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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Endocrinology and Metabolism".

Deadline for manuscript submissions: closed (20 July 2022) | Viewed by 14483

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Special Issue Editor

Dr. María A. Pajares

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Guest Editor

Centro de Investigaciones Biológicas Margarita Salas (CSIC), Madrid, Spain
Interests: amino acid metabolism; one-carbon metabolism; sulfur amino acids and liver disease; homocysteine and hearing loss; structure/function relationships; redox stress; cysteine modifications
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Special Issue Information

Dear Colleagues,

Amino acids are better known as the building blocks of proteins, but their roles extend to the synthesis of other key compounds for the function of any organism and even the post-translational modification of proteins. Among these additional roles, a special place is reserved for the synthesis of S-adenosylmethionine, which seems involved in as many reactions as ATP, but also for the synthesis of neurotransmitters, glutathione, and nucleotides. Pathways of amino acid metabolism are interconnected to recycle essential amino acids, thus guaranteeing their supply under unfavorable conditions, but also with energy metabolism. Vitamins and cations are important for enzymes in these routes, further linking amino acid metabolism to nutrition, an aspect to be considered in pathological states where patients tend to change their habits or decrease their daily food ingestion. Moreover, human mutations in genes involved in amino acid metabolism are constantly being discovered, studied, and linked to a variety of outcomes, including major and rare diseases. This Special Issue is focused on these additional roles of amino acids, how pathological impairments of their metabolism impact cell function, and whether they can be prevented or ameliorated by drugs and/or nutritional interventions.

Dr. María A. Pajares
Guest Editor

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Keywords

amino acid transport
essential amino acids
hearing loss
liver disease
mutations
neurological disorders
oligomerization state
post-translational modifications
protein–protein interactions
structure/function relationships
sulfur amino acids

Published Papers (6 papers)

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Editorial

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4 pages, 221 KiB

Open AccessEditorial

Amino Acid Metabolism and Disease

by María Ángeles Pajares

Int. J. Mol. Sci. 2023, 24(15), 11935; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms241511935 - 26 Jul 2023

Viewed by 1147

Abstract

The origin of life is still a matter of debate, and several hypotheses have been proposed to explain how the building blocks leading to the minimal cell were formed [...] Full article

(This article belongs to the Special Issue Amino Acid Metabolism and Disease)

Research

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13 pages, 980 KiB

Open AccessArticle

Dysregulated Metabolic Pathways in Subjects with Obesity and Metabolic Syndrome

by Fayaz Ahmad Mir, Ehsan Ullah, Raghvendra Mall, Ahmad Iskandarani, Tareq A. Samra, Farhan Cyprian, Aijaz Parray, Meis Alkasem, Ibrahem Abdalhakam, Faisal Farooq and Abdul-Badi Abou-Samra

Int. J. Mol. Sci. 2022, 23(17), 9821; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23179821 - 29 Aug 2022

Cited by 6 | Viewed by 2161

Abstract

Background: Obesity coexists with variable features of metabolic syndrome, which is associated with dysregulated metabolic pathways. We assessed potential associations between serum metabolites and features of metabolic syndrome in Arabic subjects with obesity. Methods: We analyzed a dataset of 39 subjects with obesity only (OBO, n = 18) age-matched to subjects with obesity and metabolic syndrome (OBM, n = 21). We measured 1069 serum metabolites and correlated them to clinical features. Results: A total of 83 metabolites, mostly lipids, were significantly different (p < 0.05) between the two groups. Among lipids, 22 sphingomyelins were decreased in OBM compared to OBO. Among non-lipids, quinolinate, kynurenine, and tryptophan were also decreased in OBM compared to OBO. Sphingomyelin is negatively correlated with glucose, HbA1C, insulin, and triglycerides but positively correlated with HDL, LDL, and cholesterol. Differentially enriched pathways include lysine degradation, amino sugar and nucleotide sugar metabolism, arginine and proline metabolism, fructose and mannose metabolism, and galactose metabolism. Conclusions: Metabolites and pathways associated with chronic inflammation are differentially expressed in subjects with obesity and metabolic syndrome compared to subjects with obesity but without the clinical features of metabolic syndrome. Full article

(This article belongs to the Special Issue Amino Acid Metabolism and Disease)

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17 pages, 5494 KiB

Open AccessArticle

Insights into Domain Organization and Regulatory Mechanism of Cystathionine Beta-Synthase from Toxoplasma gondii

by Carolina Conter, Silvia Fruncillo, Filippo Favretto, Carmen Fernández-Rodríguez, Paola Dominici, Luis Alfonso Martínez-Cruz and Alessandra Astegno

Int. J. Mol. Sci. 2022, 23(15), 8169; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23158169 - 25 Jul 2022

Cited by 4 | Viewed by 1311

Abstract

Cystathionine beta-synthase (CBS) is a key regulator of homocysteine metabolism. Although eukaryotic CBS have a similar domain architecture with a catalytic core and a C-terminal Bateman module, their regulation varies widely across phyla. In human CBS (HsCBS), the C-terminus has an autoinhibitory effect by acting as a cap that avoids the entry of substrates into the catalytic site. The binding of the allosteric modulator AdoMet to this region alleviates this cap, allowing the protein to progress from a basal toward an activated state. The same activation is obtained by artificial removal or heat-denaturation of the Bateman module. Recently, we reported the crystal structure of CBS from Toxoplasma gondii (TgCBS) showing that the enzyme assembles into basket-like dimers similar to the basal conformers of HsCBS. These findings would suggest a similar lid function for the Bateman module which, as in HsCBS, should relax in the absence of the C-terminal module. However, herein we demonstrate that, in contrast with HsCBS, removal of the Bateman module in TgCBS through deletion mutagenesis, limited proteolysis, or thermal denaturation has no effects on its activity, oligomerization, and thermal stability. This opposite behavior we have now found in TgCBS provides evidence of a novel type of CBS regulation. Full article

(This article belongs to the Special Issue Amino Acid Metabolism and Disease)

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23 pages, 5898 KiB

Open AccessArticle

Polar Interactions at the Dimer–Dimer Interface of Methionine Adenosyltransferase MAT I Control Tetramerization

by Gabino Francisco Sánchez-Pérez and María Ángeles Pajares

Int. J. Mol. Sci. 2021, 22(24), 13206; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms222413206 - 08 Dec 2021

Cited by 1 | Viewed by 2059

Abstract

Catalytic MATα1 subunits associate into kinetically distinct homo-dimers (MAT III) and homo-tetramers (MAT I) that synthesize S-adenosylmethionine in the adult liver. Pathological reductions in S-adenosylmethionine levels correlate with MAT III accumulation; thus, it is important to know the determinants of dimer–dimer associations. Here, polar interactions (<3.5 Å) at the rat MAT I dimer–dimer interface were disrupted by site-directed mutagenesis. Heterologous expression rendered decreased soluble mutant MATα1 levels that appeared mostly as dimers. Substitutions at the B1–B2 or B3–C1 β-strand loops, or changes in charge on helix α2 located behind, induced either MAT III or MAT I accumulation. Notably, double mutants combining neutral changes on helix α2 with substitutions at either β-strand loop further increased MAT III content. Mutations had negligible impact on secondary or tertiary protein structure, but induced changes of 5–10 °C in thermal stability. All mutants preserved tripolyphosphatase activity, although AdoMet synthesis was only detected in single mutants. Kinetic parameters were altered in all purified proteins, their AdoMet synthesis V_max and methionine affinities correlating with the association state induced by the corresponding mutations. In conclusion, polar interactions control MATα1 tetramerization and kinetics, diverse effects being induced by changes on opposite β-sheet loops putatively leading to subtle variations in central domain β-sheet orientation. Full article

(This article belongs to the Special Issue Amino Acid Metabolism and Disease)

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13 pages, 2745 KiB

Open AccessArticle

The Influence of UV Varnishes on the Content of Cysteine and Methionine in Women Nail Plates—Chromatographic Studies

by Kamila Borowczyk and Rafał Głowacki

Int. J. Mol. Sci. 2021, 22(22), 12447; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms222212447 - 18 Nov 2021

Cited by 1 | Viewed by 1688

Abstract

The main purpose of this work was to determine if the use of hybrid nail polishes causes changes in concentration of the most important sulfur amino acids that build nail plate structures, cysteine and methionine. We found that the average contents of cysteine and methionine in studied samples before the use of hybrid manicure were 1275.3 ± 145.9 nmol mg⁻¹ and 111.7 ± 23.8 nmol mg⁻¹, respectively. After six months of hybrid manicure use, the average amount of these sulfur amino acids in studied samples were 22.1% and 36.5% lower in the case of cysteine and methionine, respectively. The average amounts of cysteine and methionine in nail plate samples after the use of hybrid manicures were 992.4 ± 96.2 nmol mg⁻¹ and 70.9 ± 14.8 nmol mg⁻¹, respectively. We also confirmed that in studied women the application of UV light varnishes reduced the thickness of the nail plate, from 0.50 ± 0.12 mm before to 0.46 ± 0.12 mm after the use of the hybrid manicure. Full article

(This article belongs to the Special Issue Amino Acid Metabolism and Disease)

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Review

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11 pages, 1262 KiB

Open AccessReview

Role of Essential Amino Acids in Age-Induced Bone Loss

by Ziquan Lv, Wenbiao Shi and Qian Zhang

Int. J. Mol. Sci. 2022, 23(19), 11281; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms231911281 - 24 Sep 2022

Cited by 16 | Viewed by 4904

Abstract

Age-induced osteoporosis is a global problem. Essential amino acids (EAAs) work as an energy source and a molecular pathway modulator in bone, but their functions have not been systematically reviewed in aging bone. This study aimed to discuss the contribution of EAAs on aging bone from in vitro, in vivo, and human investigations. In aged people with osteoporosis, serum EAAs were detected changing up and down, without a well-established conclusion. The supply of EAAs in aged people either rescued or did not affect bone mineral density (BMD) and bone volume. In most signaling studies, EAAs were proven to increase bone mass. Lysine, threonine, methionine, tryptophan, and isoleucine can increase osteoblast proliferation, activation, and differentiation, and decrease osteoclast activity. Oxidized L-tryptophan promotes bone marrow stem cells (BMSCs) differentiating into osteoblasts. However, the oxidation product of tryptophan called kynurenine increases osteoclast activity, and enhances the differentiation of adipocytes from BMSCs. Taken together, in terms of bone minerals and volume, more views consider EAAs to have a positive effect on aging bone, but the function of EAAs in bone metabolism has not been fully demonstrated and more studies are needed in this area in the future. Full article

(This article belongs to the Special Issue Amino Acid Metabolism and Disease)

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