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Article ; Online: Biotin in metabolism, gene expression, and human disease.

León-Del-Río, Alfonso

2019 Volume 42, Issue 4, Page(s) 647–654

Abstract: Biotin is a water-soluble vitamin that belongs to the vitamin B complex and which is an essential nutrient of all living organisms from bacteria to man. In eukaryotic cells biotin functions as a prosthetic group of enzymes, collectively known as biotin- ... ...

Abstract	Biotin is a water-soluble vitamin that belongs to the vitamin B complex and which is an essential nutrient of all living organisms from bacteria to man. In eukaryotic cells biotin functions as a prosthetic group of enzymes, collectively known as biotin-dependent carboxylases that catalyze key reactions in gluconeogenesis, fatty acid synthesis, and amino acid catabolism. Enzyme-bound biotin acts as a vector to transfer a carboxyl group between donor and acceptor molecules during carboxylation reactions. In recent years, evidence has mounted that biotin also regulates gene expression through a mechanism beyond its role as a prosthetic group of carboxylases. These activities may offer a mechanistic background to a developing literature on the action of biotin in neurological disorders. This review summarizes the role of biotin in activating carboxylases and proposed mechanisms associated with a role in gene expression and in ameliorating neurological disease.
MeSH term(s)	Amino Acids/metabolism ; Biotin/deficiency ; Biotin/metabolism ; Biotinidase/metabolism ; Biotinidase Deficiency/enzymology ; Biotinidase Deficiency/genetics ; Carbon-Carbon Ligases/metabolism ; Gene Expression Regulation ; Humans ; Infant, Newborn ; Metabolism, Inborn Errors/genetics ; Metabolism, Inborn Errors/metabolism ; Multiple Carboxylase Deficiency/genetics ; Multiple Carboxylase Deficiency/metabolism
Chemical Substances	Amino Acids ; Biotin (6SO6U10H04) ; Biotinidase (EC 3.5.1.12) ; Carbon-Carbon Ligases (EC 6.4.-)
Language	English
Publishing date	2019-03-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	438341-2
ISSN	1573-2665 ; 0141-8955
ISSN (online)	1573-2665
ISSN	0141-8955
DOI	10.1002/jimd.12073
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Article ; Online: Arsenic reduces the GATA3 expression associated with an increase in proliferation and migration of mammary epithelial cell line MCF-10A.

Vergara-Gerónimo, Cristian A / León-Del-Rio, Alfonso / Rodríguez-Dorantes, Mauricio / Camacho-Carranza, Rafael / Ostrosky-Wegman, Patricia / Salazar, Ana María

Toxicology and applied pharmacology

2023 Volume 472, Page(s) 116573

Abstract: Arsenic is associated with the development of breast cancer. However, the molecular mechanisms of arsenic induction of breast cancer are not fully defined. Interaction with zinc finger (ZnF) motifs in proteins is one of the proposed mechanisms of arsenic ...

Abstract	Arsenic is associated with the development of breast cancer. However, the molecular mechanisms of arsenic induction of breast cancer are not fully defined. Interaction with zinc finger (ZnF) motifs in proteins is one of the proposed mechanisms of arsenic toxicity. GATA3 is a transcription factor that regulates the transcription of genes associated with cell proliferation, cell differentiation and the epithelial-mesenchymal transition (EMT) in mammary luminal cells. Given that GATA3 possesses two ZnF motifs essential for the function of this protein and that arsenic could alter the function of GATA3 through interaction with these structural motifs, we evaluated the effect of sodium arsenite (NaAsO
MeSH term(s)	Female ; Humans ; Arsenic/toxicity ; Breast Neoplasms/chemically induced ; Breast Neoplasms/genetics ; Cell Line, Tumor ; Cell Movement ; Cell Proliferation ; Epithelial Cells/metabolism ; GATA3 Transcription Factor/antagonists & inhibitors ; GATA3 Transcription Factor/metabolism ; Transcription Factors
Chemical Substances	Arsenic (N712M78A8G) ; GATA3 protein, human ; GATA3 Transcription Factor ; Transcription Factors
Language	English
Publishing date	2023-06-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	204477-8
ISSN	1096-0333 ; 0041-008X
ISSN (online)	1096-0333
ISSN	0041-008X
DOI	10.1016/j.taap.2023.116573
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Article: Uncovering a novel mechanism: Butyrate induces estrogen receptor alpha activation independent of estrogen stimulation in MCF-7 breast cancer cells.

Gutierrez-Martinez, Veronica Dayali / León-Del-Río, Alfonso / Camacho-Luis, Abelardo / Ayala-Garcia, Victor Manuel / Lopez-Rodriguez, Angélica María / Ruiz-Baca, Estela / Meneses-Morales, Ivan

Genetics and molecular biology

2024 Volume 47, Issue 1, Page(s) e20230110

Abstract: Butyrate is a promising candidate for an antitumoral drug, as it promotes cancer cell apoptosis and reduces hormone receptor activity, while promoting differentiation and proliferation in normal cells. However, the effects of low-dose butyrate on breast ... ...

Abstract	Butyrate is a promising candidate for an antitumoral drug, as it promotes cancer cell apoptosis and reduces hormone receptor activity, while promoting differentiation and proliferation in normal cells. However, the effects of low-dose butyrate on breast cancer cell cultures are unclear. We explored the impact of sub-therapeutic doses of butyrate on estrogen receptor alpha (ERα) transcriptional activity in MCF-7 cells, using RT-qPCR, Western blot, wound-healing assays, and chromatin immunoprecipitation. Our results showed that sub-therapeutic doses of sodium butyrate (0.1 - 0.2 mM) increased the transcription of ESR1, TFF1, and CSTD genes, but did not affect ERα protein levels. Moreover, we observed an increase in cell migration in wound-healing assays. ChIP assays revealed that treatment with 0.1 mM of sodium butyrate resulted in estrogen-independent recruitment of ERα at the pS2 promoter and loss of NCoR. Appropriate therapeutic dosage of butyrate is essential to avoid potential adverse effects on patients' health, especially in the case of estrogen receptor-positive breast tumors. Sub-therapeutic doses of butyrate may induce undesirable cell processes, such as migration due to low-dose butyrate-mediated ERα activation. These findings shed light on the complex effects of butyrate in breast cancer and provide insights for research in the development of antitumoral drugs.
Language	English
Publishing date	2024-03-08
Publishing country	Brazil
Document type	Journal Article
ZDB-ID	1445712-x
ISSN	1678-4685 ; 1415-4757
ISSN (online)	1678-4685
ISSN	1415-4757
DOI	10.1590/1678-4685-GMB-2023-0110
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Article ; Online: Arsenic-protein interactions as a mechanism of arsenic toxicity.

Vergara-Gerónimo, Cristian A / León Del Río, Alfonso / Rodríguez-Dorantes, Mauricio / Ostrosky-Wegman, Patricia / Salazar, Ana María

Toxicology and applied pharmacology

2021 Volume 431, Page(s) 115738

Abstract: Millions of people worldwide are exposed to arsenic, a metalloid listed as one of the top chemical pollutants of concern to human health. Epidemiological and experimental studies link arsenic exposure to the development of cancer and other diseases. ... ...

Abstract	Millions of people worldwide are exposed to arsenic, a metalloid listed as one of the top chemical pollutants of concern to human health. Epidemiological and experimental studies link arsenic exposure to the development of cancer and other diseases. Several mechanisms have been proposed to explain the effects induced by arsenic. Notably, arsenic and its metabolites interact with proteins by direct binding to individual cysteine residues, cysteine clusters, zinc finger motifs, and RING finger domains. Consequently, arsenic interactions with proteins disrupt the functions of proteins and may lead to the development and progression of diseases. In this review, we focus on current evidence in the literature that implicates the interaction of arsenic with proteins as a mechanism of arsenic toxicity. Data show that arsenic-protein interactions affect multiple cellular processes and alter epigenetic regulation, cause endocrine disruption, inhibit DNA damage repair mechanisms, and deregulate gene expression, among other adverse effects.
MeSH term(s)	Animals ; Arsenic Poisoning/etiology ; Arsenic Poisoning/genetics ; Arsenic Poisoning/metabolism ; Arsenicals/adverse effects ; Arsenicals/metabolism ; Cysteine ; DNA Repair/drug effects ; Endocrine Disruptors/adverse effects ; Endocrine Disruptors/metabolism ; Environmental Pollutants/adverse effects ; Environmental Pollutants/metabolism ; Epigenesis, Genetic/drug effects ; Humans ; Protein Binding ; Proteins/genetics ; Proteins/metabolism ; RING Finger Domains ; Risk Assessment ; Zinc Fingers
Chemical Substances	Arsenicals ; Endocrine Disruptors ; Environmental Pollutants ; Proteins ; Cysteine (K848JZ4886)
Language	English
Publishing date	2021-10-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	204477-8
ISSN	1096-0333 ; 0041-008X
ISSN (online)	1096-0333
ISSN	0041-008X
DOI	10.1016/j.taap.2021.115738
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Article ; Online: The inhibitory effect of trastuzumab on BT474 triple‑positive breast cancer cell viability is reversed by the combination of progesterone and estradiol.

López-Méndez, José A / Ventura-Gallegos, José L / Camacho-Arroyo, Ignacio / Lizano, Marcela / Cabrera-Quintero, Alberto J / Romero-Córdoba, Sandra L / Martínez-Vázquez, Mariano / Jacobo-Herrera, Nadia J / León-Del-Río, Alfonso / Paredes-Villa, Adrian A / Zentella-Dehesa, Alejandro

Oncology letters

2023 Volume 27, Issue 1, Page(s) 19

Abstract: Breast cancer expressing the estrogen receptor (ER), progesterone receptor (PR) and human epidermal growth factor receptor-2 (HER2) is known as triple-positive (TPBC). TPBC represents 9-11% of breast cancer cases worldwide and is a heterogeneous subtype. ...

Abstract	Breast cancer expressing the estrogen receptor (ER), progesterone receptor (PR) and human epidermal growth factor receptor-2 (HER2) is known as triple-positive (TPBC). TPBC represents 9-11% of breast cancer cases worldwide and is a heterogeneous subtype. Notably, TPBC presents a therapeutic challenge due to the crosstalk between the hormonal (ER and PR) and HER2 pathways. Patients with TPBC are treated with trastuzumab (TTZ); however, several patients treated with TTZ tend to relapse. The present study aimed to investigate the effect of the PR on inhibitory effect of TTZ on cell viability. BT474 cells (a model of TPBC) and BT474 PR-silenced cells were treated with either TTZ, progesterone (Pg), the PR antagonist mifepristone (RU486) or estradiol (E2) alone or in combination for 144 h (6 days). Cell viability assays and western blotting were subsequently performed. The results showed that Pg and E2 interfered with the inhibitory effect of TTZ on cell viability and this effect was potentiated when both hormones were combined. Pg was revealed to act through the PR, mainly activating the PR isoform B (PR-B) and inducing the protein expression levels of CDK4 and cyclin D1; however, it did not reactivate the HER2/Akt pathway. By contrast, E2 was able to increase PR isoform A (PR-A) expression, which was inhibited by Pg. Notably, in most of the experiments, RU486 did not antagonize the effects of Pg. In conclusion, Pg and E2 may interfere with the inhibitory effect of TTZ on cell viability through PR-B activation and PR-A inactivation.
Language	English
Publishing date	2023-11-15
Publishing country	Greece
Document type	Journal Article
ZDB-ID	2573196-8
ISSN	1792-1082 ; 1792-1074
ISSN (online)	1792-1082
ISSN	1792-1074
DOI	10.3892/ol.2023.14152
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Article ; Online: Holocarboxylase Synthetase: A Moonlighting Transcriptional Coregulator of Gene Expression and a Cytosolic Regulator of Biotin Utilization.

León-Del-Río, Alfonso / Valadez-Graham, Viviana / Gravel, Roy A

Annual review of nutrition

2017 Volume 37, Page(s) 207–223

Abstract: The vitamin biotin is an essential nutrient for the metabolism and survival of all organisms owing to its function as a cofactor of enzymes collectively known as biotin-dependent carboxylases. These enzymes use covalently attached biotin as a vector to ... ...

Abstract	The vitamin biotin is an essential nutrient for the metabolism and survival of all organisms owing to its function as a cofactor of enzymes collectively known as biotin-dependent carboxylases. These enzymes use covalently attached biotin as a vector to transfer a carboxyl group between donor and acceptor molecules during carboxylation reactions. In human cells, biotin-dependent carboxylases catalyze key reactions in gluconeogenesis, fatty acid synthesis, and amino acid catabolism. Biotin is attached to apocarboxylases by a biotin ligase: holocarboxylase synthetase (HCS) in mammalian cells and BirA in microbes. Despite their evolutionary distance, these proteins share structural and sequence similarities, underscoring their importance across all life forms. However, beyond its role in metabolism, HCS participates in the regulation of biotin utilization and acts as a nuclear transcriptional coregulator of gene expression. In this review, we discuss the function of HCS and biotin in metabolism and human disease, a putative role for the enzyme in histone biotinylation, and its participation as a nuclear factor in chromatin dynamics. We suggest that HCS be classified as a moonlighting protein, with two biotin-dependent cytosolic metabolic roles and a distinct biotin-independent nuclear coregulatory function.
MeSH term(s)	Biotin/metabolism ; Biotinylation ; Carbon-Nitrogen Ligases/metabolism ; Chromatin/metabolism ; Cytosol/metabolism ; Gene Expression Regulation ; Histones/metabolism ; Humans
Chemical Substances	Chromatin ; Histones ; Biotin (6SO6U10H04) ; Carbon-Nitrogen Ligases (EC 6.3.-) ; holocarboxylase synthetases (EC 6.3.4.-)
Language	English
Publishing date	2017-08-21
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	406980-8
ISSN	1545-4312 ; 0199-9885
ISSN (online)	1545-4312
ISSN	0199-9885
DOI	10.1146/annurev-nutr-042617-104653
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Article ; Online: Jab1 is a T2-dependent coactivator or a T3-dependent corepressor of TRB1-mediated gene regulation.

Hernández-Puga, Gabriela / Mendoza, Arturo / León-Del-Río, Alfonso / Orozco, Aurea

The Journal of endocrinology

2017 Volume 232, Issue 3, Page(s) 451–459

Abstract: Thyroid hormones (THs) induce pleiotropic effects in vertebrates, mainly through the activation or repression of gene expression. These mechanisms involve thyroid hormone binding to thyroid hormone receptors, an event that is followed by the sequential ... ...

Abstract	Thyroid hormones (THs) induce pleiotropic effects in vertebrates, mainly through the activation or repression of gene expression. These mechanisms involve thyroid hormone binding to thyroid hormone receptors, an event that is followed by the sequential recruitment of coactivator or corepressor proteins, which in turn modify the rate of transcription. In the present study, we looked for specific coregulators recruited by the long isoform of the teleostean thyroid hormone receptor beta 1 (L-Trb1) when bound to the bioactive TH, 3,5-T
MeSH term(s)	Animals ; COP9 Signalosome Complex ; Cell Line ; Dose-Response Relationship, Drug ; Gene Expression Regulation/drug effects ; Intracellular Signaling Peptides and Proteins ; Proteins/genetics ; Proteins/metabolism ; Rats ; Receptors, Thyroid Hormone/metabolism ; Thyroid Hormone Receptors beta/metabolism ; Thyroid Hormones/pharmacology
Chemical Substances	Gps1 protein, rat ; Intracellular Signaling Peptides and Proteins ; Proteins ; Receptors, Thyroid Hormone ; Thyroid Hormone Receptors beta ; Thyroid Hormones ; COP9 Signalosome Complex (EC 3.4.19.12)
Language	English
Publishing date	2017-01-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3028-4
ISSN	1479-6805 ; 0022-0795
ISSN (online)	1479-6805
ISSN	0022-0795
DOI	10.1530/JOE-16-0485
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Article ; Online: Tristetraprolin: A cytosolic regulator of mRNA turnover moonlighting as transcriptional corepressor of gene expression.

Rodríguez-Gómez, Gabriel / Paredes-Villa, Alejandro / Cervantes-Badillo, Mayte Guadalupe / Gómez-Sonora, Jessica Paola / Jorge-Pérez, Jesús H / Cervantes-Roldán, Rafael / León-Del-Río, Alfonso

Molecular genetics and metabolism

2021 Volume 133, Issue 2, Page(s) 137–147

Abstract: Tristetraprolin (TTP) is a nucleocytoplasmic 326 amino acid protein whose sequence is characterized by possessing two CCCH-type zinc finger domains. In the cytoplasm TTP function is to promote the degradation of mRNAs that contain adenylate/uridylate- ... ...

Abstract	Tristetraprolin (TTP) is a nucleocytoplasmic 326 amino acid protein whose sequence is characterized by possessing two CCCH-type zinc finger domains. In the cytoplasm TTP function is to promote the degradation of mRNAs that contain adenylate/uridylate-rich elements (AREs). Mechanistically, TTP promotes the recruitment of poly(A)-specific deadenylases and exoribonucleases. By reducing the half-life of about 10% of all the transcripts in the cell TTP has been shown to participate in multiple cell processes that include regulation of gene expression, cell proliferation, metabolic homeostasis and control of inflammation and immune responses. However, beyond its role in mRNA decay, in the cell nucleus TTP acts as a transcriptional coregulator by interacting with chromatin modifying enzymes. TTP has been shown to repress the transactivation of NF-κB and estrogen receptor suggesting the possibility that it participates in the transcriptional regulation of hundreds of genes in human cells and its possible involvement in breast cancer progression. In this review, we discuss the cytoplasmic and nuclear functions of TTP and the effect of the dysregulation of its protein levels in the development of human diseases. We suggest that TTP be classified as a moonlighting tumor supressor protein that regulates gene expression through two different mechanims; the decay of ARE-mRNAs and a transcriptional coregulatory function.
MeSH term(s)	Cell Proliferation/genetics ; Cytosol/metabolism ; Gene Expression Regulation/genetics ; Humans ; Inflammation/genetics ; Inflammation/pathology ; RNA Stability/genetics ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Transcriptional Activation/genetics ; Tristetraprolin/genetics ; Tristetraprolin/metabolism ; Zinc Fingers/genetics
Chemical Substances	RNA, Messenger ; Tristetraprolin
Language	English
Publishing date	2021-03-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1418518-0
ISSN	1096-7206 ; 1096-7192
ISSN (online)	1096-7206
ISSN	1096-7192
DOI	10.1016/j.ymgme.2021.03.015
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Article: Biotin-dependent regulation of gene expression in human cells.

León-Del-Río, Alfonso

The Journal of nutritional biochemistry

2005 Volume 16, Issue 7, Page(s) 432–434

Abstract: The role of biotin as cofactor of carboxylases and its importance in metabolic homeostasis are well known. In recent years, different researchers have suggested the participation of biotin as a regulator molecule in the control of gene expression. Biotin- ...

Abstract	The role of biotin as cofactor of carboxylases and its importance in metabolic homeostasis are well known. In recent years, different researchers have suggested the participation of biotin as a regulator molecule in the control of gene expression. Biotin-dependent gene expression requires of the transformation of biotin into biotinyl-5'-AMP by holocarboxylase synthetase and the activation of soluble guanylate cyclase and a cGMP-dependent protein kinase. The regulatory role of biotin is responsible for the correct expression of enzymes involved in biotin utilization in human cells. We propose that this mechanism protects the brain from biotin deficiency.
MeSH term(s)	Biotin/deficiency ; Biotin/metabolism ; Biotinidase Deficiency/metabolism ; Carbon-Nitrogen Ligases/genetics ; Carbon-Nitrogen Ligases/metabolism ; Gene Expression Regulation ; Holocarboxylase Synthetase Deficiency/metabolism ; Humans ; Symporters/genetics ; Symporters/metabolism
Chemical Substances	Symporters ; biotin transporter ; Biotin (6SO6U10H04) ; Carbon-Nitrogen Ligases (EC 6.3.-) ; holocarboxylase synthetases (EC 6.3.4.-)
Language	English
Publishing date	2005-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1014929-6
ISSN	1873-4847 ; 0955-2863
ISSN (online)	1873-4847
ISSN	0955-2863
DOI	10.1016/j.jnutbio.2005.03.021
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Article: IFI27/ISG12 Downregulates Estrogen Receptor α Transactivation by Facilitating Its Interaction With CRM1/XPO1 in Breast Cancer Cells.

Cervantes-Badillo, Mayte Guadalupe / Paredes-Villa, Alejandro / Gómez-Romero, Vania / Cervantes-Roldán, Rafael / Arias-Romero, Luis E / Villamar-Cruz, Olga / González-Montiel, Miroslava / Barrios-García, Tonatiuh / Cabrera-Quintero, Alberto J / Rodríguez-Gómez, Gabriel / Cancino-Villeda, Laura / Zentella-Dehesa, Alejandro / León-Del-Río, Alfonso

Frontiers in endocrinology

2020 Volume 11, Page(s) 568375

Abstract: The estrogen receptor alpha (ERα) is a ligand-activated transcription factor whose activity is modulated by its interaction with multiple protein complexes. In this work, we have identified the protein interferon alpha inducible protein 27 (IFI27/ISG12) ... ...

Abstract	The estrogen receptor alpha (ERα) is a ligand-activated transcription factor whose activity is modulated by its interaction with multiple protein complexes. In this work, we have identified the protein interferon alpha inducible protein 27 (IFI27/ISG12) as a novel ERα-associated protein. IFI27/ISG12 transcription is regulated by interferon and estradiol and its overexpression is associated to reduced overall survival in ER+ breast cancer patients but its function in mammary gland tissue remains elusive. In this study we showed that overexpression of IFI27/ISG12 in breast cancer cells attenuates ERα transactivation activity and the expression of ERα-dependent genes. Our results demonstrated that IFI27/ISG12 overexpression in MCF-7 cells reduced their proliferation rate in 2-D and 3-D cell culture assays and impaired their ability to migrate in a wound-healing assay. We show that IFI27/ISG12 downregulation of ERα transactivation activity is mediated by its ability to facilitate the interaction between ERα and CRM1/XPO1 that mediates the nuclear export of large macromolecules to the cytoplasm. IFI27/ISG12 overexpression was shown to impair the estradiol-dependent proliferation and tamoxifen-induced apoptosis in breast cancer cells. Our results suggest that IFI27/ISG12 may be an important factor in regulating ERα activity in breast cancer cells by modifying its nuclear versus cytoplasmic protein levels. We propose that IFI27/ISG12 may be a potential target of future strategies to control the growth and proliferation of ERα-positive breast cancer tumors.
MeSH term(s)	Breast Neoplasms/genetics ; Breast Neoplasms/metabolism ; Databases, Genetic ; Down-Regulation/drug effects ; Down-Regulation/physiology ; Estradiol/pharmacology ; Estrogen Receptor alpha/antagonists & inhibitors ; Estrogen Receptor alpha/biosynthesis ; Estrogen Receptor alpha/genetics ; Female ; Humans ; Karyopherins/biosynthesis ; Karyopherins/genetics ; MCF-7 Cells ; Membrane Proteins/biosynthesis ; Membrane Proteins/genetics ; Receptors, Cytoplasmic and Nuclear/biosynthesis ; Receptors, Cytoplasmic and Nuclear/genetics ; Tamoxifen/pharmacology ; Transcriptional Activation/drug effects ; Transcriptional Activation/physiology ; Exportin 1 Protein
Chemical Substances	ESR1 protein, human ; Estrogen Receptor alpha ; IFI27 protein, human ; Karyopherins ; Membrane Proteins ; Receptors, Cytoplasmic and Nuclear ; Tamoxifen (094ZI81Y45) ; Estradiol (4TI98Z838E)
Language	English
Publishing date	2020-10-07
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2592084-4
ISSN	1664-2392
ISSN	1664-2392
DOI	10.3389/fendo.2020.568375
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