BBA AdvancesPub Date : 2024-01-01Epub Date: 2023-12-21DOI: 10.1016/j.bbadva.2023.100112
Catarina Barbosa , Carolina F. Rodrigues , Nikola Lončar , Lígia O. Martins , Smilja Todorovic , Célia M. Silveira
{"title":"Spectroelectrochemistry for determination of the redox potential in heme enzymes: Dye-decolorizing peroxidases","authors":"Catarina Barbosa , Carolina F. Rodrigues , Nikola Lončar , Lígia O. Martins , Smilja Todorovic , Célia M. Silveira","doi":"10.1016/j.bbadva.2023.100112","DOIUrl":"10.1016/j.bbadva.2023.100112","url":null,"abstract":"<div><p>Dye-decolorizing peroxidases (DyPs) are heme-containing enzymes that are structurally unrelated to other peroxidases. Some DyPs show high potential for applications in biotechnology, which critically depends on the stability and redox potential (E°') of the enzyme. Here we provide a comparative analysis of UV–Vis- and surface-enhanced resonance Raman-based spectroelectrochemical methods for determination of the E°' of DyPs from two different organisms, and their variants generated targeting E°' upshift. We show that substituting the highly conserved Arginine in the distal side of the heme pocket by hydrophobic amino acid residues impacts the heme architecture and redox potential of DyPs from the two organisms in a very distinct manner. We demonstrate the advantages and drawbacks of the used spectroelectrochemical approaches, which is relevant for other heme proteins that contain multiple heme centers or spin populations.</p></div>","PeriodicalId":34672,"journal":{"name":"BBA Advances","volume":"5 ","pages":"Article 100112"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2667160323000418/pdfft?md5=8419855c4edb70fa4f28249071742bfe&pid=1-s2.0-S2667160323000418-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138993309","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BBA AdvancesPub Date : 2024-01-01Epub Date: 2024-11-30DOI: 10.1016/j.bbadva.2024.100127
Ishani Sharma, Anup Padmanabhan
{"title":"Mechano-regulation of germline development, maintenance, and differentiation","authors":"Ishani Sharma, Anup Padmanabhan","doi":"10.1016/j.bbadva.2024.100127","DOIUrl":"10.1016/j.bbadva.2024.100127","url":null,"abstract":"<div><div>Biochemical signaling arising from mechanical force-induced physical changes in biological macromolecules is a critical determinant of key physiological processes across all biological lengths and time scales. Recent studies have deepened our understanding of how mechano-transduction regulates somatic tissues such as those in alveolar, gastrointestinal, embryonic, and skeleto-muscular systems. The germline of an organism has a heterogeneous composition - of germ cells at different stages of maturation and mature gametes, often supported and influenced by their accessory somatic tissues. While biochemical signaling underlying germline functioning has been extensively investigated, a deeper interest in their mechanical regulation has been gaining traction in recent years. In this review, we delve into the myriad ways in which germ cell development, maintenance, and functions are regulated by mechanical forces.</div></div>","PeriodicalId":34672,"journal":{"name":"BBA Advances","volume":"6 ","pages":"Article 100127"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11667016/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142885680","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BBA AdvancesPub Date : 2023-08-01DOI: 10.1016/j.bbadva.2023.100098
Gisele Alvarenga Simpson, Isabela Fernandes Rezende, Alencar da Silva Peixoto, Igor Barbosa de Oliveira Soares, J. Barbosa, S. M. de Freitas, N. Valadares
{"title":"Crystal structure and interconversion of monomers and domain-swapped dimers of the walnut tree phytocystatin","authors":"Gisele Alvarenga Simpson, Isabela Fernandes Rezende, Alencar da Silva Peixoto, Igor Barbosa de Oliveira Soares, J. Barbosa, S. M. de Freitas, N. Valadares","doi":"10.1016/j.bbadva.2023.100098","DOIUrl":"https://doi.org/10.1016/j.bbadva.2023.100098","url":null,"abstract":"","PeriodicalId":34672,"journal":{"name":"BBA Advances","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43143953","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Novel dicarbonyl metabolic pathway via mitochondrial ES1 possessing glyoxalase III activity","authors":"Ginga Ito , Yota Tatara , Ken Itoh , Miwa Yamada , Tetsuro Yamashita , Kimitoshi Sakamoto , Takayuki Nozaki , Kinji Ishida , Yui Wake , Takehito Kaneko , Tomokazu Fukuda , Eriko Sugano , Hiroshi Tomita , Taku Ozaki","doi":"10.1016/j.bbadva.2023.100092","DOIUrl":"10.1016/j.bbadva.2023.100092","url":null,"abstract":"<div><p>Glycation, caused by reactive dicarbonyls, plays a role in various diseases by forming advanced glycation end products. In live cells, reactive dicarbonyls such as glyoxal (GO) and methylglyoxal (MGO) are produced during cell metabolism, and these should be removed consistently. However, the dicarbonyl metabolic system in the mitochondria remains unclear. It has been speculated that the mammalian mitochondrial protein ES1 is a homolog of bacterial elbB possessing glyoxalase III (GLO3) activity. Therefore, in this study, to investigate ES1 functions and GLO3 activity, we generated <em>ES1</em>-knockout (KO) mice and recombinant mouse ES1 protein and investigated the biochemical and histological analyses. In the mitochondrial fraction obtained from <em>ES1</em>-KO mouse brains, the GO metabolism and cytochrome c oxidase activity were significantly lower than those in the mitochondrial fraction obtained from wildtype (WT) mouse brains. However, the morphological features of the mitochondria did not change noticeably in the <em>ES1</em>-KO mouse brains compared with those in the WT mouse brains. The mitochondrial proteome analysis showed that the MGO degradation III pathway and oxidative phosphorylation-related proteins were increased. These should be the response to the reduced GO metabolism caused by <em>ES1</em> deletion to compensate for the dicarbonyl metabolism and damaged cytochrome c oxidase by elevated GO. Recombinant mouse ES1 protein exhibited catalytic activity of converting GO to glycolic acid. These results indicate that ES1 possesses GLO3 activity and modulates the metabolism of GO in the mitochondria. To our knowledge, this is the first study to show a novel metabolic pathway for reactive dicarbonyls in mitochondria.</p></div>","PeriodicalId":34672,"journal":{"name":"BBA Advances","volume":"3 ","pages":"Article 100092"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/cf/01/main.PMC10209487.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9545670","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BBA AdvancesPub Date : 2023-01-01Epub Date: 2023-02-14DOI: 10.1016/j.bbadva.2023.100083
Barend O.W. Elenbaas , Stefanie M. Kremsreiter , Lucie Khemtemourian , J. Antoinette Killian , Tessa Sinnige
{"title":"Fibril elongation by human islet amyloid polypeptide is the main event linking aggregation to membrane damage","authors":"Barend O.W. Elenbaas , Stefanie M. Kremsreiter , Lucie Khemtemourian , J. Antoinette Killian , Tessa Sinnige","doi":"10.1016/j.bbadva.2023.100083","DOIUrl":"10.1016/j.bbadva.2023.100083","url":null,"abstract":"<div><p>The aggregation of human islet amyloid polypeptide (hIAPP) is linked to the death of pancreatic β-cells in type II diabetes. The process of fibril formation by hIAPP is thought to cause membrane damage, but the precise mechanisms are still unclear. Previously, we showed that the aggregation of hIAPP in the presence of membranes containing anionic lipids is dominated by secondary nucleation events, which occur at the interface between existing fibrils and the membrane surface. Here, we used vesicles with different lipid composition to explore the connection between hIAPP aggregation and vesicle leakage. We found that different anionic lipids promote hIAPP aggregation to the same extent, whereas remarkably stochastic behaviour is observed on purely zwitterionic membranes. Vesicle leakage induced by hIAPP consists of two distinct phases for any of the used membrane compositions: (i) an initial phase in which hIAPP binding causes a certain level of leakage that is strongly dependent on osmotic conditions, membrane composition and the used dye, and (ii) a main leakage event that we attribute to elongation of hIAPP fibrils, based on seeded experiments. Altogether, our results shed more light on the relationship between hIAPP fibril formation and membrane damage, and strongly suggest that oligomeric intermediates do not considerably contribute to vesicle leakage.</p></div>","PeriodicalId":34672,"journal":{"name":"BBA Advances","volume":"3 ","pages":"Article 100083"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10074975/pdf/main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9379196","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BBA AdvancesPub Date : 2023-01-01Epub Date: 2022-12-20DOI: 10.1016/j.bbadva.2022.100069
Igor B. Philyppov, Ganna V. Sotkis, Bizhan R. Sharopov, Anastasiia O. Danshyna, Semen I. Yelyashov, Valeri G. Naidenov, Olga P. Lyubanova, Yaroslav M. Shuba
{"title":"Temperature-dependent contractility of rat tunica dartos muscle: Contribution of cold, menthol-sensitive TRPM8","authors":"Igor B. Philyppov, Ganna V. Sotkis, Bizhan R. Sharopov, Anastasiia O. Danshyna, Semen I. Yelyashov, Valeri G. Naidenov, Olga P. Lyubanova, Yaroslav M. Shuba","doi":"10.1016/j.bbadva.2022.100069","DOIUrl":"10.1016/j.bbadva.2022.100069","url":null,"abstract":"<div><p>Tunica dartos smooth muscle (TDSM) lies beneath the scrotal skin, and its contraction leads to scrotum wrinkling upon cooling. However, neither the nature of TDSM cold-sensitivity nor the underlying molecular sensors are well understood. Here we have investigated the role of cold/menthol-sensitive TRPM8 channel in TDSM temperature-dependent contractility. The contraction of isolated male rat TDSM strips was studied by tensiometry. TRPM8 expression was assayed by RT-PCR and fluorescence immunochemistry. Isolated TDSM strips responded to cooling from 33 °C to 20 °C by enhancement of basal tension, and increase of the amplitude and duration of electric field stimulated (EFS) contractions. The effects of cold on basal tension, but not on EFS-contractions, could be 80% inhibited by TRPM8 blockers, capsazepine and BCTC [N-(4‑tert-butylphenyl)-4-(3-chloropyridin-2-yl)piperazine-1-carboxamide], and could be partially mimicked by menthol. RT-PCR and immunolabeling showed TRPM8 mRNA and protein expression in TDSM cells with protein labelling being predominantly localized to intracellular compartments. Chemical castration of male rats consequent to the treatment with androgen receptor blocker, flutamide, led to the abrogation of cold effects on TDSM basal tension, but not on EFS-contractions, and to the disappearance of TRPM8 protein expression. We conclude that TRPM8 is involved in the maintenance of basal cold-induced TDSM tonus, but not in sympathetic nerve-mediated contractility, by acting as endoplasmic reticulum Ca<sup>2+</sup> release channel whose expression in TDSM cells requires the presence of a functional androgen receptor. Thus, TRPM8 plays a crucial role in scrotal thermoregulation which is important for maintaining normal spermatogenesis and male fertility.</p></div>","PeriodicalId":34672,"journal":{"name":"BBA Advances","volume":"3 ","pages":"Article 100069"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10074839/pdf/main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9379201","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BBA AdvancesPub Date : 2023-01-01Epub Date: 2023-01-13DOI: 10.1016/j.bbadva.2023.100075
Valeriy Filonenko , Ivan Gout
{"title":"Discovery and functional characterisation of protein CoAlation and the antioxidant function of coenzyme A","authors":"Valeriy Filonenko , Ivan Gout","doi":"10.1016/j.bbadva.2023.100075","DOIUrl":"10.1016/j.bbadva.2023.100075","url":null,"abstract":"<div><p>Coenzyme A (CoA) is an essential cofactor in all living cells which plays critical role in cellular metabolism, the regulation of gene expression and the biosynthesis of major cellular constituents. Recently, CoA was found to function as a major antioxidant in both prokaryotic and eukaryotic cells. This unconventional function of CoA is mediated by a novel post-translational modification, termed protein CoAlation. This review will highlight the history of this discovery, current knowledge, and future directions on studying molecular mechanisms of protein CoAlation and whether the antioxidant function of CoA is associated with pathologies, such as neurodegeneration and cancer.</p></div>","PeriodicalId":34672,"journal":{"name":"BBA Advances","volume":"3 ","pages":"Article 100075"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10074942/pdf/main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9385043","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BBA AdvancesPub Date : 2023-01-01Epub Date: 2022-12-23DOI: 10.1016/j.bbadva.2022.100068
Kyoko Takatsu , Naohiro Kobayashi , Nan Wu , Yves L. Janin , Toshio Yamazaki , Yutaka Kuroda
{"title":"Biophysical analysis of Gaussia luciferase bioluminescence mechanisms using a non-oxidizable coelenterazine","authors":"Kyoko Takatsu , Naohiro Kobayashi , Nan Wu , Yves L. Janin , Toshio Yamazaki , Yutaka Kuroda","doi":"10.1016/j.bbadva.2022.100068","DOIUrl":"https://doi.org/10.1016/j.bbadva.2022.100068","url":null,"abstract":"<div><p><em>Gaussia</em> luciferase (GLuc 18.2kDa; 168 residues) is a marine copepod luciferase that emits a bright blue light when oxidizing coelenterazine (CTZ). It is a helical protein where two homologous sequential repeats form two anti-parallel bundles, each made of four helices. We previously identified a hydrophobic cavity as a prime candidate for the catalytic site, but GLuc's fast bioluminescence reaction hampered a detailed analysis. Here, we used azacoelenterazine (Aza-CTZ), a non-oxidizable coelenterazine (CTZ) analog, as a probe to investigate its binding mode to GLuc. While analysing GLuc's activity, we unexpectedly found that salt and monovalent anions are absolutely required for Gluc's bioluminescence, which retrospectively appears reasonable for a sea-dwelling organism. The NMR-based investigation, using chemical shift perturbations monitored by <sup>15</sup>N-<sup>1</sup>H HSQC, suggested that Aza-CTZ (and thus unoxidized CTZ) binds to residues in or near the hydrophobic cavity. These NMR data are in line with a recent structural prediction of GLuc, hypothesizing that large structural changes occur in regions remote from the hydrophobic cavity upon the addition of CTZ. Interestingly, these results point toward a unique mode of catalysis to achieve CTZ oxidative decarboxylation.</p></div>","PeriodicalId":34672,"journal":{"name":"BBA Advances","volume":"3 ","pages":"Article 100068"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49775971","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BBA AdvancesPub Date : 2023-01-01Epub Date: 2023-01-22DOI: 10.1016/j.bbadva.2023.100079
Paul Voziyan , Sasidhar Uppuganti , Micheal Leser , Kristie L. Rose , Jeffry S. Nyman
{"title":"Mapping glycation and glycoxidation sites in collagen I of human cortical bone","authors":"Paul Voziyan , Sasidhar Uppuganti , Micheal Leser , Kristie L. Rose , Jeffry S. Nyman","doi":"10.1016/j.bbadva.2023.100079","DOIUrl":"10.1016/j.bbadva.2023.100079","url":null,"abstract":"<div><p>Accumulation of advanced glycation end products (AGEs), particularly in long-lived extracellular matrix proteins, has been implicated in pathogenesis of diabetic complications and in aging. Knowledge about specific locations of AGEs and their precursors within protein primary structure is critical for understanding their physiological and pathophysiological impact. However, the information on specific AGE sites is lacking. Here, we identified sequence positions of four major AGEs, carboxymethyllysine, carboxyethyllysine, 5-hydro-5-methyl imidazolone, and 5-hydro-imidazolone, and an AGE precursor fructosyllysine within the triple helical region of collagen I from cortical bone of human femurs. The presented map provides a basis for site-specific quantitation of AGEs and other non-enzymatic post-translational modifications and identification of those sites affected by aging, diabetes, and other diseases such as osteoporosis; it can also help in guiding future studies of AGE impact on structure and function of collagen I in bone.</p></div>","PeriodicalId":34672,"journal":{"name":"BBA Advances","volume":"3 ","pages":"Article 100079"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10074956/pdf/main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9385444","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}