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Biomolecular Basis of Life Processes

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

Deadline for manuscript submissions: 20 August 2025 | Viewed by 7329

Special Issue Editor


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Guest Editor
Jerzy Kukuczka Academy of Physical Education, 40-065 Katowice, Poland
Interests: aging processes; systemic homeostasis; energy metabolism; neurodegeneration; cellular turnover; pathology of cancers
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Special Issue Information

Dear Colleagues,

The phenomenon of life is an extraordinary challenge for modern science. Energy metabolism is the basis of all biological processes occurring in living organisms. Maintaining a balanced energy metabolism is therefore one of the pillars of life. In addition, the proper functioning and health of a human being depend on the ability of their body to obtain several essential nutrients and trace elements from the environment, which allow for maintaining homeostasis at the cellular and tissue level. A special role here is played by calcium and phosphate signaling. An important but so far underestimated attribute of life is the adaptation of a living organism to the natural environment and its interaction with the intestinal and epithelial microbiota. In recent years, the problem of the role of motor activity has also emerged and in particular bone–muscle interaction and cellular turnover. Disturbances and the dysregulation of all these processes underlie the pathology of old age: metabolic syndrome and cancer. Our holistic approach to the problems of aging and geriatric problems will allow modern medicine to improve the quality of life of the rapidly aging human population.

Prof. Dr. Janusz Błaszczyk
Guest Editor

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Keywords

  • energy metabolism
  • bone-muscle interaction
  • ATP signalling
  • calcium–phosphate signalling
  • metabolic syndrome
  • aging
  • cellular turnover
  • cancers

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Published Papers (3 papers)

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Research

11 pages, 233 KiB  
Article
Association Between Telomere Shortening and Erythropoietin Resistance in Patients with Chronic Kidney Disease Undergoing Hemodialysis
by Blanca Olivia Murillo-Ortiz, Marcos Javier Romero-Vázquez, Angélica Jeanette Luevanos-Aguilera, Paulina Monserrat Meza-Herrán, Edna Montserrat Ramos-Rodriguez, Sandra Martínez-Garza and Mario Murguia-Perez
Int. J. Mol. Sci. 2025, 26(7), 3405; https://doi.org/10.3390/ijms26073405 - 5 Apr 2025
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Abstract
The relationship between telomere shortening and patients with chronic kidney disease (CKD) has recently been investigated. Although most patients respond adequately to erythropoiesis-stimulating agents (ESAs), approximately 10% do not, and this is referred to as ESA resistance. The aim of our study was [...] Read more.
The relationship between telomere shortening and patients with chronic kidney disease (CKD) has recently been investigated. Although most patients respond adequately to erythropoiesis-stimulating agents (ESAs), approximately 10% do not, and this is referred to as ESA resistance. The aim of our study was to investigate the relationship between telomere shortening and erythropoietin resistance in patients with CKD on hemodialysis. This cross-sectional, comparative, analytical, and observational study was conducted in patients of both sexes over 18 years of age diagnosed with CKD. Two groups of patients were identified. The first group consisted of 40 patients receiving erythropoiesis-stimulating agents with erythropoietin resistance. The second group consisted of 40 patients with the same characteristics but without erythropoietin resistance. Telomere length was measured by real-time PCR. Eighty patients were included in the study. Mean hemoglobin levels were lower in the erythropoietin resistance group (8.8 ± 1.67 vs. 11.95 ± 1.81, p = 0.001). Differences were observed in hematocrit and albumin levels, which were lower in patients with erythropoietin resistance, while PTH levels were higher in this group (788 ± 538.47 vs. 535.65 ± 603.06, p = 0.001). A significant difference in telomere length (T/S) was observed between the two groups, with shorter telomere length in the erythropoietin resistance group (0.45 ± 0.04 vs. 0.56 ± 0.03, p = 0.01). Telomere shortening may be associated with anemia and erythropoietin resistance in patients with CKD undergoing hemodialysis. This relationship suggests the need to explore whether telomere length recovery improves the response to ESAs. Full article
(This article belongs to the Special Issue Biomolecular Basis of Life Processes)
13 pages, 2021 KiB  
Article
Effect of Combining Exercise with Adipose-Derived Mesenchymal Stem Cells in Muscle Atrophy Model of Sarcopenia
by Dong-Hwa Jeong, Min-Jeong Kim and Chul-Hyun Park
Int. J. Mol. Sci. 2025, 26(2), 451; https://doi.org/10.3390/ijms26020451 - 7 Jan 2025
Viewed by 3329
Abstract
Deterioration in muscle mass, strength, and physical performance due to conditions such as sarcopenia can affect daily activities and quality of life in the elderly. Exercise and mesenchymal stem cells (MSCs) are potential therapies for sarcopenia. This study evaluates the combined effects of [...] Read more.
Deterioration in muscle mass, strength, and physical performance due to conditions such as sarcopenia can affect daily activities and quality of life in the elderly. Exercise and mesenchymal stem cells (MSCs) are potential therapies for sarcopenia. This study evaluates the combined effects of exercise and adipose-derived MSCs (ADMSCs) in aged rats with sarcopenia. Eighteen-month-old rats were randomly divided into four groups: control, exercise (Ex), ADMSCs injection (MSC), and ADMSCs injection with exercise (MSC + Ex). Gastrocnemius (GCM) muscle mass increased in the Ex, MSC, and MSC + Ex groups compared to the control group. Although the mean CSA did not differ significantly between the groups, the size distribution of myofibers shifted toward larger sizes in the Ex and MSC + Ex groups. The MSC + Ex group performed best in functional tests, including the rotarod and hot plate tests. The protein expression levels of tumor necrosis factor (TNF) and the p-AMP-activated protein kinase (AMPK)/AMPK ratio in the GCM muscle were the lowest in the MSC + Ex group. This study demonstrates that combining exercise and ADMSC interventions was the most effective treatment for aged sarcopenic rats, suggesting a potential synergistic approach for sarcopenia treatment. Full article
(This article belongs to the Special Issue Biomolecular Basis of Life Processes)
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20 pages, 3448 KiB  
Article
Homeodomain Involvement in Nuclear HOX Protein Homo- and Heterodimerization
by Damien Marchese, Laetitia Evrard, Isabelle Bergiers, Ludovic Boas, Justine Duphénieux, Maryse Hermant, Tamara Pringels, Fisnik Zeqiri, Marc Pirson, Jean-Claude Twizere, Françoise Gofflot, René Rezsohazy and Laure Bridoux
Int. J. Mol. Sci. 2025, 26(1), 423; https://doi.org/10.3390/ijms26010423 - 6 Jan 2025
Viewed by 3138
Abstract
HOX genes play essential roles in patterning the anteroposterior axis of animal embryos and in the formation of various organs. In mammals, there are 39 HOX genes organized into four clusters (HOXA–D) located on different chromosomes. In relationship with their orderly arrangement along [...] Read more.
HOX genes play essential roles in patterning the anteroposterior axis of animal embryos and in the formation of various organs. In mammals, there are 39 HOX genes organized into four clusters (HOXA–D) located on different chromosomes. In relationship with their orderly arrangement along the chromosomes, these genes show nested expression patterns which imply that embryonic territories co-express multiple HOX genes along the main body axis. Interactomic database entries, as well as a handful of publications, support that some HOX proteins can form homodimers or interact with other HOX proteins. However, the consequences of HOX protein interactions have been poorly investigated and remain largely elusive. In this study, we compiled a repository of all HOX–HOX interactions from available databases, and taking HOXA1, HOXA2, and HOXA5 as examples, we investigated the capacity of HOX proteins to form homo- and heterodimers. We revealed that while the DNA-binding domain, the homeodomain, is not necessary for HOXA1 homodimerization, the nuclear localization of the dimerization is dependent on the homeodomain, particularly the integrity of the third helix of HOXA1. Furthermore, we demonstrated that HOXA1 can influence the localization of HOXA1 when it is deprived of the homeodomain, increasing its abundance in the chromatin-containing fraction. Moreover, HOXA1 nuclear homodimerization occurs independently of the integrity of the hexapeptide and, consequently, of its well-known interactor, the homeodomain protein PBX. These results hint at a potential involvement of dimerization in the complex landscape of HOX regulatory mechanisms. Full article
(This article belongs to the Special Issue Biomolecular Basis of Life Processes)
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