View source for SULT1A1

{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox gene}}
'''Sulfotransferase 1A1''' is an [[enzyme]] that in humans is encoded by the ''SULT1A1'' [[gene]].<ref name="pmid8288252">{{cite journal | vauthors = Dooley TP, Obermoeller RD, Leiter EH, Chapman HD, Falany CN, Deng Z, Siciliano MJ | title = Mapping of the phenol sulfotransferase gene (STP) to human chromosome 16p12.1-p11.2 and to mouse chromosome 7 | journal = Genomics | volume = 18 | issue = 2 | pages = 440–3 | date = November 1993 | pmid = 8288252 | doi = 10.1006/geno.1993.1494 }}</ref><ref name="pmid8912648">{{cite journal | vauthors = Dooley TP, Huang Z | title = Genomic organization and DNA sequences of two human phenol sulfotransferase genes (STP1 and STP2) on the short arm of chromosome 16 | journal = Biochemical and Biophysical Research Communications | volume = 228 | issue = 1 | pages = 134–40 | date = November 1996 | pmid = 8912648 | doi = 10.1006/bbrc.1996.1628 }}</ref><ref name="entrez">{{cite web | title = SULT1A1 sulfotransferase family 1A member 1 [ Homo sapiens (human) ]| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6817}}</ref>
[[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 [[alternative splicing|alternatively spliced variants]] that encode two isoforms have been identified for this gene.<ref name="entrez"/>
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).<ref name="pmid31184104">{{cite journal | vauthors = McCoy J, Goren A, Naccarato T, Kovacevic M, Situm M, Skudar VL, Lotti T | title = Identification of the sulfotransferase iso-enzyme primarily responsible for the bio-activation of topical minoxidil | journal = Journal of Biological Regulators and Homeostatic Agents | volume = 33 | issue = 3 | pages = 817–819 | date = 2019 | pmid = 31184104 }}</ref> 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.<ref name="pmid25112173">{{cite journal | vauthors = Goren A, Shapiro J, Roberts J, McCoy J, Desai N, Zarrab Z, Pietrzak A, Lotti T | display-authors = 6 | title = Clinical utility and validity of minoxidil response testing in androgenetic alopecia | journal = Dermatologic Therapy | volume = 28 | issue = 1 | pages = 13–6 | date = 2015 | pmid = 25112173 | doi = 10.1111/dth.12164 | s2cid = 205082682 | doi-access = free }}</ref> In a clinical study, a novel formula using a hypoxia mimetic pathway demonstrated to increase SULT1A1 activity in human subjects in-vivo.<ref name="pmid32432358">{{cite journal | vauthors = Ramos PM, McCoy J, Wambier C, Shapiro J, Vañó-Galvan S, Sinclair R, Goren A | title = Novel topical booster enhances follicular sulfotransferase activity in patients with androgenetic alopecia: a new strategy to improve minoxidil response | journal = Journal of the European Academy of Dermatology and Venereology | date = May 2020 | volume = 34 | issue = 12 | pages = e799–e800 | pmid = 32432358 | doi = 10.1111/jdv.16645 | hdl = 11343/278544 | s2cid = 218755089 | hdl-access = free }}</ref>
== See also ==
* [[Steroid sulfotransferase]]
* [[Steroidogenic enzyme]]
== References ==
{{reflist}}
== Further reading ==
{{refbegin | 2}}
* {{cite journal | vauthors = Weinshilboum RM, Otterness DM, Aksoy IA, Wood TC, Her C, Raftogianis RB | title = Sulfation and sulfotransferases 1: Sulfotransferase molecular biology: cDNAs and genes | journal = FASEB Journal | volume = 11 | issue = 1 | pages = 3–14 | date = January 1997 | pmid = 9034160 | doi = 10.1096/fasebj.11.1.9034160 | doi-access = free | s2cid = 12532583 }}
* {{cite journal | vauthors = Windmill KF, Christiansen A, Teusner JT, Bhasker CR, Birkett DJ, Zhu X, McManus ME | title = Localisation of aryl sulfotransferase expression in human tissues using hybridisation histochemistry and immunohistochemistry | journal = Chemico-Biological Interactions | volume = 109 | issue = 1–3 | pages = 341–6 | date = February 1998 | pmid = 9566757 | doi = 10.1016/S0009-2797(97)00144-0 | bibcode = 1998CBI...109..341W | url = http://espace.library.uq.edu.au/view/UQ:34748/UQ_AV_34748.pdf }}
* {{cite journal | vauthors = Glatt H, Engelke CE, Pabel U, Teubner W, Jones AL, Coughtrie MW, Andrae U, Falany CN, Meinl W | display-authors = 6 | title = Sulfotransferases: genetics and role in toxicology | journal = Toxicology Letters | volume = 112-113 | pages = 341–8 | date = March 2000 | pmid = 10720750 | doi = 10.1016/S0378-4274(99)00214-3 }}
* {{cite journal | vauthors = Glatt H | title = Sulfotransferases in the bioactivation of xenobiotics | journal = Chemico-Biological Interactions | volume = 129 | issue = 1–2 | pages = 141–70 | date = December 2000 | pmid = 11154739 | doi = 10.1016/S0009-2797(00)00202-7 | bibcode = 2000CBI...129..141G }}
* {{cite journal | vauthors = Glatt H, Boeing H, Engelke CE, Ma L, Kuhlow A, Pabel U, Pomplun D, Teubner W, Meinl W | display-authors = 6 | title = Human cytosolic sulphotransferases: genetics, characteristics, toxicological aspects | journal = Mutation Research | volume = 482 | issue = 1–2 | pages = 27–40 | date = October 2001 | pmid = 11535246 | doi = 10.1016/S0027-5107(01)00207-X }}
* {{cite journal | vauthors = Ozawa S, Nagata K, Shimada M, Ueda M, Tsuzuki T, Yamazoe Y, Kato R | title = Primary structures and properties of two related forms of aryl sulfotransferases in human liver | journal = Pharmacogenetics | volume = 5 Spec No | pages = S135-40 | year = 1995 | pmid = 7581483 | doi = 10.1097/00008571-199512001-00015 }}
* {{cite journal | vauthors = Jones AL, Hagen M, Coughtrie MW, Roberts RC, Glatt H | title = Human platelet phenolsulfotransferases: cDNA cloning, stable expression in V79 cells and identification of a novel allelic variant of the phenol-sulfating form | journal = Biochemical and Biophysical Research Communications | volume = 208 | issue = 2 | pages = 855–62 | date = March 1995 | pmid = 7695643 | doi = 10.1006/bbrc.1995.1414 }}
* {{cite journal | vauthors = Hwang SR, Kohn AB, Hook VY | title = Molecular cloning of an isoform of phenol sulfotransferase from human brain hippocampus | journal = Biochemical and Biophysical Research Communications | volume = 207 | issue = 2 | pages = 701–7 | date = February 1995 | pmid = 7864863 | doi = 10.1006/bbrc.1995.1244 }}
* {{cite journal | vauthors = Yamazoe Y, Nagata K, Ozawa S, Kato R | title = Structural similarity and diversity of sulfotransferases | journal = Chemico-Biological Interactions | volume = 92 | issue = 1–3 | pages = 107–17 | date = June 1994 | pmid = 8033246 | doi = 10.1016/0009-2797(94)90057-4 | bibcode = 1994CBI....92..107Y }}
* {{cite journal | vauthors = Falany CN, Zhuang W, Falany JL | title = Characterization of expressed human phenol-sulfating phenol sulfotransferase: effect of mutating cys70 on activity and thermostability | journal = Chemico-Biological Interactions | volume = 92 | issue = 1–3 | pages = 57–66 | date = June 1994 | pmid = 8033270 | doi = 10.1016/0009-2797(94)90053-1 }}
* {{cite journal | vauthors = Veronese ME, Burgess W, Zhu X, McManus ME | title = 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 | journal = The Biochemical Journal | volume = 302 ( Pt 2) | issue = 2 | pages = 497–502 | date = September 1994 | pmid = 8093002 | pmc = 1137255 | doi = 10.1042/bj3020497 }}
* {{cite journal | vauthors = Zhu X, Veronese ME, Bernard CC, Sansom LN, McManus ME | title = Identification of two human brain aryl sulfotransferase cDNAs | journal = Biochemical and Biophysical Research Communications | volume = 195 | issue = 1 | pages = 120–7 | date = August 1993 | pmid = 8363592 | doi = 10.1006/bbrc.1993.2018 }}
* {{cite journal | vauthors = Wilborn TW, Comer KA, Dooley TP, Reardon IM, Heinrikson RL, Falany CN | title = Sequence analysis and expression of the cDNA for the phenol-sulfating form of human liver phenol sulfotransferase | journal = Molecular Pharmacology | volume = 43 | issue = 1 | pages = 70–7 | date = January 1993 | pmid = 8423770 }}
* {{cite journal | vauthors = Zhu X, Veronese ME, Sansom LN, McManus ME | title = Molecular characterisation of a human aryl sulfotransferase cDNA | journal = Biochemical and Biophysical Research Communications | volume = 192 | issue = 2 | pages = 671–6 | date = April 1993 | pmid = 8484775 | doi = 10.1006/bbrc.1993.1467 }}
* {{cite journal | vauthors = Her C, Raftogianis R, Weinshilboum RM | title = Human phenol sulfotransferase STP2 gene: molecular cloning, structural characterization, and chromosomal localization | journal = Genomics | volume = 33 | issue = 3 | pages = 409–20 | date = May 1996 | pmid = 8661000 | doi = 10.1006/geno.1996.0216 }}
* {{cite journal | vauthors = Bernier F, Soucy P, Luu-The V | title = Human phenol sulfotransferase gene contains two alternative promoters: Structure and expression of the gene | journal = DNA and Cell Biology | volume = 15 | issue = 5 | pages = 367–75 | date = May 1996 | pmid = 8924211 | doi = 10.1089/dna.1996.15.367 }}
* {{cite journal | vauthors = Raftogianis RB, Her C, Weinshilboum RM | title = Human phenol sulfotransferase pharmacogenetics: STP1 gene cloning and structural characterization | journal = Pharmacogenetics | volume = 6 | issue = 6 | pages = 473–87 | date = December 1996 | pmid = 9014197 | doi = 10.1097/00008571-199612000-00001 }}
{{refend}}
{{PDB Gallery|geneid=6817}}
{{Cholesterol and steroid metabolism enzymes}}
{{gene-16-stub}}