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Article: Mutation in the Common Docking Domain Affects MAP Kinase ERK2 Catalysis and Stability.

Novak, Leonore / Petrosino, Maria / Pasquo, Alessandra / Chaikuad, Apirat / Chiaraluce, Roberta / Knapp, Stefan / Consalvi, Valerio

Cancers

2023 Volume 15, Issue 11

Abstract: The extracellular-signal-regulated kinase 2 (ERK2), a mitogen-activated protein kinase (MAPK) located downstream of the Ras-Raf-MEK-ERK signal transduction cascade, is involved in the regulation of a large variety of cellular processes. The ERK2, ... ...

Abstract	The extracellular-signal-regulated kinase 2 (ERK2), a mitogen-activated protein kinase (MAPK) located downstream of the Ras-Raf-MEK-ERK signal transduction cascade, is involved in the regulation of a large variety of cellular processes. The ERK2, activated by phosphorylation, is the principal effector of a central signaling cascade that converts extracellular stimuli into cells. Deregulation of the ERK2 signaling pathway is related to many human diseases, including cancer. This study reports a comprehensive biophysical analysis of structural, function, and stability data of pure, recombinant human non-phosphorylated (NP-) and phosphorylated (P-) ERK2 wild-type and missense variants in the common docking site (CD-site) found in cancer tissues. Because the CD-site is involved in interaction with protein substrates and regulators, a biophysical characterization of missense variants adds information about the impact of point mutations on the ERK2 structure-function relationship. Most of the P-ERK2 variants in the CD-site display a reduced catalytic efficiency, and for the P-ERK2 D321E, D321N, D321V and E322K, changes in thermodynamic stability are observed. The thermal stability of NP-ERK2 and P-ERK2 D321E, D321G, and E322K is decreased with respect to the wild-type. In general, a single residue mutation in the CD-site may lead to structural local changes that reflects in alterations in the global ERK2 stability and catalysis.
Language	English
Publishing date	2023-05-26
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2527080-1
ISSN	2072-6694
ISSN	2072-6694
DOI	10.3390/cancers15112938
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Article: The Role of Organosulfur Compounds as Nrf2 Activators and Their Antioxidant Effects.

Egbujor, Melford Chuka / Petrosino, Maria / Zuhra, Karim / Saso, Luciano

Antioxidants (Basel, Switzerland)

2022 Volume 11, Issue 7

Abstract: Nuclear factor erythroid 2-related factor 2 (Nrf2) signaling has become a key pathway for cellular regulation against oxidative stress and inflammation, and therefore an attractive therapeutic target. Several organosulfur compounds are reportedly ... ...

Abstract	Nuclear factor erythroid 2-related factor 2 (Nrf2) signaling has become a key pathway for cellular regulation against oxidative stress and inflammation, and therefore an attractive therapeutic target. Several organosulfur compounds are reportedly activators of the Nrf2 pathway. Organosulfur compounds constitute an important class of therapeutic agents in medicinal chemistry due to their ability to participate in biosynthesis, metabolism, cellular functions, and protection of cells from oxidative damage. Sulfur has distinctive chemical properties such as a large number of oxidation states and versatility of reactions that promote fundamental biological reactions and redox biochemistry. The presence of sulfur is responsible for the peculiar features of organosulfur compounds which have been utilized against oxidative stress-mediated diseases. Nrf2 activation being a key therapeutic strategy for oxidative stress is closely tied to sulfur-based chemistry since the ability of compounds to react with sulfhydryl (-SH) groups is a common property of Nrf2 inducers. Although some individual organosulfur compounds have been reported as Nrf2 activators, there are no papers with a collective analysis of these Nrf2-activating organosulfur compounds which may help to broaden the knowledge of their therapeutic potentials and motivate further research. In line with this fact, for the first time, this review article provides collective and comprehensive information on Nrf2-activating organosulfur compounds and their therapeutic effects against oxidative stress, thereby enriching the chemical and pharmacological diversity of Nrf2 activators.
Language	English
Publishing date	2022-06-26
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2704216-9
ISSN	2076-3921
ISSN	2076-3921
DOI	10.3390/antiox11071255
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Article: The Role of Organosulfur Compounds as Nrf2 Activators and Their Antioxidant Effects

Egbujor, Melford Chuka / Petrosino, Maria / Zuhra, Karim / Saso, Luciano

Antioxidants. 2022 June 26, v. 11, no. 7

2022

Abstract	Nuclear factor erythroid 2-related factor 2 (Nrf2) signaling has become a key pathway for cellular regulation against oxidative stress and inflammation, and therefore an attractive therapeutic target. Several organosulfur compounds are reportedly activators of the Nrf2 pathway. Organosulfur compounds constitute an important class of therapeutic agents in medicinal chemistry due to their ability to participate in biosynthesis, metabolism, cellular functions, and protection of cells from oxidative damage. Sulfur has distinctive chemical properties such as a large number of oxidation states and versatility of reactions that promote fundamental biological reactions and redox biochemistry. The presence of sulfur is responsible for the peculiar features of organosulfur compounds which have been utilized against oxidative stress-mediated diseases. Nrf2 activation being a key therapeutic strategy for oxidative stress is closely tied to sulfur-based chemistry since the ability of compounds to react with sulfhydryl (-SH) groups is a common property of Nrf2 inducers. Although some individual organosulfur compounds have been reported as Nrf2 activators, there are no papers with a collective analysis of these Nrf2-activating organosulfur compounds which may help to broaden the knowledge of their therapeutic potentials and motivate further research. In line with this fact, for the first time, this review article provides collective and comprehensive information on Nrf2-activating organosulfur compounds and their therapeutic effects against oxidative stress, thereby enriching the chemical and pharmacological diversity of Nrf2 activators.
Keywords	antioxidants ; biosynthesis ; inflammation ; oxidation ; oxidative stress ; sulfur ; therapeutics
Language	English
Dates of publication	2022-0626
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2704216-9
ISSN	2076-3921
ISSN	2076-3921
DOI	10.3390/antiox11071255
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Article ; Online: H2S biogenesis by cystathionine beta-synthase: mechanism of inhibition by aminooxyacetic acid and unexpected role of serine

Petrosino, Maria / Zuhra, Karim / Kopec, Jola / Hutchin, Andrew / Szabó, Csaba / Majtan, Tomas

Cell. Mol. Life Sci.. 2022 Aug., v. 79, no. 8 p.438-438

2022

Abstract: Cystathionine beta-synthase (CBS) is a pivotal enzyme of the transsulfuration pathway responsible for diverting homocysteine to the biosynthesis of cysteine and production of hydrogen sulfide (H₂S). Aberrant upregulation of CBS and overproduction of H₂S ... ...

Abstract	Cystathionine beta-synthase (CBS) is a pivotal enzyme of the transsulfuration pathway responsible for diverting homocysteine to the biosynthesis of cysteine and production of hydrogen sulfide (H₂S). Aberrant upregulation of CBS and overproduction of H₂S contribute to pathophysiology of several diseases including cancer and Down syndrome. Therefore, pharmacological CBS inhibition has emerged as a prospective therapeutic approach. Here, we characterized binding and inhibitory mechanism of aminooxyacetic acid (AOAA), the most commonly used CBS inhibitor. We found that AOAA binds CBS tighter than its respective substrates and forms a dead-end PLP-bound intermediate featuring an oxime bond. Surprisingly, serine, but not cysteine, replaced AOAA from CBS and formed an aminoacrylate reaction intermediate, which allowed for the continuation of the catalytic cycle. Indeed, serine rescued and essentially normalized the enzymatic activity of AOAA-inhibited CBS. Cellular studies confirmed that AOAA decreased H₂S production and bioenergetics, while additional serine rescued CBS activity, H₂S production and mitochondrial function. The crystal structure of AOAA-bound human CBS showed a lack of hydrogen bonding with residues G305 and Y308, found in the serine-bound model. Thus, AOAA-inhibited CBS could be reactivated by serine. This difference may be important in a cellular environment in multiple pathophysiological conditions and may modulate the CBS-inhibitory activity of AOAA. In addition, our results demonstrate additional complexities of using AOAA as a CBS-specific inhibitor of H₂S biogenesis and point to the urgent need to develop a potent, selective and specific pharmacological CBS inhibitor.
Keywords	Down syndrome ; aminooxyacetic acid ; biogenesis ; biosynthesis ; crystal structure ; cystathionine beta-synthase ; cysteine ; energy metabolism ; enzyme activity ; homocysteine ; humans ; hydrogen ; hydrogen sulfide ; mitochondria ; models ; pathophysiology ; serine ; therapeutics
Language	English
Dates of publication	2022-08
Size	p. 438.
Publishing place	Springer International Publishing
Document type	Article ; Online
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-022-04479-9
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: H

Petrosino, Maria / Zuhra, Karim / Kopec, Jola / Hutchin, Andrew / Szabo, Csaba / Majtan, Tomas

Cellular and molecular life sciences : CMLS

2022 Volume 79, Issue 8, Page(s) 438

Abstract	Cystathionine beta-synthase (CBS) is a pivotal enzyme of the transsulfuration pathway responsible for diverting homocysteine to the biosynthesis of cysteine and production of hydrogen sulfide (H
MeSH term(s)	Aminooxyacetic Acid/pharmacology ; Cystathionine beta-Synthase/metabolism ; Cysteine ; Humans ; Hydrogen Sulfide/metabolism ; Hydrogen Sulfide/pharmacology ; Serine
Chemical Substances	Aminooxyacetic Acid (14I68GI3OQ) ; Serine (452VLY9402) ; Cystathionine beta-Synthase (EC 4.2.1.22) ; Cysteine (K848JZ4886) ; Hydrogen Sulfide (YY9FVM7NSN)
Language	English
Publishing date	2022-07-21
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-022-04479-9
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Article ; Online: Inhibition of the 3-mercaptopyruvate sulfurtransferase-hydrogen sulfide system promotes cellular lipid accumulation.

Casili, Giovanna / Randi, Elisa / Panagaki, Theodora / Zuhra, Karim / Petrosino, Maria / Szabo, Csaba

GeroScience

2022 Volume 44, Issue 4, Page(s) 2271–2289

Abstract: ... H ... 2 ... S is generated in the adipose tissue by cystathionine γ-lyase, cystathionine β-synthase, and 3-mercaptopyruvate sulfurtransferase (3-MST). H ... 2 ... S plays multiple roles in the regulation of various metabolic processes, including ... ...

Abstract	H<sub>2</sub>S is generated in the adipose tissue by cystathionine γ-lyase, cystathionine β-synthase, and 3-mercaptopyruvate sulfurtransferase (3-MST). H<sub>2</sub>S plays multiple roles in the regulation of various metabolic processes, including insulin resistance. H<sub>2</sub>S biosynthesis also occurs in adipocytes. Aging is known to be associated with a decline in H<sub>2</sub>S. Therefore, the question arises whether endogenous H<sub>2</sub>S deficiency may affect the process of adipocyte maturation and lipid accumulation. Among the three H<sub>2</sub>S-generating enzymes, the role of 3-MST is the least understood in adipocytes. Here we tested the effect of the 3-MST inhibitor 2-[(4-hydroxy-6-methylpyrimidin-2-yl)sulfanyl]-1-(naphthalen-1-yl)ethan-1-one (HMPSNE) and the H<sub>2</sub>S donor (GYY4137) on the differentiation and adipogenesis of the adipocyte-like cells 3T3-L1 in vitro. 3T3-L1 cells were differentiated into mature adipocytes in the presence of GYY4137 or HMPSNE. HMPSNE significantly enhanced lipid accumulation into the maturing adipocytes. On the other hand, suppressed lipid accumulation was observed in cells treated with the H<sub>2</sub>S donor. 3-MST inhibition increased, while H<sub>2</sub>S donation suppressed the expression of various H<sub>2</sub>S-producing enzymes during adipocyte differentiation. 3-MST knockdown also facilitated adipocytic differentiation and lipid uptake. The underlying mechanisms may involve impairment of oxidative phosphorylation and fatty acid oxidation as well as the activation of various differentiation-associated transcription factors. Thus, the 3-MST/H<sub>2</sub>S system plays a tonic role in suppressing lipid accumulation and limiting the differentiation of adipocytes. Stimulation of 3-MST activity or supplementation of H<sub>2</sub>S-which has been recently linked to various experimental therapeutic approaches during aging-may be a potential experimental approach to counteract adipogenesis.
MeSH term(s)	Hydrogen Sulfide/pharmacology ; Hydrogen Sulfide/metabolism ; Sulfurtransferases/metabolism ; Lipids
Chemical Substances	3-mercaptopyruvate sulphurtransferase (EC 2.8.1.2) ; Hydrogen Sulfide (YY9FVM7NSN) ; GYY 4137 ; Sulfurtransferases (EC 2.8.1.-) ; Lipids
Language	English
Publishing date	2022-06-10
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2886586-8
ISSN	2509-2723 ; 2509-2715
ISSN (online)	2509-2723
ISSN	2509-2715
DOI	10.1007/s11357-022-00600-9
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Article ; Online: The complex impact of cancer-related missense mutations on the stability and on the biophysical and biochemical properties of MAPK1 and MAPK3 somatic variants.

Petrosino, Maria / Novak, Leonore / Pasquo, Alessandra / Turina, Paola / Capriotti, Emidio / Minicozzi, Velia / Consalvi, Valerio / Chiaraluce, Roberta

Human genomics

2023 Volume 17, Issue 1, Page(s) 95

Abstract: Mitogen-activated protein kinases 1 and 3 (MAPK1 and MAPK3), also called extracellular regulated kinases (ERK2 and ERK1), are serine/threonine kinase activated downstream by the Ras/Raf/MEK/ERK signal transduction cascade that regulates a variety of ... ...

Abstract	Mitogen-activated protein kinases 1 and 3 (MAPK1 and MAPK3), also called extracellular regulated kinases (ERK2 and ERK1), are serine/threonine kinase activated downstream by the Ras/Raf/MEK/ERK signal transduction cascade that regulates a variety of cellular processes. A dysregulation of MAPK cascade is frequently associated to missense mutations on its protein components and may be related to many pathologies, including cancer. In this study we selected from COSMIC database a set of MAPK1 and MAPK3 somatic variants found in cancer tissues carrying missense mutations distributed all over the MAPK1 and MAPK3 sequences. The proteins were expressed as pure recombinant proteins, and their biochemical and biophysical properties have been studied in comparison with the wild type. The missense mutations lead to changes in the tertiary arrangements of all the variants. The thermodynamic stability of the wild type and variants has been investigated in the non-phosphorylated and in the phosphorylated form. Significant differences in the thermal stabilities of most of the variants have been observed, as well as changes in the catalytic efficiencies. The energetics of the catalytic reaction is affected for all the variants for both the MAPK proteins. The stability changes and the variation in the enzyme catalysis observed for most of MAPK1/3 variants suggest that a local change in a residue, distant from the catalytic site, may have long-distance effects that reflect globally on enzyme stability and functions.
MeSH term(s)	Humans ; Mitogen-Activated Protein Kinase 1/metabolism ; Mutation, Missense/genetics ; Neoplasms/genetics ; Neoplasms/metabolism ; Phosphorylation ; Protein Serine-Threonine Kinases/metabolism ; Signal Transduction
Chemical Substances	MAPK1 protein, human (EC 2.7.11.24) ; Mitogen-Activated Protein Kinase 1 (EC 2.7.11.24) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; MAPK3 protein, human (EC 2.7.11.24)
Language	English
Publishing date	2023-10-27
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2147618-4
ISSN	1479-7364 ; 1479-7364
ISSN (online)	1479-7364
ISSN	1479-7364
DOI	10.1186/s40246-023-00544-x
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Article ; Online: Catalytic specificity and crystal structure of cystathionine γ-lyase from Pseudomonas aeruginosa.

Pedretti, Marco / Fernández-Rodríguez, Carmen / Conter, Carolina / Oyenarte, Iker / Favretto, Filippo / di Matteo, Adele / Dominici, Paola / Petrosino, Maria / Martinez-Chantar, Maria Luz / Majtan, Tomas / Astegno, Alessandra / Martínez-Cruz, Luis Alfonso

Scientific reports

2024 Volume 14, Issue 1, Page(s) 9364

Abstract: The escalating drug resistance among microorganisms underscores the urgent need for innovative therapeutic strategies and a comprehensive understanding of bacteria's defense mechanisms against oxidative stress and antibiotics. Among the recently ... ...

Abstract	The escalating drug resistance among microorganisms underscores the urgent need for innovative therapeutic strategies and a comprehensive understanding of bacteria's defense mechanisms against oxidative stress and antibiotics. Among the recently discovered barriers, the endogenous production of hydrogen sulfide (H
MeSH term(s)	Pseudomonas aeruginosa/enzymology ; Cystathionine gamma-Lyase/metabolism ; Cystathionine gamma-Lyase/chemistry ; Crystallography, X-Ray ; Substrate Specificity ; Catalytic Domain ; Hydrogen Sulfide/metabolism ; Hydrogen Sulfide/chemistry ; Models, Molecular ; Cysteine/metabolism ; Cysteine/chemistry ; Protein Conformation ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Humans ; Homocysteine/metabolism ; Homocysteine/chemistry ; Catalysis
Chemical Substances	Cystathionine gamma-Lyase (EC 4.4.1.1) ; Hydrogen Sulfide (YY9FVM7NSN) ; Cysteine (K848JZ4886) ; Bacterial Proteins ; Homocysteine (0LVT1QZ0BA)
Language	English
Publishing date	2024-04-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-024-57625-7
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Article ; Online: Analysis and Interpretation of the Impact of Missense Variants in Cancer.

Petrosino, Maria / Novak, Leonore / Pasquo, Alessandra / Chiaraluce, Roberta / Turina, Paola / Capriotti, Emidio / Consalvi, Valerio

International journal of molecular sciences

2021 Volume 22, Issue 11

Abstract: Large scale genome sequencing allowed the identification of a massive number of genetic variations, whose impact on human health is still unknown. In this review we analyze, by an in silico-based strategy, the impact of missense variants on cancer- ... ...

Abstract	Large scale genome sequencing allowed the identification of a massive number of genetic variations, whose impact on human health is still unknown. In this review we analyze, by an in silico-based strategy, the impact of missense variants on cancer-related genes, whose effect on protein stability and function was experimentally determined. We collected a set of 164 variants from 11 proteins to analyze the impact of missense mutations at structural and functional levels, and to assess the performance of state-of-the-art methods (FoldX and Meta-SNP) for predicting protein stability change and pathogenicity. The result of our analysis shows that a combination of experimental data on protein stability and in silico pathogenicity predictions allowed the identification of a subset of variants with a high probability of having a deleterious phenotypic effect, as confirmed by the significant enrichment of the subset in variants annotated in the COSMIC database as putative cancer-driving variants. Our analysis suggests that the integration of experimental and computational approaches may contribute to evaluate the risk for complex disorders and develop more effective treatment strategies.
MeSH term(s)	Computational Biology/methods ; Computer Simulation ; Humans ; Mutation, Missense/genetics ; Neoplasms/genetics ; Protein Stability ; Proteins/genetics
Chemical Substances	Proteins
Language	English
Publishing date	2021-05-21
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms22115416
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Article ; Online: Epigallocatechin gallate is a potent inhibitor of cystathionine beta-synthase: Structure-activity relationship and mechanism of action.

Zuhra, Karim / Petrosino, Maria / Gupta, Barkha / Panagaki, Theodora / Cecconi, Marco / Myrianthopoulos, Vassilios / Schneiter, Roger / Mikros, Emmanuel / Majtan, Tomas / Szabo, Csaba

Nitric oxide : biology and chemistry

2022 Volume 128, Page(s) 12–24

Abstract: Epigallocatechin gallate (EGCG) is the main bioactive component of green tea. Through screening of a small library of natural compounds, we discovered that EGCG inhibits cystathionine β-synthase (CBS), a major ... ...

Abstract	Epigallocatechin gallate (EGCG) is the main bioactive component of green tea. Through screening of a small library of natural compounds, we discovered that EGCG inhibits cystathionine β-synthase (CBS), a major H
MeSH term(s)	Catechin/analogs & derivatives ; Cystathionine beta-Synthase/metabolism ; Cystathionine gamma-Lyase/metabolism ; Humans ; Hydrogen Sulfide/metabolism ; Phosphates ; Pyridoxal ; Structure-Activity Relationship
Chemical Substances	Phosphates ; Pyridoxal (3THM379K8A) ; Catechin (8R1V1STN48) ; epigallocatechin gallate (BQM438CTEL) ; Cystathionine beta-Synthase (EC 4.2.1.22) ; Cystathionine gamma-Lyase (EC 4.4.1.1) ; Hydrogen Sulfide (YY9FVM7NSN)
Language	English
Publishing date	2022-08-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1362794-6
ISSN	1089-8611 ; 1089-8603
ISSN (online)	1089-8611
ISSN	1089-8603
DOI	10.1016/j.niox.2022.07.007
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