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Article ; Online: Multi-Anticancer Activities of Phytoestrogens in Human Osteosarcoma.

Cimmino, Alessio / Fasciglione, Giovanni Francesco / Gioia, Magda / Marini, Stefano / Ciaccio, Chiara

International journal of molecular sciences

2023 Volume 24, Issue 17

Abstract: Phytoestrogens are plant-derived bioactive compounds with estrogen-like properties. Their potential health benefits, especially in cancer prevention and treatment, have been a subject of considerable research in the past decade. Phytoestrogens exert ... ...

Abstract	Phytoestrogens are plant-derived bioactive compounds with estrogen-like properties. Their potential health benefits, especially in cancer prevention and treatment, have been a subject of considerable research in the past decade. Phytoestrogens exert their effects, at least in part, through interactions with estrogen receptors (ERs), mimicking or inhibiting the actions of natural estrogens. Recently, there has been growing interest in exploring the impact of phytoestrogens on osteosarcoma (OS), a type of bone malignancy that primarily affects children and young adults and is currently presenting limited treatment options. Considering the critical role of the estrogen/ERs axis in bone development and growth, the modulation of ERs has emerged as a highly promising approach in the treatment of OS. This review provides an extensive overview of current literature on the effects of phytoestrogens on human OS models. It delves into the multiple mechanisms through which these molecules regulate the cell cycle, apoptosis, and key pathways implicated in the growth and progression of OS, including ER signaling. Moreover, potential interactions between phytoestrogens and conventional chemotherapy agents commonly used in OS treatment will be examined. Understanding the impact of these compounds in OS holds great promise for developing novel therapeutic approaches that can augment current OS treatment modalities.
MeSH term(s)	Child ; Young Adult ; Humans ; Phytoestrogens/pharmacology ; Phytoestrogens/therapeutic use ; Osteosarcoma/drug therapy ; Apoptosis ; Estrogens ; Bone Neoplasms/drug therapy
Chemical Substances	Phytoestrogens ; Estrogens
Language	English
Publishing date	2023-08-28
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/ijms241713344
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Article ; Online: Role of hemoglobin structural-functional relationships in oxygen transport.

Ciaccio, Chiara / Coletta, Andrea / Coletta, Massimo

Molecular aspects of medicine

2021 Volume 84, Page(s) 101022

Abstract: The molecular mechanism of ... ...

Abstract	The molecular mechanism of O
MeSH term(s)	Binding Sites ; Biological Transport ; Eye/blood supply ; Hemoglobins/chemistry ; Hemoglobins/metabolism ; Humans ; Lung/metabolism ; Oxygen/metabolism ; Retina/anatomy & histology ; Retina/metabolism ; Thermodynamics
Chemical Substances	Hemoglobins ; Oxygen (S88TT14065)
Language	English
Publishing date	2021-09-09
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	197640-0
ISSN	1872-9452 ; 0098-2997
ISSN (online)	1872-9452
ISSN	0098-2997
DOI	10.1016/j.mam.2021.101022
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Article ; Online: Cyclic Stretch-Induced Mechanical Stress Applied at 1 Hz Frequency Can Alter the Metastatic Potential Properties of SAOS-2 Osteosarcoma Cells.

Alloisio, Giulia / Rodriguez, David Becerril / Luce, Marco / Ciaccio, Chiara / Marini, Stefano / Cricenti, Antonio / Gioia, Magda

International journal of molecular sciences

2023 Volume 24, Issue 9

Abstract: Recently, there has been an increasing focus on cellular morphology and mechanical behavior in order to gain a better understanding of the modulation of cell malignancy. This study used uniaxial-stretching technology to select a mechanical regimen able ... ...

Abstract	Recently, there has been an increasing focus on cellular morphology and mechanical behavior in order to gain a better understanding of the modulation of cell malignancy. This study used uniaxial-stretching technology to select a mechanical regimen able to elevate SAOS-2 cell migration, which is crucial in osteosarcoma cell pathology. Using confocal and atomic force microscopy, we demonstrated that a 24 h 0.5% cyclic elongation applied at 1 Hz induces morphological changes in cells. Following mechanical stimulation, the cell area enlarged, developing a more elongated shape, which disrupted the initial nuclear-to-cytoplasm ratio. The peripheral cell surface also increased its roughness. Cell-based biochemical assays and real-time PCR quantification showed that these morphologically induced changes are unrelated to the osteoblastic differentiative grade. Interestingly, two essential cell-motility properties in the modulation of the metastatic process changed following the 24 h 1 Hz mechanical stimulation. These were cell adhesion and cell migration, which, in fact, were dampened and enhanced, respectively. Notably, our results showed that the stretch-induced up-regulation of cell motility occurs through a mechanism that does not depend on matrix metalloproteinase (MMP) activity, while the inhibition of ion-stretch channels could counteract it. Overall, our results suggest that further research on mechanobiology could represent an alternative approach for the identification of novel molecular targets of osteosarcoma cell malignancy.
MeSH term(s)	Humans ; Stress, Mechanical ; Osteosarcoma/genetics ; Cell Movement ; Cell Differentiation ; Ion Channels ; Bone Neoplasms/genetics
Chemical Substances	Ion Channels
Language	English
Publishing date	2023-04-22
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms24097686
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Article ; Online: Ligand-dependent inequivalence of the α and β subunits of ferric human hemoglobin bound to haptoglobin.

Ascenzi, Paolo / De Simone, Giovanna / Ciaccio, Chiara / Coletta, Massimo

Journal of inorganic biochemistry

2019 Volume 202, Page(s) 110814

Abstract: Haptoglobin (Hp) prevents extra-erythrocytic hemoglobin- (Hb-)mediated damage. Hp binds αβ dimers of Hb, displaying heme-based reactivity. Here, kinetics and thermodynamics of cyanide, thiocyanate and imidazole binding to ferric human Hb (Hb(III)), Hb( ... ...

Abstract	Haptoglobin (Hp) prevents extra-erythrocytic hemoglobin- (Hb-)mediated damage. Hp binds αβ dimers of Hb, displaying heme-based reactivity. Here, kinetics and thermodynamics of cyanide, thiocyanate and imidazole binding to ferric human Hb (Hb(III)), Hb(III) dimers complexed with the human Hp phenotypes 1-1 and 2-2 (Hp1-1:Hb(III) and Hp2-2:Hb(III), respectively), and α(III) and β(III) chains are reported and analyzed in parallel with fluoride and azide binding properties (at pH 7.0 and 20.0 °C). Cyanide and fluoride bind to Hb(III), Hp1-1:Hb(III), Hp2-2:Hb(III), α(III), and β(III) with a simple behavior. In contrast, azide, thiocyanate and imidazole binding to Hb(III), Hp1-1:Hb(III) and Hp2-2:Hb(III) follows a two-step process, whereas ligand binding to α(III) and β(III) chains follows a simple behavior. However, azide, thiocyanate and imidazole binding to Hb(III), Hp1-1:Hb(III) and Hp2-2:Hb(III) is characterized by a simple equilibrium, reflecting the compensation of kinetic parameters. The fast and the slow step of azide, thiocyanate and imidazole binding to Hb(III), Hp1-1:Hb(III) and Hp2-2:Hb(III) mirror the ligand binding properties of the β(III) and α(III) chains, respectively. Values of kinetic and thermodynamic parameters for binding of ferric ligands to Hp1-1:Hb(III) and Hp2-2:Hb(III) match very well with those obtained for ligation of Hb(III) and α(III) and β(III) chains, confirming the ligand-dependent kinetic inequivalence of α(III) and β(III) subunits. However, a variation between tetrameric Hb(III) on one side and Hp1-1:Hb(III), Hp2-2:Hb(III), α(III), and β(III) on the other side for the rate-limiting step (likely referable to the dissociation of heme-coordinated H
MeSH term(s)	Haptoglobins/chemistry ; Heme/chemistry ; Hemoglobins/chemistry ; Humans ; Iron/chemistry ; Ligands ; Protein Domains
Chemical Substances	Haptoglobins ; Hemoglobins ; Ligands ; Heme (42VZT0U6YR) ; Iron (E1UOL152H7)
Language	English
Publishing date	2019-09-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	162843-4
ISSN	1873-3344 ; 0162-0134
ISSN (online)	1873-3344
ISSN	0162-0134
DOI	10.1016/j.jinorgbio.2019.110814
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Article ; Online: NO Scavenging through Reductive Nitrosylation of Ferric

De Simone, Giovanna / di Masi, Alessandra / Ciaccio, Chiara / Coletta, Massimo / Ascenzi, Paolo

International journal of molecular sciences

2020 Volume 21, Issue 24

Abstract: Ferric nitrobindins (Nbs) selectively bind NO and catalyze the conversion of peroxynitrite to nitrate. In this study, we show that NO scavenging occurs through the reductive nitrosylation of ... ...

Abstract	Ferric nitrobindins (Nbs) selectively bind NO and catalyze the conversion of peroxynitrite to nitrate. In this study, we show that NO scavenging occurs through the reductive nitrosylation of ferric
MeSH term(s)	Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Hemeproteins/chemistry ; Hemeproteins/metabolism ; Humans ; Kinetics ; Mycobacterium tuberculosis/enzymology ; Nitric Oxide/chemistry ; Nitric Oxide/metabolism ; Oxidation-Reduction ; Peroxynitrous Acid/metabolism ; Protein Binding
Chemical Substances	Bacterial Proteins ; Hemeproteins ; Peroxynitrous Acid (14691-52-2) ; Nitric Oxide (31C4KY9ESH)
Language	English
Publishing date	2020-12-10
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms21249395
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Article ; Online: Effects of Extracellular Osteoanabolic Agents on the Endogenous Response of Osteoblastic Cells.

Alloisio, Giulia / Ciaccio, Chiara / Fasciglione, Giovanni Francesco / Tarantino, Umberto / Marini, Stefano / Coletta, Massimo / Gioia, Magda

Cells

2021 Volume 10, Issue 9

Abstract: The complex multidimensional skeletal organization can adapt its structure in accordance with external contexts, demonstrating excellent self-renewal capacity. Thus, optimal extracellular environmental properties are critical for bone regeneration and ... ...

Abstract	The complex multidimensional skeletal organization can adapt its structure in accordance with external contexts, demonstrating excellent self-renewal capacity. Thus, optimal extracellular environmental properties are critical for bone regeneration and inextricably linked to the mechanical and biological states of bone. It is interesting to note that the microstructure of bone depends not only on genetic determinants (which control the bone remodeling loop through autocrine and paracrine signals) but also, more importantly, on the continuous response of cells to external mechanical cues. In particular, bone cells sense mechanical signals such as shear, tensile, loading and vibration, and once activated, they react by regulating bone anabolism. Although several specific surrounding conditions needed for osteoblast cells to specifically augment bone formation have been empirically discovered, most of the underlying biomechanical cellular processes underneath remain largely unknown. Nevertheless, exogenous stimuli of endogenous osteogenesis can be applied to promote the mineral apposition rate, bone formation, bone mass and bone strength, as well as expediting fracture repair and bone regeneration. The following review summarizes the latest studies related to the proliferation and differentiation of osteoblastic cells, enhanced by mechanical forces or supplemental signaling factors (such as trace metals, nutraceuticals, vitamins and exosomes), providing a thorough overview of the exogenous osteogenic agents which can be exploited to modulate and influence the mechanically induced anabolism of bone. Furthermore, this review aims to discuss the emerging role of extracellular stimuli in skeletal metabolism as well as their potential roles and provide new perspectives for the treatment of bone disorders.
MeSH term(s)	Anabolic Agents/pharmacology ; Animals ; Bone Regeneration ; Cell Differentiation ; Humans ; Mechanotransduction, Cellular ; Osteoblasts/cytology ; Osteoblasts/drug effects ; Signal Transduction
Chemical Substances	Anabolic Agents
Language	English
Publishing date	2021-09-10
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells10092383
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Article ; Online: Oxygen-mediated oxidation of ferrous nitrosylated nitrobindins.

De Simone, Giovanna / di Masi, Alessandra / Fattibene, Paola / Ciaccio, Chiara / Platas-Iglesias, Carlos / Coletta, Massimo / Pesce, Alessandra / Ascenzi, Paolo

Journal of inorganic biochemistry

2021 Volume 224, Page(s) 111579

Abstract: ... The ... ...

Abstract	The O
MeSH term(s)	Animals ; Arabidopsis Proteins/metabolism ; Bacterial Proteins/metabolism ; Ferric Compounds/metabolism ; Ferrous Compounds/metabolism ; Heme/metabolism ; Hemeproteins/metabolism ; Hemoglobins/metabolism ; Horses ; Humans ; Mycobacterium tuberculosis/metabolism ; Myoglobin/metabolism ; Nitric Oxide/metabolism ; Oxidation-Reduction ; Oxygen/metabolism ; Rabbits
Chemical Substances	Arabidopsis Proteins ; Bacterial Proteins ; Ferric Compounds ; Ferrous Compounds ; Hemeproteins ; Hemoglobins ; Myoglobin ; Nitric Oxide (31C4KY9ESH) ; Heme (42VZT0U6YR) ; Oxygen (S88TT14065)
Language	English
Publishing date	2021-08-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	162843-4
ISSN	1873-3344 ; 0162-0134
ISSN (online)	1873-3344
ISSN	0162-0134
DOI	10.1016/j.jinorgbio.2021.111579
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Article ; Online: Haptoglobin: From hemoglobin scavenging to human health.

di Masi, Alessandra / De Simone, Giovanna / Ciaccio, Chiara / D'Orso, Silvia / Coletta, Massimo / Ascenzi, Paolo

Molecular aspects of medicine

2020 Volume 73, Page(s) 100851

Abstract: Haptoglobin (Hp) belongs to the family of acute-phase plasma proteins and represents the most important plasma detoxifier of hemoglobin (Hb). The basic Hp molecule is a tetrameric protein built by two α/β dimers. Each Hp α/β dimer is encoded by a single ... ...

Abstract	Haptoglobin (Hp) belongs to the family of acute-phase plasma proteins and represents the most important plasma detoxifier of hemoglobin (Hb). The basic Hp molecule is a tetrameric protein built by two α/β dimers. Each Hp α/β dimer is encoded by a single gene and is synthesized as a single polypeptide. Following post-translational protease-dependent cleavage of the Hp polypeptide, the α and β chains are linked by disulfide bridge(s) to generate the mature Hp protein. As human Hp gene is characterized by two common Hp1 and Hp2 alleles, three major genotypes can result (i.e., Hp1-1, Hp2-1, and Hp2-2). Hp regulates Hb clearance from circulation by the macrophage-specific receptor CD163, thus preventing Hb-mediated severe consequences for health. Indeed, the antioxidant and Hb binding properties of Hp as well as its ability to stimulate cells of the monocyte/macrophage lineage and to modulate the helper T-cell type 1 and type 2 balance significantly associate with a variety of pathogenic disorders (e.g., infectious diseases, diabetes, cardiovascular diseases, and cancer). Alternative functions of the variants Hp1 and Hp2 have been reported, particularly in the susceptibility and protection against infectious (e.g., pulmonary tuberculosis, HIV, and malaria) and non-infectious (e.g., diabetes, cardiovascular diseases and obesity) diseases. Both high and low levels of Hp are indicative of clinical conditions: Hp plasma levels increase during infections, inflammation, and various malignant diseases, and decrease during malnutrition, hemolysis, hepatic disease, allergic reactions, and seizure disorders. Of note, the Hp:Hb complexes display heme-based reactivity; in fact, they bind several ferrous and ferric ligands, including O
MeSH term(s)	Alleles ; Animals ; Antioxidants/metabolism ; Carrier Proteins ; Disease Susceptibility ; Evolution, Molecular ; Gene Expression Regulation ; Genetic Variation ; Haptoglobins/chemistry ; Haptoglobins/metabolism ; Haptoglobins/physiology ; Heme/chemistry ; Heme/metabolism ; Hemoglobins/chemistry ; Hemoglobins/genetics ; Hemoglobins/metabolism ; Humans ; Immunomodulation ; Oxidation-Reduction ; Protein Binding ; Protein Processing, Post-Translational ; Signal Transduction ; Structure-Activity Relationship
Chemical Substances	Antioxidants ; Carrier Proteins ; Haptoglobins ; Hemoglobins ; haptoglobin-hemoglobin complex ; Heme (42VZT0U6YR)
Language	English
Publishing date	2020-07-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	197640-0
ISSN	1872-9452 ; 0098-2997
ISSN (online)	1872-9452
ISSN	0098-2997
DOI	10.1016/j.mam.2020.100851
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Article ; Online: Hydroxylamine-induced oxidation of ferrous carbonylated truncated hemoglobins from Mycobacterium tuberculosis and Campylobacter jejuni is limited by carbon monoxide dissociation.

Ascenzi, Paolo / Ciaccio, Chiara / Gasperi, Tecla / Pesce, Alessandra / Caporaso, Lucia / Coletta, Massimo

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry

2017 Volume 22, Issue 6, Page(s) 977–986

Abstract: Hydroxylamine (HA) is an oxidant of ferrous globins and its action has been reported to be inhibited by CO, even though this mechanism has not been clarified. Here, kinetics of the HA-mediated oxidation of ferrous carbonylated Mycobacterium tuberculosis ... ...

Abstract	Hydroxylamine (HA) is an oxidant of ferrous globins and its action has been reported to be inhibited by CO, even though this mechanism has not been clarified. Here, kinetics of the HA-mediated oxidation of ferrous carbonylated Mycobacterium tuberculosis truncated hemoglobin N and O (Mt-trHbN(II)-CO and Mt-trHbO(II)-CO, respectively) and Campylobacter jejuni truncated hemoglobin P (Cj-trHbP(II)-CO), at pH 7.2 and 20.0 °C, are reported. Mixing Mt-trHbN(II)-CO, Mt-trHbO(II)-CO, and Cj-trHbP(II)-CO solution with the HA solution brings about absorption spectral changes reflecting the disappearance of the ferrous carbonylated derivatives with the concomitant formation of the ferric species. HA oxidizes irreversibly Mt-trHbN(II)-CO, Mt-trHbO(II)-CO, and Cj-trHbP(II)-CO with the 1:2 stoichiometry. The dissociation of CO turns out to be the rate-limiting step for the oxidation of Mt-trHbN(II)-CO, Mt-trHbO(II)-CO, and Cj-trHbP(II)-CO by HA. Values of the second-order rate constant for HA-mediated oxidation of Mt-trHbN(II)-CO, Mt-trHbO(II)-CO, and Cj-trHbP(II)-CO range between 8.8 × 10
MeSH term(s)	Campylobacter jejuni/chemistry ; Carbon Monoxide/metabolism ; Heme/metabolism ; Hydroxylamine/pharmacology ; Iron/metabolism ; Kinetics ; Mycobacterium tuberculosis/chemistry ; Oxidation-Reduction/drug effects ; Truncated Hemoglobins/chemistry ; Truncated Hemoglobins/metabolism
Chemical Substances	Truncated Hemoglobins ; Hydroxylamine (2FP81O2L9Z) ; Heme (42VZT0U6YR) ; Carbon Monoxide (7U1EE4V452) ; Iron (E1UOL152H7)
Language	English
Publishing date	2017-08
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1464026-0
ISSN	1432-1327 ; 0949-8257
ISSN (online)	1432-1327
ISSN	0949-8257
DOI	10.1007/s00775-017-1476-x
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Article ; Online: Reductive nitrosylation of the cardiolipin-ferric cytochrome c complex.

Ascenzi, Paolo / Marino, Maria / Ciaccio, Chiara / Santucci, Roberto / Coletta, Massimo

IUBMB life

2014 Volume 66, Issue 6, Page(s) 438–447

Abstract: Native horse heart cytochrome c (cytc) displays a very low reactivity toward ligands and does not exhibit catalytic properties. However, upon bovine cardiolipin (CL) binding, cytc achieves myoglobin-like properties. Here, NO binding to CL-cytc(III) ... ...

Abstract	Native horse heart cytochrome c (cytc) displays a very low reactivity toward ligands and does not exhibit catalytic properties. However, upon bovine cardiolipin (CL) binding, cytc achieves myoglobin-like properties. Here, NO binding to CL-cytc(III) between pH 7.2 and 9.5, at 20 °C, is reported. At pH 7.2, CL-cytc(III) undergoes reversible nitrosylation, whereas between pH 7.9 and 9.5 CL-cytc(III) undergoes irreversible reductive nitrosylation leading to the formation of CL-cytc(II)-NO. Over the whole pH range explored, first-order kinetics of NO binding to CL-cytc(III) (k = 9.3 s(-1) ) indicates that ligand binding is limited by the cleavage of the weak heme-Fe distal bond. Between pH 7.9 and 9.5, nitrosylated CL-cytc(III) converts to the ligand-free ferrous derivative (CL-cytc(II)), this process being pH-dependent (hOH- = 3.0 × 10(3) M(-1) s(-1) ). Then, CL-cytc(II) converts to nitrosylated CL-cytc(II), in the presence of NO excess. The value of the second-order rate constant for CL-cytc(II) nitrosylation is essentially pH-independent, the average value of lon being 1.4 × 10(7) M(-1) s(-1) . These results agree with the view that CL-cytc nitrosylation may play a role in apoptosis regulation.
MeSH term(s)	Animals ; Apoptosis/physiology ; Cardiolipins/metabolism ; Cattle ; Cytochromes c/metabolism ; Heme/metabolism ; Horses ; Hydrogen-Ion Concentration ; Iron/metabolism ; Kinetics ; Models, Biological ; Multiprotein Complexes/metabolism ; Myocardium/metabolism ; Nitric Oxide/metabolism ; Oxidation-Reduction
Chemical Substances	Cardiolipins ; Multiprotein Complexes ; Nitric Oxide (31C4KY9ESH) ; Heme (42VZT0U6YR) ; Cytochromes c (9007-43-6) ; Iron (E1UOL152H7)
Language	English
Publishing date	2014-06
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1492141-8
ISSN	1521-6551 ; 1521-6543
ISSN (online)	1521-6551
ISSN	1521-6543
DOI	10.1002/iub.1283
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