenol sulfotransferase SULT1A1 in living cells. RSC chemical biology, 2(3), 830-834. https://doi.org/10.1039/d0cb00231c
Baglia, Regina A, et al. "An activity-based fluorescent sensor for the detection of the phenol sulfotransferase SULT1A1 in living cells." RSC chemical biology vol. 2,3 (2021): 830-834. doi: https://doi.org/10.1039/d0cb00231c
Baglia RA, Mills KR, Mitra K, Tutol JN, Ball D, Page KM, Kallu J, Gottipolu S, D'Arcy S, Nielsen SO, Dodani SC. An activity-based fluorescent sensor for the detection of the phenol sulfotransferase SULT1A1 in living cells. RSC Chem Biol. 2021 Mar 15;2(3):830-834. doi: 10.1039/d0cb00231c. PMID: 34212150; PMCID: PMC8190907.
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Regulations of expressions of rat/human sulfotransferases by anticancer drug, nolatrexed, and micronutrients.

Anti-cancer drugs

Maiti S, MaitiDutta S, Chen G.
PMID: 34387600
Anticancer Drugs. 2022 Jan 01;33(1):e525-e533. doi: 10.1097/CAD.0000000000001155.

Cancer is related to the cellular proliferative state. Increase in cell-cycle regulatory function augments cellular folate pool. This pathway is therapeutically targeted. A number of drugs influences this metabolism, that is, folic acid, folinic acid, nolatrexed, and methotrexate. Our...

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Maiti S, MaitiDutta S, Chen G. Regulations of expressions of rat/human sulfotransferases by anticancer drug, nolatrexed, and micronutrients. Anticancer Drugs. 2022;33(1):e525-e533doi: 10.1097/CAD.0000000000001155.
Maiti, S., MaitiDutta, S., & Chen, G. (2022). Regulations of expressions of rat/human sulfotransferases by anticancer drug, nolatrexed, and micronutrients. Anti-cancer drugs, 33(1), e525-e533. https://doi.org/10.1097/CAD.0000000000001155
Maiti, Smarajit, et al. "Regulations of expressions of rat/human sulfotransferases by anticancer drug, nolatrexed, and micronutrients." Anti-cancer drugs vol. 33,1 (2022): e525-e533. doi: https://doi.org/10.1097/CAD.0000000000001155
Maiti S, MaitiDutta S, Chen G. Regulations of expressions of rat/human sulfotransferases by anticancer drug, nolatrexed, and micronutrients. Anticancer Drugs. 2022 Jan 01;33(1):e525-e533. doi: 10.1097/CAD.0000000000001155. PMID: 34387600.
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Loss of Hs3st3a1 or Hs3st3b1 enzymes alters heparan sulfate to reduce epithelial morphogenesis and adult salivary gland function.

Matrix biology : journal of the International Society for Matrix Biology

Patel VN, Pineda DL, Berenstein E, Hauser BR, Choi S, Prochazkova M, Zheng C, Goldsmith CM, van Kuppevelt TH, Kulkarni A, Song Y, Linhardt RJ, Chibly AM, Hoffman MP.
PMID: 34653670
Matrix Biol. 2021 Sep;103:37-57. doi: 10.1016/j.matbio.2021.10.002. Epub 2021 Oct 12.

Heparan sulfate 3-O-sulfotransferases generate highly sulfated but rare 3-O-sulfated heparan sulfate (HS) epitopes on cell surfaces and in the extracellular matrix. Previous ex vivo experiments suggested functional redundancy exists among the family of seven enzymes but that Hs3st3a1 and...

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Patel VN, Pineda DL, Berenstein E, et al. Loss of Hs3st3a1 or Hs3st3b1 enzymes alters heparan sulfate to reduce epithelial morphogenesis and adult salivary gland function. Matrix Biol. 2021;103:37-57doi: 10.1016/j.matbio.2021.10.002.
Patel, V. N., Pineda, D. L., Berenstein, E., Hauser, B. R., Choi, S., Prochazkova, M., Zheng, C., Goldsmith, C. M., van Kuppevelt, T. H., Kulkarni, A., Song, Y., Linhardt, R. J., Chibly, A. M., & Hoffman, M. P. (2021). Loss of Hs3st3a1 or Hs3st3b1 enzymes alters heparan sulfate to reduce epithelial morphogenesis and adult salivary gland function. Matrix biology : journal of the International Society for Matrix Biology, 10337-57. https://doi.org/10.1016/j.matbio.2021.10.002
Patel, Vaishali N, et al. "Loss of Hs3st3a1 or Hs3st3b1 enzymes alters heparan sulfate to reduce epithelial morphogenesis and adult salivary gland function." Matrix biology : journal of the International Society for Matrix Biology vol. 103 (2021): 37-57. doi: https://doi.org/10.1016/j.matbio.2021.10.002
Patel VN, Pineda DL, Berenstein E, Hauser BR, Choi S, Prochazkova M, Zheng C, Goldsmith CM, van Kuppevelt TH, Kulkarni A, Song Y, Linhardt RJ, Chibly AM, Hoffman MP. Loss of Hs3st3a1 or Hs3st3b1 enzymes alters heparan sulfate to reduce epithelial morphogenesis and adult salivary gland function. Matrix Biol. 2021 Sep;103:37-57. doi: 10.1016/j.matbio.2021.10.002. Epub 2021 Oct 12. PMID: 34653670; PMCID: PMC8629026.
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Ocular metabolism and distribution of drugs in the rabbit eye: Quantitative assessment after intracameral and intravitreal administrations.

International journal of pharmaceutics

Del Amo EM, Hammid A, Tausch M, Toropainen E, Sadeghi A, Valtari A, Puranen J, Reinisalo M, Ruponen M, Urtti A, Sauer A, Honkakoski P.
PMID: 34896561
Int J Pharm. 2021 Dec 09;613:121361. doi: 10.1016/j.ijpharm.2021.121361. Epub 2021 Dec 09.

Quantitation of ocular drug metabolism is important, but only sparse data is currently available. Herein, the pharmacokinetics of four drugs, substrates of metabolizing enzymes, was investigated in albino rabbit eyes after intracameral and intravitreal administrations. Acetaminophen, brimonidine, cefuroxime axetil,...

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Del Amo EM, Hammid A, Tausch M, et al. Ocular metabolism and distribution of drugs in the rabbit eye: Quantitative assessment after intracameral and intravitreal administrations. Int J Pharm. 2021;613:121361doi: 10.1016/j.ijpharm.2021.121361.
Del Amo, E. M., Hammid, A., Tausch, M., Toropainen, E., Sadeghi, A., Valtari, A., Puranen, J., Reinisalo, M., Ruponen, M., Urtti, A., Sauer, A., & Honkakoski, P. (2021). Ocular metabolism and distribution of drugs in the rabbit eye: Quantitative assessment after intracameral and intravitreal administrations. International journal of pharmaceutics, 613121361. https://doi.org/10.1016/j.ijpharm.2021.121361
Del Amo, Eva M, et al. "Ocular metabolism and distribution of drugs in the rabbit eye: Quantitative assessment after intracameral and intravitreal administrations." International journal of pharmaceutics vol. 613 (2021): 121361. doi: https://doi.org/10.1016/j.ijpharm.2021.121361
Del Amo EM, Hammid A, Tausch M, Toropainen E, Sadeghi A, Valtari A, Puranen J, Reinisalo M, Ruponen M, Urtti A, Sauer A, Honkakoski P. Ocular metabolism and distribution of drugs in the rabbit eye: Quantitative assessment after intracameral and intravitreal administrations. Int J Pharm. 2021 Dec 09;613:121361. doi: 10.1016/j.ijpharm.2021.121361. Epub 2021 Dec 09. PMID: 34896561.
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Congenital Disorders of Deficiency in Glycosaminoglycan Biosynthesis.

Frontiers in genetics

Mizumoto S, Yamada S.
PMID: 34539746
Front Genet. 2021 Sep 03;12:717535. doi: 10.3389/fgene.2021.717535. eCollection 2021.

Glycosaminoglycans (GAGs) including chondroitin sulfate, dermatan sulfate, and heparan sulfate are covalently attached to specific core proteins to form proteoglycans, which are distributed at the cell surface as well as in the extracellular matrix. Proteoglycans and GAGs have been...

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Mizumoto S, Yamada S. Congenital Disorders of Deficiency in Glycosaminoglycan Biosynthesis. Front Genet. 2021;12:717535doi: 10.3389/fgene.2021.717535.
Mizumoto, S., & Yamada, S. (2021). Congenital Disorders of Deficiency in Glycosaminoglycan Biosynthesis. Frontiers in genetics, 12717535. https://doi.org/10.3389/fgene.2021.717535
Mizumoto, Shuji, and Yamada, Shuhei. "Congenital Disorders of Deficiency in Glycosaminoglycan Biosynthesis." Frontiers in genetics vol. 12 (2021): 717535. doi: https://doi.org/10.3389/fgene.2021.717535
Mizumoto S, Yamada S. Congenital Disorders of Deficiency in Glycosaminoglycan Biosynthesis. Front Genet. 2021 Sep 03;12:717535. doi: 10.3389/fgene.2021.717535. eCollection 2021. PMID: 34539746; PMCID: PMC8446454.
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Echinacoside alleviates acetaminophen-induced liver injury by attenuating oxidative stress and inflammatory cytokines in mice.

Journal of applied biomedicine

Thida M, Li B, Zhang X, Chen C, Zhang X.
PMID: 34907710
J Appl Biomed. 2021 May;19(2):105-112. doi: 10.32725/jab.2021.011. Epub 2021 Apr 26.

This study evaluates the protective effect of Echinacoside on acute liver toxicity induced by acetaminophen in mice and the mechanism behind it. Echinacoside and N-Acetyl Cysteine were intragastrically administrated for 7 days, and acetaminophen was intraperitoneally injected into mice...

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Thida M, Li B, Zhang X, et al. Echinacoside alleviates acetaminophen-induced liver injury by attenuating oxidative stress and inflammatory cytokines in mice. J Appl Biomed. 2021;19(2):105-112doi: 10.32725/jab.2021.011.
Thida, M., Li, B., Zhang, X., Chen, C., & Zhang, X. (2021). Echinacoside alleviates acetaminophen-induced liver injury by attenuating oxidative stress and inflammatory cytokines in mice. Journal of applied biomedicine, 19(2), 105-112. https://doi.org/10.32725/jab.2021.011
Thida, Mya, et al. "Echinacoside alleviates acetaminophen-induced liver injury by attenuating oxidative stress and inflammatory cytokines in mice." Journal of applied biomedicine vol. 19,2 (2021): 105-112. doi: https://doi.org/10.32725/jab.2021.011
Thida M, Li B, Zhang X, Chen C, Zhang X. Echinacoside alleviates acetaminophen-induced liver injury by attenuating oxidative stress and inflammatory cytokines in mice. J Appl Biomed. 2021 May;19(2):105-112. doi: 10.32725/jab.2021.011. Epub 2021 Apr 26. PMID: 34907710.
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