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Article ; Online: Enzymatic activation in vitamin D signaling - Past, present and future.

Norlin, Maria / Wikvall, Kjell

2023 Volume 742, Page(s) 109639

Abstract: Vitamin D signaling is important in regulating calcium homeostasis essential for bone health but also displays other functions in cells of several tissues. Disturbed vitamin D signaling is linked to a large number of diseases. The multiple cytochrome ... ...

Abstract	Vitamin D signaling is important in regulating calcium homeostasis essential for bone health but also displays other functions in cells of several tissues. Disturbed vitamin D signaling is linked to a large number of diseases. The multiple cytochrome P450 (CYP) enzymes catalyzing the different hydroxylations in bioactivation of vitamin D
MeSH term(s)	Vitamin D ; Vitamins ; Cytochrome P-450 Enzyme System/metabolism ; Substrate Specificity ; Hydroxylation
Chemical Substances	Vitamin D (1406-16-2) ; Vitamins ; Cytochrome P-450 Enzyme System (9035-51-2)
Language	English
Publishing date	2023-05-18
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2023.109639
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Article ; Online: Effects of vitamin D in the nervous system: Special focus on interaction with steroid hormone signalling and a possible role in the treatment of brain cancer.

Norlin, Maria

Journal of neuroendocrinology

2019 Volume 32, Issue 1, Page(s) e12799

Abstract: The active vitamin D hormone, 1,25-dihydroxyvitamin ... ...

Abstract	The active vitamin D hormone, 1,25-dihydroxyvitamin D
MeSH term(s)	Astrocytes/metabolism ; Brain/metabolism ; Brain Neoplasms/metabolism ; Gonadal Steroid Hormones/metabolism ; Humans ; Neurons/metabolism ; Receptors, Calcitriol/metabolism ; Signal Transduction/physiology ; Vitamin D/metabolism
Chemical Substances	Gonadal Steroid Hormones ; Receptors, Calcitriol ; Vitamin D (1406-16-2)
Language	English
Publishing date	2019-10-23
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1007517-3
ISSN	1365-2826 ; 0953-8194
ISSN (online)	1365-2826
ISSN	0953-8194
DOI	10.1111/jne.12799
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Article ; Online: Enzymatic activation in vitamin D signaling - Past, present and future

Norlin, Maria / Wikvall, Kjell

Archives of Biochemistry and Biophysics. 2023 July, v. 742 p.109639-

2023

Abstract	Vitamin D signaling is important in regulating calcium homeostasis essential for bone health but also displays other functions in cells of several tissues. Disturbed vitamin D signaling is linked to a large number of diseases. The multiple cytochrome P450 (CYP) enzymes catalyzing the different hydroxylations in bioactivation of vitamin D₃ are crucial for vitamin D signaling and function. This review is focused on the progress achieved in identification of the bioactivating enzymes and their genes in production of 1α,25-dihydroxyvitamin D₃ and other active metabolites. Results obtained on species- and tissue-specific expression, catalytic reactions, substrate specificity, enzyme kinetics, and consequences of gene mutations are evaluated. Matters of incomplete understanding regarding the physiological roles of some vitamin D hydroxylases are critically discussed and the authors will give their view of the importance of each enzyme for vitamin D signaling. Roles of different vitamin D receptors and an alternative bioactivation pathway, leading to 20-hydroxylated vitamin D₃ metabolites, are also discussed. Considerable progress has been achieved in knowledge of the vitamin D₃ bioactivating enzymes. Nevertheless, several intriguing areas deserve further attention to understand the pleiotropic and diverse activities elicited by vitamin D signaling and the mechanisms of enzymatic activation necessary for vitamin D-induced responses.
Keywords	biophysics ; bone health ; calcium ; cytochrome P-450 ; enzyme kinetics ; enzymes ; genes ; homeostasis ; metabolites ; substrate specificity ; Vitamin D bioactivation ; Vitamin D hydroxylase ; Cytochrome P450 ; CYP2R1 ; CYP27A1 ; CYP27B1 ; CTX ; CYP ; FGF23 ; MARRS ; PDIA3 ; PTH ; PVDR ; RXR ; VDDR ; VDR ; VDRE
Language	English
Dates of publication	2023-07
Publishing place	Elsevier Inc.
Document type	Article ; Online
Note	Use and reproduction
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2023.109639
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Article ; Online: Cellular responses to silencing of PDIA3 (protein disulphide-isomerase A3): Effects on proliferation, migration, and genes in control of active vitamin D.

Kermpatsou, Despoina / Olsson, Frida / Wåhlén, Erik / Söderberg, Ola / Lennartsson, Johan / Norlin, Maria

The Journal of steroid biochemistry and molecular biology

2024 Volume 240, Page(s) 106497

Abstract: The active form of vitamin D, 1,25-dihydroxyvitamin ... ...

Abstract	The active form of vitamin D, 1,25-dihydroxyvitamin D
Language	English
Publishing date	2024-03-07
Publishing country	England
Document type	Journal Article
ZDB-ID	1049188-0
ISSN	1879-1220 ; 0960-0760
ISSN (online)	1879-1220
ISSN	0960-0760
DOI	10.1016/j.jsbmb.2024.106497
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Article ; Online: Effects of 1α,25-dihydroxyvitamin D

Olsson, Frida / Sarri, Niki / Papadopoulos, Natalia / Lennartsson, Johan / Norlin, Maria

Biochemistry and biophysics reports

2022 Volume 31, Page(s) 101313

Abstract: The active hormonal form of vitamin D, 1α,25-dihydroxyvitamin ... ...

Abstract	The active hormonal form of vitamin D, 1α,25-dihydroxyvitamin D
Language	English
Publishing date	2022-07-31
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2831046-9
ISSN	2405-5808 ; 2405-5808
ISSN (online)	2405-5808
ISSN	2405-5808
DOI	10.1016/j.bbrep.2022.101313
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Article ; Online: Vitamin D Analogues Tacalcitol and Calcipotriol Inhibit Proliferation and Migration of T98G Human Glioblastoma Cells.

Emanuelsson, Ida / Wikvall, Kjell / Friman, Tomas / Norlin, Maria

Basic & clinical pharmacology & toxicology

2018 Volume 123, Issue 2, Page(s) 130–136

Abstract: The active form of vitamin D (1α,25-dihydroxyvitamin D) acts as a steroid hormone and binds to the vitamin D receptor. This receptor is expressed in most cell types including cells in the central nervous system (CNS). Vitamin D has several functions in ... ...

Abstract	The active form of vitamin D (1α,25-dihydroxyvitamin D) acts as a steroid hormone and binds to the vitamin D receptor. This receptor is expressed in most cell types including cells in the central nervous system (CNS). Vitamin D has several functions in the body including effects on brain development, neuroprotection and immunological regulation. It has been shown that vitamin D has antiproliferative activities in different cancer cell lines. Tacalcitol and calcipotriol are synthetic analogues of 1α,25-dihydroxyvitamin D with reduced effect on calcium metabolism. The aim of this study was to analyse the effects of tacalcitol and calcipotriol on cell viability, proliferation and migration in the human glioblastoma cell line T98G. Glioblastoma is the most lethal type of primary tumours in the CNS. Both analogues decreased cell viability and/or growth, dose-dependently, in concentrations between 1 nM and 10 μM. Manual counting indicated suppressive effects by the vitamin D analogues on proliferation. Treatment with tacalcitol strongly suppressed thymidine incorporation, indicating that the vitamin D analogues mainly inhibit proliferation. Also, effects on cell migration were measured with wound-healing assay. Both calcipotriol and tacalcitol reduced the migration rate of T98G cells compared to vehicle-treated cells. However, they had no effect on caspase-3 and -7 activities, suggesting that their mechanism of action does not involve induction of apoptosis. The current results indicate that the vitamin D analogues tacalcitol and calcipotriol strongly reduce proliferation and migration of human glioblastoma T98G cells, suggesting a potential role for this type of compounds in treatment of brain cancer.
MeSH term(s)	Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Calcitriol/analogs & derivatives ; Calcitriol/pharmacology ; Calcitriol/therapeutic use ; Cell Line, Tumor ; Cell Movement/drug effects ; Cell Proliferation/drug effects ; Cell Survival/drug effects ; Dihydroxycholecalciferols/pharmacology ; Dihydroxycholecalciferols/therapeutic use ; Drug Evaluation, Preclinical ; Glioblastoma/drug therapy ; Glioblastoma/pathology ; Humans ; Receptors, Calcitriol/metabolism
Chemical Substances	Antineoplastic Agents ; Dihydroxycholecalciferols ; Receptors, Calcitriol ; VDR protein, human ; calcipotriene (143NQ3779B) ; 1 alpha,24-dihydroxyvitamin D3 (60965-80-2) ; Calcitriol (FXC9231JVH)
Language	English
Publishing date	2018-04-25
Publishing country	England
Document type	Journal Article
ZDB-ID	2134679-3
ISSN	1742-7843 ; 1742-7835
ISSN (online)	1742-7843
ISSN	1742-7835
DOI	10.1111/bcpt.13007
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Article ; Online: Estrogen-mediated regulation of steroid metabolism in rat glial cells; effects on neurosteroid levels via regulation of CYP7B1-mediated catalysis.

Wicher, Grzegorz / Norlin, Maria

The Journal of steroid biochemistry and molecular biology

2014 Volume 145, Page(s) 21–27

Abstract: Many neuroactive steroids, including dehydroepiandrosterone (DHEA), pregnenolone, 27-hydroxycholesterol and 17β-estradiol, are known to affect development and function of the brain and nervous system. These and other steroids can undergo tissue and/or ... ...

Abstract	Many neuroactive steroids, including dehydroepiandrosterone (DHEA), pregnenolone, 27-hydroxycholesterol and 17β-estradiol, are known to affect development and function of the brain and nervous system. These and other steroids can undergo tissue and/or cell-specific enzymatic conversions into steroid metabolites. Carefully regulated production of steroids with various physiological effects is important for cells of the nervous system. Astrocytes express many steroidogenic enzymes and are considered important producers of brain steroids. The quantitative roles of different pathways for steroid metabolism in rat astrocytes are not clear. In the current study we examined effects of estrogens on steroid metabolism catalyzed by CYP7B1 and other enzymes in primary cultures of rat astrocytes. The CYP7B1 enzyme, which has been linked to neurodegenerative disease, is involved in the metabolism of several important neurosteroids. In the present study, we found that 7α-hydroxylation, performed by CYP7B1, is the quantitatively most important pathway for DHEA metabolism in rat astrocytes. In addition, our present experiments on catalytic steroid conversions revealed that estrogens significantly suppress the CYP7B1-catalyzed metabolism of not only DHEA but also of pregnenolone and 27-hydroxycholesterol in rat astrocytes. These novel findings point to a regulatory mechanism for control of the cellular levels of these neurosteroids via CYP7B1. Our hypothesis that estrogens can regulate neurosteroid levels via this enzymatic reaction was supported by experiments using ELISA to assay levels of DHEA and pregnenolone in the presence or absence of estrogen. Furthermore, the present results show that estrogen suppresses CYP7B1-catalyzed 7α-hydroxylation also in primary cultures of rat Schwann cells, indicating that regulation by estrogen via this enzyme may be of relevance in both the CNS and the PNS.
MeSH term(s)	Androstenedione/metabolism ; Androstenes/chemistry ; Animals ; Astrocytes/cytology ; Brain/cytology ; Brain/pathology ; Catalysis ; Cells, Cultured ; Culture Media ; Cytochrome P450 Family 7 ; Dehydroepiandrosterone/metabolism ; Dehydroepiandrosterone Sulfate/metabolism ; Estrogens/metabolism ; Female ; Hydroxycholesterols/metabolism ; Male ; Nervous System ; Neuroglia/cytology ; Neuroglia/metabolism ; Neurotransmitter Agents/metabolism ; Rats ; Rats, Sprague-Dawley ; Schwann Cells/cytology ; Sciatic Nerve/pathology ; Steroid Hydroxylases/metabolism ; Steroids/metabolism
Chemical Substances	Androstenes ; Culture Media ; Estrogens ; Hydroxycholesterols ; Neurotransmitter Agents ; Steroids ; Androstenedione (409J2J96VR) ; Dehydroepiandrosterone (459AG36T1B) ; Dehydroepiandrosterone Sulfate (57B09Q7FJR) ; 27-hydroxycholesterol (6T2NA6P5SQ) ; Steroid Hydroxylases (EC 1.14.-) ; Cytochrome P450 Family 7 (EC 1.14.14.23) ; Cyp7b1 protein, rat (EC 1.14.14.29)
Language	English
Publishing date	2014-09-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1049188-0
ISSN	1879-1220 ; 0960-0760
ISSN (online)	1879-1220
ISSN	0960-0760
DOI	10.1016/j.jsbmb.2014.09.022
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Article ; Online: Effects of Osteoporosis-Inducing Drugs on Vitamin D-Related Gene Transcription and Mineralization in MG-63 and Saos-2 Cells.

Wegler, Christine / Wikvall, Kjell / Norlin, Maria

Basic & clinical pharmacology & toxicology

2016 Volume 119, Issue 5, Page(s) 436–442

Abstract: ... Vitamin ... ...

Abstract	Vitamin D
MeSH term(s)	25-Hydroxyvitamin D3 1-alpha-Hydroxylase/metabolism ; Anti-Retroviral Agents/adverse effects ; Benzoxazines/adverse effects ; Bone Density/drug effects ; Calcitriol/metabolism ; Cell Line, Tumor ; Dexamethasone/adverse effects ; Glucocorticoids/adverse effects ; Humans ; Osteoblasts/metabolism ; Osteoporosis/chemically induced ; Ritonavir/adverse effects ; Transcription, Genetic/drug effects ; Up-Regulation ; Vitamin D3 24-Hydroxylase/metabolism ; Vitamins
Chemical Substances	Anti-Retroviral Agents ; Benzoxazines ; Glucocorticoids ; Vitamins ; Dexamethasone (7S5I7G3JQL) ; 25-Hydroxyvitamin D3 1-alpha-Hydroxylase (EC 1.14.13.13) ; CYP24A1 protein, human (EC 1.14.15.16) ; Vitamin D3 24-Hydroxylase (EC 1.14.15.16) ; CYP27B1 protein, human (EC 1.14.15.18) ; Calcitriol (FXC9231JVH) ; efavirenz (JE6H2O27P8) ; Ritonavir (O3J8G9O825)
Language	English
Publishing date	2016-05-20
Publishing country	England
Document type	Journal Article
ZDB-ID	2134679-3
ISSN	1742-7843 ; 1742-7835
ISSN (online)	1742-7843
ISSN	1742-7835
DOI	10.1111/bcpt.12612
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Article: Expression of key enzymes in bile acid biosynthesis during development: CYP7B1-mediated activities show tissue-specific differences.

Norlin, Maria

Journal of lipid research

2002 Volume 43, Issue 5, Page(s) 721–731

Abstract: The developmental variation of cytochrome P450 (CYP)7A1, CYP7B1, CYP27A1, and 3beta-hydroxy-Delta(5)-C(27)-steroid dehydrogenase, key enzymes in bile acid biosynthesis, were investigated in pigs of different ages. As part of these studies, peptide ... ...

Abstract	The developmental variation of cytochrome P450 (CYP)7A1, CYP7B1, CYP27A1, and 3beta-hydroxy-Delta(5)-C(27)-steroid dehydrogenase, key enzymes in bile acid biosynthesis, were investigated in pigs of different ages. As part of these studies, peptide sequences from a purified pig liver oxysterol 7alpha-hydroxylase were analyzed. The sequences showed a high degree of identity with those of murine and human CYP7B1. Enzymatic activities and mRNA levels of CYP27A1 and 3beta-hydroxy-Delta(5)-C(27)-steroid dehydrogenase were similar in livers of newborn and 6-month-old pigs. Enzymatic activity mediated by CYP7A1 increased several-fold between infancy and adolescence. Hepatic CYP7A1 and CYP7B1 mRNA levels increased several-fold with age. Hepatic microsomal 7alpha-hydroxylation of 27-hydroxycholesterol and dehydroepiandrosterone, substrates typical for CYP7B1, increased about 5-fold between infancy and adolescence whereas the activities in kidney microsomes decreased at least 10-fold. In conclusion, the results indicate that the expression of CYP27A1 and 3beta-hydroxy-Delta(5)-C(27)-steroid dehydrogenase are similar in livers of newborn and 6-month-old pigs whereas the levels of CYP7A1 increase. The finding that the levels of CYP7B1 increase with age in the liver but decrease in the kidney suggest a tissue-specific developmental regulation of CYP7B1. The age-dependent variation in the liver and kidney suggests that hormonal factors are involved in the regulation of CYP7B1.
MeSH term(s)	Aging/genetics ; Amino Acid Sequence ; Animals ; Animals, Newborn ; Base Sequence ; Bile Acids and Salts/biosynthesis ; Cytochrome P-450 Enzyme System/genetics ; Cytochrome P450 Family 7 ; Gene Expression Regulation, Developmental/physiology ; Gene Expression Regulation, Enzymologic/physiology ; Humans ; Kinetics ; Male ; Mice ; Mitochondria, Liver/enzymology ; Molecular Sequence Data ; Orchiectomy ; Organ Specificity ; Peptide Fragments/chemistry ; Polymerase Chain Reaction ; Progesterone Reductase/genetics ; RNA, Messenger/genetics ; Sequence Alignment ; Sequence Homology, Amino Acid ; Steroid Hydroxylases/genetics ; Swine ; Transcription, Genetic
Chemical Substances	Bile Acids and Salts ; Peptide Fragments ; RNA, Messenger ; Cytochrome P-450 Enzyme System (9035-51-2) ; Progesterone Reductase (EC 1.1.1.145) ; Steroid Hydroxylases (EC 1.14.-) ; oxysterol 7-alpha-hydroxylase (EC 1.14.13.-) ; Cytochrome P450 Family 7 (EC 1.14.14.23) ; CYP7B1 protein, human (EC 1.14.14.29)
Language	English
Publishing date	2002-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80154-9
ISSN	1539-7262 ; 0022-2275
ISSN (online)	1539-7262
ISSN	0022-2275
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Article: Effects of CYP7B1-related steroids on androgen receptor activation in different cell lines.

Lundqvist, Johan / Norlin, Maria

Biochimica et biophysica acta

2012 Volume 1821, Issue 7, Page(s) 973–979

Abstract: The widely expressed steroid hydroxylase CYP7B1 is involved in metabolism of a number of steroids reported to influence estrogen and androgen signaling. Several studies by us and other investigators have linked this enzyme to effects on estrogen receptor ...

Abstract	The widely expressed steroid hydroxylase CYP7B1 is involved in metabolism of a number of steroids reported to influence estrogen and androgen signaling. Several studies by us and other investigators have linked this enzyme to effects on estrogen receptor activation. In a previous report we examined the effect of CYP7B1-mediated hormone metabolism for estrogen-mediated response in kidney-derived HEK293 cells. In the current study we used an androgen response element (ARE) reporter system to examine androgen-dependent response of some CYP7B1 substrates and CYP7B1-formed metabolites in several cell lines derived from different tissues. The results indicate significantly lower androgen receptor activation by CYP7B1-formed steroid metabolites than by the corresponding steroid substrates, suggesting that CYP7B1-mediated catalysis may decrease some androgenic responses. Thus, CYP7B1-dependent metabolism may be of importance not only for estrogenic signaling but also for androgenic. This finding, that CYP7B1 activity may be a regulator of androgenic signaling by converting AR ligands into less active metabolites, is also supported by real-time RT-PCR experiment where a CYP7B1 substrate, but not the corresponding product, was able to stimulate known androgen-sensitive genes. Furthermore, our data indicate that the effects of some steroids on hormone response element reporter systems are cell line-specific. For instance, despite transfection of the same reporter systems, 5-androstene-3β,17β-diol strongly activates an androgen-dependent response element in prostate cancer cells whereas it elicits only ER-dependent responses in kidney HEK293 cells. Potential roles of cell-specific metabolism or comodulator expression for the observed differences are discussed.
MeSH term(s)	Androgens/pharmacology ; Androstenediol/analogs & derivatives ; Androstenediol/pharmacology ; Cell Line, Tumor ; Cytochrome P450 Family 7 ; Gene Expression ; HEK293 Cells ; Humans ; Male ; Organ Specificity ; Prostatic Neoplasms ; Receptors, Androgen/genetics ; Receptors, Androgen/metabolism ; Response Elements ; Reverse Transcriptase Polymerase Chain Reaction ; Signal Transduction ; Steroid Hydroxylases/genetics ; Steroid Hydroxylases/metabolism ; Testosterone/biosynthesis ; Transfection
Chemical Substances	Androgens ; Receptors, Androgen ; Testosterone (3XMK78S47O) ; Androstenediol (95PS51EMXY) ; Steroid Hydroxylases (EC 1.14.-) ; Cytochrome P450 Family 7 (EC 1.14.14.23) ; CYP7B1 protein, human (EC 1.14.14.29)
Language	English
Publishing date	2012-03-28
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbalip.2012.03.007
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