The multifaceted role of proteases and modern analytical methods for investigation of their catalytic activity
Biochimie. 2024 Mar 15:S0300-9084(24)00064-6. doi: 10.1016/j.biochi.2024.03.006. Online ahead of print.ABSTRACTWe discuss the diverse functions of proteases in the context of their biotechnological and medical significance, as well as analytical approaches used to determine the functional activity of these enzymes. An insight into modern approaches to studying the kinetics and specificity of proteases, based on spectral (absorption, fluorescence), mass spectrometric, immunological, calorimetric, and electrochemical methods of analysis is given. We also examine in detail electrochemical systems for determining the activity ...
Source: Biochimie - March 17, 2024 Category: Biochemistry Authors: Tatiana A Filippova Rami A Masamrekh Yulia Yu Khudoklinova Victoria V Shumyantseva Alexey V Kuzikov Source Type: research

Short-term exposure to cigarette smoke upregulates cathepsin S and alters expression of tight junction ZO-1
Biochimie. 2024 Mar 15:S0300-9084(24)00063-4. doi: 10.1016/j.biochi.2024.03.005. Online ahead of print.ABSTRACTA long-term exposure to cigarette smoke (CS) alters the integrity of airway epithelial barrier, contributes to lung dysfunction, and elicits the expression and activity of lung cathepsin S (CatS), a cysteine protease that participates in the remodeling of connective tissue and cell junctions. Here, we observed that a short-term (4 days) exposure of mice to CS increased the expression and activity of CatS, while the expression level of zonula occludens 1 (ZO-1), an epithelial tight junction protein that stabilizes ...
Source: Biochimie - March 17, 2024 Category: Biochemistry Authors: Florent Estur Emilie Murigneux Alexis David M élia Magnen Ahlame Saidi Gilles Lalmanach Fabien Lecaille Source Type: research

The mutual and dynamic role of TSPO and ligands in their binding process: An example with PK-11195
Biochimie. 2024 Mar 15:S0300-9084(24)00067-1. doi: 10.1016/j.biochi.2024.03.009. Online ahead of print.ABSTRACTTranslocator protein (TSPO) is an 18 kDa transmembrane protein, localized primarily on the outer mitochondrial membrane. It has been found to be involved in various physiological processes and pathophysiological conditions. Though studies on its structure have been performed only recently, there is little information on the nature of dynamics and doubts about some structures referenced in the literature, especially the NMR structure of mouse TSPO. In the present work, we thoroughly study the dynamics of mouse TSPO...
Source: Biochimie - March 17, 2024 Category: Biochemistry Authors: Rajas M Rao Ibaa El Dhaybi Fr édéric Cadet Catherine Etchebest Julien Diharce Source Type: research

The molecular crosstalk of the hippo cascade in breast cancer: A potential central susceptibility
Biochimie. 2024 Mar 15:S0300-9084(24)00066-X. doi: 10.1016/j.biochi.2024.03.008. Online ahead of print.ABSTRACTThe incidence of breast cancer is perpetually growing globally, and it remains a major public health problem and the leading cause of mortality in women. Though the aberrant activities of the Hippo pathway have been reported to be associated with cancer, constructive knowledge of the pathway connecting the various elements of breast cancer remains to be elucidated. The Hippo transducers, yes-associated protein (YAP) and transcriptional co-activator with PDZ binding motif (TAZ), are reported to be either tumor supp...
Source: Biochimie - March 17, 2024 Category: Biochemistry Authors: Sulfath Thottungal Parambil Gisha Rose Antony Ajeesh Babu Littleflower Lakshmi Subhadradevi Source Type: research

Unraveling the impact of the p.R107L mutation on the structure and function of human αB-Crystallin: Implications for cataract formation
In this study, we investigated the structure, chaperone function, stability, oligomerization, and amyloidogenic properties of the p.R107L human αB-Crystallin using a number of different techniques. Our results suggest that the p.R107L mutation can cause significant changes in the secondary, tertiary, and quaternary structures of αB-Crystallin. This cataractogenic mutation led to the formation of protein oligomers with larger sizes than the wild-type protein and reduced the chemical and thermal stability of the mutant chaperone. Both fluorescence and microscopic assessments indicated that this mutation significantly alter...
Source: Biochimie - March 17, 2024 Category: Biochemistry Authors: Farid Nasiri Parisa Ebrahimi Mohammad Bagher Shahsavani Anis Barati Issa Zarei Jun Hong Masaru Hoshino Ali Akbar Moosavi-Movahedi Reza Yousefi Source Type: research

N-terminal processing by dipeptidyl peptidase 9: Cut and Go!
Biochimie. 2024 Mar 8:S0300-9084(24)00052-X. doi: 10.1016/j.biochi.2024.03.002. Online ahead of print.ABSTRACTDipeptidyl peptidase 9 (DPP9) is an intracellular amino-dipeptidase with physiological roles in the immune system, DNA repair and mitochondria homeostasis, while its deregulation is linked to cancer progression and immune-associated defects. Through its rare ability to cleave a peptide bond following the imino-acid proline, DPP9 acts as a molecular switch that regulates key proteins, such as the tumor-suppressor BRCA2. In this review we will discuss key concepts underlying the outcomes of protein processing by DPP9...
Source: Biochimie - March 10, 2024 Category: Biochemistry Authors: Samuel Zolg Laura Donzelli Ruth Geiss-Friedlander Source Type: research

N-terminal processing by dipeptidyl peptidase 9: Cut and Go!
Biochimie. 2024 Mar 8:S0300-9084(24)00052-X. doi: 10.1016/j.biochi.2024.03.002. Online ahead of print.ABSTRACTDipeptidyl peptidase 9 (DPP9) is an intracellular amino-dipeptidase with physiological roles in the immune system, DNA repair and mitochondria homeostasis, while its deregulation is linked to cancer progression and immune-associated defects. Through its rare ability to cleave a peptide bond following the imino-acid proline, DPP9 acts as a molecular switch that regulates key proteins, such as the tumor-suppressor BRCA2. In this review we will discuss key concepts underlying the outcomes of protein processing by DPP9...
Source: Biochimie - March 10, 2024 Category: Biochemistry Authors: Samuel Zolg Laura Donzelli Ruth Geiss-Friedlander Source Type: research

N-terminal processing by dipeptidyl peptidase 9: Cut and Go!
Biochimie. 2024 Mar 8:S0300-9084(24)00052-X. doi: 10.1016/j.biochi.2024.03.002. Online ahead of print.ABSTRACTDipeptidyl peptidase 9 (DPP9) is an intracellular amino-dipeptidase with physiological roles in the immune system, DNA repair and mitochondria homeostasis, while its deregulation is linked to cancer progression and immune-associated defects. Through its rare ability to cleave a peptide bond following the imino-acid proline, DPP9 acts as a molecular switch that regulates key proteins, such as the tumor-suppressor BRCA2. In this review we will discuss key concepts underlying the outcomes of protein processing by DPP9...
Source: Biochimie - March 10, 2024 Category: Biochemistry Authors: Samuel Zolg Laura Donzelli Ruth Geiss-Friedlander Source Type: research

N-terminal processing by dipeptidyl peptidase 9: Cut and Go!
Biochimie. 2024 Mar 8:S0300-9084(24)00052-X. doi: 10.1016/j.biochi.2024.03.002. Online ahead of print.ABSTRACTDipeptidyl peptidase 9 (DPP9) is an intracellular amino-dipeptidase with physiological roles in the immune system, DNA repair and mitochondria homeostasis, while its deregulation is linked to cancer progression and immune-associated defects. Through its rare ability to cleave a peptide bond following the imino-acid proline, DPP9 acts as a molecular switch that regulates key proteins, such as the tumor-suppressor BRCA2. In this review we will discuss key concepts underlying the outcomes of protein processing by DPP9...
Source: Biochimie - March 10, 2024 Category: Biochemistry Authors: Samuel Zolg Laura Donzelli Ruth Geiss-Friedlander Source Type: research

N-terminal processing by dipeptidyl peptidase 9: Cut and Go!
Biochimie. 2024 Mar 8:S0300-9084(24)00052-X. doi: 10.1016/j.biochi.2024.03.002. Online ahead of print.ABSTRACTDipeptidyl peptidase 9 (DPP9) is an intracellular amino-dipeptidase with physiological roles in the immune system, DNA repair and mitochondria homeostasis, while its deregulation is linked to cancer progression and immune-associated defects. Through its rare ability to cleave a peptide bond following the imino-acid proline, DPP9 acts as a molecular switch that regulates key proteins, such as the tumor-suppressor BRCA2. In this review we will discuss key concepts underlying the outcomes of protein processing by DPP9...
Source: Biochimie - March 10, 2024 Category: Biochemistry Authors: Samuel Zolg Laura Donzelli Ruth Geiss-Friedlander Source Type: research

N-terminal processing by dipeptidyl peptidase 9: Cut and Go!
Biochimie. 2024 Mar 8:S0300-9084(24)00052-X. doi: 10.1016/j.biochi.2024.03.002. Online ahead of print.ABSTRACTDipeptidyl peptidase 9 (DPP9) is an intracellular amino-dipeptidase with physiological roles in the immune system, DNA repair and mitochondria homeostasis, while its deregulation is linked to cancer progression and immune-associated defects. Through its rare ability to cleave a peptide bond following the imino-acid proline, DPP9 acts as a molecular switch that regulates key proteins, such as the tumor-suppressor BRCA2. In this review we will discuss key concepts underlying the outcomes of protein processing by DPP9...
Source: Biochimie - March 10, 2024 Category: Biochemistry Authors: Samuel Zolg Laura Donzelli Ruth Geiss-Friedlander Source Type: research

Exploring ligand interactions with human phosphomannomutases using recombinant bacterial thermal shift assay and biochemical validation
Biochimie. 2024 Mar 6:S0300-9084(24)00049-X. doi: 10.1016/j.biochi.2024.02.011. Online ahead of print.ABSTRACTPMM2-CDG, a disease caused by mutations in phosphomannomutase-2, is the most common congenital disorder of glycosylation. Yet, it still lacks a cure. Targeting phosphomannomutase-2 with pharmacological chaperones or inhibiting the phosphatase activity of phosphomannomutase-1 to enhance intracellular glucose-1,6-bisphosphate have been proposed as therapeutical approaches. We used Recombinant Bacterial Thermal Shift Assay to assess the binding of a substrate analog to phosphomannomutase-2 and the specific binding to ...
Source: Biochimie - March 8, 2024 Category: Biochemistry Authors: Maria Monticelli Bruno Hay Mele Demi Marie Wright Simone Guerriero Giuseppina Andreotti Maria Vittoria Cubellis Source Type: research

Exploring ligand interactions with human phosphomannomutases using recombinant bacterial thermal shift assay and biochemical validation
Biochimie. 2024 Mar 6:S0300-9084(24)00049-X. doi: 10.1016/j.biochi.2024.02.011. Online ahead of print.ABSTRACTPMM2-CDG, a disease caused by mutations in phosphomannomutase-2, is the most common congenital disorder of glycosylation. Yet, it still lacks a cure. Targeting phosphomannomutase-2 with pharmacological chaperones or inhibiting the phosphatase activity of phosphomannomutase-1 to enhance intracellular glucose-1,6-bisphosphate have been proposed as therapeutical approaches. We used Recombinant Bacterial Thermal Shift Assay to assess the binding of a substrate analog to phosphomannomutase-2 and the specific binding to ...
Source: Biochimie - March 8, 2024 Category: Biochemistry Authors: Maria Monticelli Bruno Hay Mele Demi Marie Wright Simone Guerriero Giuseppina Andreotti Maria Vittoria Cubellis Source Type: research

Enhancement of intrinsic guanine fluorescence by protonation in DNA of various structures
Biochimie. 2024 Mar 4;222:101-108. doi: 10.1016/j.biochi.2024.03.003. Online ahead of print.ABSTRACTUnderstanding the diversity of DNA structure and functions in biology requires tools to study this biomolecule selectively and thoroughly. Fluorescence methods are powerful technique for non-invasive research. Due to the low quantum yield, the intrinsic fluorescence of nucleotides has not been considered for use in the detection and differentiation of nucleic acid bases. Here, we have studied the influence of protonation of nucleotides on their fluorescence properties. We show that protonation of ATP and GTP leads to enhance...
Source: Biochimie - March 6, 2024 Category: Biochemistry Authors: Liana L Tevonyan Natalia P Bazhulina Dmitry N Kaluzhny Source Type: research

Enhancement of intrinsic guanine fluorescence by protonation in DNA of various structures
Biochimie. 2024 Mar 4:S0300-9084(24)00053-1. doi: 10.1016/j.biochi.2024.03.003. Online ahead of print.ABSTRACTUnderstanding the diversity of DNA structure and functions in biology requires tools to study this biomolecule selectively and thoroughly. Fluorescence methods are powerful technique for non-invasive research. Due to the low quantum yield, the intrinsic fluorescence of nucleotides has not been considered for use in the detection and differentiation of nucleic acid bases. Here, we have studied the influence of protonation of nucleotides on their fluorescence properties. We show that protonation of ATP and GTP leads ...
Source: Biochimie - March 6, 2024 Category: Biochemistry Authors: Liana L Tevonyan Natalia P Bazhulina Dmitry N Kaluzhny Source Type: research