Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. This gene encodes one of two phenol sulfotransferases with thermostable enzyme activity. Multiple alternatively spliced variants that encode two isoforms have been identified for this gene.[5]
The SULT1A1 enzyme is expressed in outer roots sheath of hair follicles. Minoxidil, the only US FDA approved topical drug for re-growing hair in male and female pattern hair loss (androgenetic alopecia patients) is a pro-drug. Minoxidil is converted to its active form (minoxidil sulfate) by the hair sulfotransferase enzyme (SULT1A1).[6] A large variability in sulfotransferase enzyme expression in hair is observed among people. Low sulfotransferase activity was found to be predictive to lack of response to topical minoxidil for hair re-growth.[7] In a clinical study, a novel formula using a hypoxia mimetic pathway demonstrated to increase SULT1A1 activity in human subjects in-vivo.[8]
^ abcGRCh38: Ensembl release 89: ENSG00000196502 - Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Dooley TP, Obermoeller RD, Leiter EH, Chapman HD, Falany CN, Deng Z, Siciliano MJ (November 1993). "Mapping of the phenol sulfotransferase gene (STP) to human chromosome 16p12.1-p11.2 and to mouse chromosome 7". Genomics. 18 (2): 440–3. doi:10.1006/geno.1993.1494. PMID 8288252.
^Dooley TP, Huang Z (November 1996). "Genomic organization and DNA sequences of two human phenol sulfotransferase genes (STP1 and STP2) on the short arm of chromosome 16". Biochemical and Biophysical Research Communications. 228 (1): 134–40. doi:10.1006/bbrc.1996.1628. PMID 8912648.
^ ab"SULT1A1 sulfotransferase family 1A member 1 [ Homo sapiens (human) ]".
^McCoy J, Goren A, Naccarato T, Kovacevic M, Situm M, Skudar VL, Lotti T (2019). "Identification of the sulfotransferase iso-enzyme primarily responsible for the bio-activation of topical minoxidil". Journal of Biological Regulators and Homeostatic Agents. 33 (3): 817–819. PMID 31184104.
^Goren A, Shapiro J, Roberts J, McCoy J, Desai N, Zarrab Z, et al. (2015). "Clinical utility and validity of minoxidil response testing in androgenetic alopecia". Dermatologic Therapy. 28 (1): 13–6. doi:10.1111/dth.12164. PMID 25112173. S2CID 205082682.
^Ramos PM, McCoy J, Wambier C, Shapiro J, Vañó-Galvan S, Sinclair R, Goren A (May 2020). "Novel topical booster enhances follicular sulfotransferase activity in patients with androgenetic alopecia: a new strategy to improve minoxidil response". Journal of the European Academy of Dermatology and Venereology. 34 (12): e799–e800. doi:10.1111/jdv.16645. hdl:11343/278544. PMID 32432358. S2CID 218755089.
Windmill KF, Christiansen A, Teusner JT, Bhasker CR, Birkett DJ, Zhu X, McManus ME (February 1998). "Localisation of aryl sulfotransferase expression in human tissues using hybridisation histochemistry and immunohistochemistry" (PDF). Chemico-Biological Interactions. 109 (1–3): 341–6. doi:10.1016/S0009-2797(97)00144-0. PMID 9566757.
Glatt H, Engelke CE, Pabel U, Teubner W, Jones AL, Coughtrie MW, et al. (March 2000). "Sulfotransferases: genetics and role in toxicology". Toxicology Letters. 112–113: 341–8. doi:10.1016/S0378-4274(99)00214-3. PMID 10720750.
Glatt H (December 2000). "Sulfotransferases in the bioactivation of xenobiotics". Chemico-Biological Interactions. 129 (1–2): 141–70. doi:10.1016/S0009-2797(00)00202-7. PMID 11154739.
Glatt H, Boeing H, Engelke CE, Ma L, Kuhlow A, Pabel U, et al. (October 2001). "Human cytosolic sulphotransferases: genetics, characteristics, toxicological aspects". Mutation Research. 482 (1–2): 27–40. doi:10.1016/S0027-5107(01)00207-X. PMID 11535246.
Ozawa S, Nagata K, Shimada M, Ueda M, Tsuzuki T, Yamazoe Y, Kato R (1995). "Primary structures and properties of two related forms of aryl sulfotransferases in human liver". Pharmacogenetics. 5 Spec No: S135-40. doi:10.1097/00008571-199512001-00015. PMID 7581483.
Jones AL, Hagen M, Coughtrie MW, Roberts RC, Glatt H (March 1995). "Human platelet phenolsulfotransferases: cDNA cloning, stable expression in V79 cells and identification of a novel allelic variant of the phenol-sulfating form". Biochemical and Biophysical Research Communications. 208 (2): 855–62. doi:10.1006/bbrc.1995.1414. PMID 7695643.
Hwang SR, Kohn AB, Hook VY (February 1995). "Molecular cloning of an isoform of phenol sulfotransferase from human brain hippocampus". Biochemical and Biophysical Research Communications. 207 (2): 701–7. doi:10.1006/bbrc.1995.1244. PMID 7864863.
Yamazoe Y, Nagata K, Ozawa S, Kato R (June 1994). "Structural similarity and diversity of sulfotransferases". Chemico-Biological Interactions. 92 (1–3): 107–17. doi:10.1016/0009-2797(94)90057-4. PMID 8033246.
Falany CN, Zhuang W, Falany JL (June 1994). "Characterization of expressed human phenol-sulfating phenol sulfotransferase: effect of mutating cys70 on activity and thermostability". Chemico-Biological Interactions. 92 (1–3): 57–66. doi:10.1016/0009-2797(94)90053-1. PMID 8033270.
Veronese ME, Burgess W, Zhu X, McManus ME (September 1994). "Functional characterization of two human sulphotransferase cDNAs that encode monoamine- and phenol-sulphating forms of phenol sulphotransferase: substrate kinetics, thermal-stability and inhibitor-sensitivity studies". The Biochemical Journal. 302 ( Pt 2) (2): 497–502. doi:10.1042/bj3020497. PMC1137255. PMID 8093002.
Zhu X, Veronese ME, Bernard CC, Sansom LN, McManus ME (August 1993). "Identification of two human brain aryl sulfotransferase cDNAs". Biochemical and Biophysical Research Communications. 195 (1): 120–7. doi:10.1006/bbrc.1993.2018. PMID 8363592.
Wilborn TW, Comer KA, Dooley TP, Reardon IM, Heinrikson RL, Falany CN (January 1993). "Sequence analysis and expression of the cDNA for the phenol-sulfating form of human liver phenol sulfotransferase". Molecular Pharmacology. 43 (1): 70–7. PMID 8423770.
Zhu X, Veronese ME, Sansom LN, McManus ME (April 1993). "Molecular characterisation of a human aryl sulfotransferase cDNA". Biochemical and Biophysical Research Communications. 192 (2): 671–6. doi:10.1006/bbrc.1993.1467. PMID 8484775.
Bernier F, Soucy P, Luu-The V (May 1996). "Human phenol sulfotransferase gene contains two alternative promoters: Structure and expression of the gene". DNA and Cell Biology. 15 (5): 367–75. doi:10.1089/dna.1996.15.367. PMID 8924211.
sult1a1, sulfotransferase, enzyme, that, humans, encoded, gene, available, structurespdbhuman, uniprot, search, pdbe, rcsblist, codes1ls6, 1z28, 2d06, 3qvu, 3qvv, 3u3j, 3u3k, 3u3m, 3u3o, 3u3r, 4graidentifiersaliases, hast1, hast2, st1a1, st1a3, stp1, tspst1, s. Sulfotransferase 1A1 is an enzyme that in humans is encoded by the SULT1A1 gene 3 4 5 SULT1A1Available structuresPDBHuman UniProt search PDBe RCSBList of PDB id codes1LS6 1Z28 2D06 3QVU 3QVV 3U3J 3U3K 3U3M 3U3O 3U3R 4GRAIdentifiersAliasesSULT1A1 HAST1 HAST2 P PST PST ST1A1 ST1A3 STP STP1 TSPST1 sulfotransferase family 1A member 1 ts PST P PST 1External IDsOMIM 171150 HomoloGene 134950 GeneCards SULT1A1Gene location Human Chr Chromosome 16 human 1 Band16p11 2Start28 603 944 bp 1 End28 623 625 bp 1 RNA expression patternBgeeHumanMouse ortholog Top expressed inright lobe of liverleft adrenal glandmonocyterectumright lobe of thyroid glandright lungspleenleft lobe of thyroid glandupper lobe of left lunganterior pituitaryn aMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functiontransferase activity sulfotransferase activity steroid sulfotransferase activity flavonol 3 sulfotransferase activity protein binding aryl sulfotransferase activityCellular componentcytoplasm cytosolBiological processsteroid metabolic process amine metabolic process catecholamine metabolic process estrogen metabolic process sulfation lipid metabolism flavonoid metabolic process xenobiotic metabolic process ethanol catabolic process 3 phosphoadenosine 5 phosphosulfate metabolic processSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez6817n aEnsemblENSG00000196502n aUniProtP50225n aRefSeq mRNA NM 177536NM 001055NM 177529NM 177530NM 177534NM 001394421NM 001394422NM 001394423NM 001394424NM 001394425n aRefSeq protein NP 001046NP 803565NP 803566NP 803878NP 803880n aLocation UCSC Chr 16 28 6 28 62 Mbn aPubMed search 2 n aWikidataView Edit HumanSulfotransferase enzymes catalyze the sulfate conjugation of many hormones neurotransmitters drugs and xenobiotic compounds These cytosolic enzymes are different in their tissue distributions and substrate specificities The gene structure number and length of exons is similar among family members This gene encodes one of two phenol sulfotransferases with thermostable enzyme activity Multiple alternatively spliced variants that encode two isoforms have been identified for this gene 5 The SULT1A1 enzyme is expressed in outer roots sheath of hair follicles Minoxidil the only US FDA approved topical drug for re growing hair in male and female pattern hair loss androgenetic alopecia patients is a pro drug Minoxidil is converted to its active form minoxidil sulfate by the hair sulfotransferase enzyme SULT1A1 6 A large variability in sulfotransferase enzyme expression in hair is observed among people Low sulfotransferase activity was found to be predictive to lack of response to topical minoxidil for hair re growth 7 In a clinical study a novel formula using a hypoxia mimetic pathway demonstrated to increase SULT1A1 activity in human subjects in vivo 8 See also editSteroid sulfotransferase Steroidogenic enzymeReferences edit a b c GRCh38 Ensembl release 89 ENSG00000196502 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Dooley TP Obermoeller RD Leiter EH Chapman HD Falany CN Deng Z Siciliano MJ November 1993 Mapping of the phenol sulfotransferase gene STP to human chromosome 16p12 1 p11 2 and to mouse chromosome 7 Genomics 18 2 440 3 doi 10 1006 geno 1993 1494 PMID 8288252 Dooley TP Huang Z November 1996 Genomic organization and DNA sequences of two human phenol sulfotransferase genes STP1 and STP2 on the short arm of chromosome 16 Biochemical and Biophysical Research Communications 228 1 134 40 doi 10 1006 bbrc 1996 1628 PMID 8912648 a b SULT1A1 sulfotransferase family 1A member 1 Homo sapiens human McCoy J Goren A Naccarato T Kovacevic M Situm M Skudar VL Lotti T 2019 Identification of the sulfotransferase iso enzyme primarily responsible for the bio activation of topical minoxidil Journal of Biological Regulators and Homeostatic Agents 33 3 817 819 PMID 31184104 Goren A Shapiro J Roberts J McCoy J Desai N Zarrab Z et al 2015 Clinical utility and validity of minoxidil response testing in androgenetic alopecia Dermatologic Therapy 28 1 13 6 doi 10 1111 dth 12164 PMID 25112173 S2CID 205082682 Ramos PM McCoy J Wambier C Shapiro J Vano Galvan S Sinclair R Goren A May 2020 Novel topical booster enhances follicular sulfotransferase activity in patients with androgenetic alopecia a new strategy to improve minoxidil response Journal of the European Academy of Dermatology and Venereology 34 12 e799 e800 doi 10 1111 jdv 16645 hdl 11343 278544 PMID 32432358 S2CID 218755089 Further reading editWeinshilboum RM Otterness DM Aksoy IA Wood TC Her C Raftogianis RB January 1997 Sulfation and sulfotransferases 1 Sulfotransferase molecular biology cDNAs and genes FASEB Journal 11 1 3 14 doi 10 1096 fasebj 11 1 9034160 PMID 9034160 S2CID 12532583 Windmill KF Christiansen A Teusner JT Bhasker CR Birkett DJ Zhu X McManus ME February 1998 Localisation of aryl sulfotransferase expression in human tissues using hybridisation histochemistry and immunohistochemistry PDF Chemico Biological Interactions 109 1 3 341 6 doi 10 1016 S0009 2797 97 00144 0 PMID 9566757 Glatt H Engelke CE Pabel U Teubner W Jones AL Coughtrie MW et al March 2000 Sulfotransferases genetics and role in toxicology Toxicology Letters 112 113 341 8 doi 10 1016 S0378 4274 99 00214 3 PMID 10720750 Glatt H December 2000 Sulfotransferases in the bioactivation of xenobiotics Chemico Biological Interactions 129 1 2 141 70 doi 10 1016 S0009 2797 00 00202 7 PMID 11154739 Glatt H Boeing H Engelke CE Ma L Kuhlow A Pabel U et al October 2001 Human cytosolic sulphotransferases genetics characteristics toxicological aspects Mutation Research 482 1 2 27 40 doi 10 1016 S0027 5107 01 00207 X PMID 11535246 Ozawa S Nagata K Shimada M Ueda M Tsuzuki T Yamazoe Y Kato R 1995 Primary structures and properties of two related forms of aryl sulfotransferases in human liver Pharmacogenetics 5 Spec No S135 40 doi 10 1097 00008571 199512001 00015 PMID 7581483 Jones AL Hagen M Coughtrie MW Roberts RC Glatt H March 1995 Human platelet phenolsulfotransferases cDNA cloning stable expression in V79 cells and identification of a novel allelic variant of the phenol sulfating form Biochemical and Biophysical Research Communications 208 2 855 62 doi 10 1006 bbrc 1995 1414 PMID 7695643 Hwang SR Kohn AB Hook VY February 1995 Molecular cloning of an isoform of phenol sulfotransferase from human brain hippocampus Biochemical and Biophysical Research Communications 207 2 701 7 doi 10 1006 bbrc 1995 1244 PMID 7864863 Yamazoe Y Nagata K Ozawa S Kato R June 1994 Structural similarity and diversity of sulfotransferases Chemico Biological Interactions 92 1 3 107 17 doi 10 1016 0009 2797 94 90057 4 PMID 8033246 Falany CN Zhuang W Falany JL June 1994 Characterization of expressed human phenol sulfating phenol sulfotransferase effect of mutating cys70 on activity and thermostability Chemico Biological Interactions 92 1 3 57 66 doi 10 1016 0009 2797 94 90053 1 PMID 8033270 Veronese ME Burgess W Zhu X McManus ME September 1994 Functional characterization of two human sulphotransferase cDNAs that encode monoamine and phenol sulphating forms of phenol sulphotransferase substrate kinetics thermal stability and inhibitor sensitivity studies The Biochemical Journal 302 Pt 2 2 497 502 doi 10 1042 bj3020497 PMC 1137255 PMID 8093002 Zhu X Veronese ME Bernard CC Sansom LN McManus ME August 1993 Identification of two human brain aryl sulfotransferase cDNAs Biochemical and Biophysical Research Communications 195 1 120 7 doi 10 1006 bbrc 1993 2018 PMID 8363592 Wilborn TW Comer KA Dooley TP Reardon IM Heinrikson RL Falany CN January 1993 Sequence analysis and expression of the cDNA for the phenol sulfating form of human liver phenol sulfotransferase Molecular Pharmacology 43 1 70 7 PMID 8423770 Zhu X Veronese ME Sansom LN McManus ME April 1993 Molecular characterisation of a human aryl sulfotransferase cDNA Biochemical and Biophysical Research Communications 192 2 671 6 doi 10 1006 bbrc 1993 1467 PMID 8484775 Her C Raftogianis R Weinshilboum RM May 1996 Human phenol sulfotransferase STP2 gene molecular cloning structural characterization and chromosomal localization Genomics 33 3 409 20 doi 10 1006 geno 1996 0216 PMID 8661000 Bernier F Soucy P Luu The V May 1996 Human phenol sulfotransferase gene contains two alternative promoters Structure and expression of the gene DNA and Cell Biology 15 5 367 75 doi 10 1089 dna 1996 15 367 PMID 8924211 Raftogianis RB Her C Weinshilboum RM December 1996 Human phenol sulfotransferase pharmacogenetics STP1 gene cloning and structural characterization Pharmacogenetics 6 6 473 87 doi 10 1097 00008571 199612000 00001 PMID 9014197 nbsp This article on a gene on human chromosome 16 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title SULT1A1 amp oldid 1136356353, wikipedia, wiki, book, books, library,
