Sub-cellular biochemistry最新文献

{"title":"Applications of Carbonic Anhydrase Inhibitors in Arthritis, Neuropathic Pain, Acute Mountain Sickness, and Cerebral Ischemia.","authors":"Alessio Nocentini, Rashmi Pundeer, Claudiu T Supuran","doi":"10.1007/978-3-032-23172-7_8","DOIUrl":"10.1007/978-3-032-23172-7_8","url":null,"abstract":"<p><p>Carbonic anhydrase inhibitors (CAIs) have long been used as diuretics, topically acting antiglaucoma agents, anticonvulsants, and for the treatment of altitude sickness. Lately, they have shown promising results as anti-obesity, antimicrobial, and mainly antitumor agents. Recent studies have reported the efficacy of CAIs in treating inflammatory conditions such as arthritis and neuropathic pain. Moreover, a polypharmacological profile has been demonstrated for sulfonamide COX-2 inhibitors such as celecoxib, which also effectively inhibit CAs. Additionally, emerging research showed the effectiveness of CAIs in cerebral ischemia, where they help protect brain tissue by modulating pH levels and reducing acidosis-induced neuronal damage.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"123 ","pages":"163-177"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147821025","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":"Introduction to Carbonic Anhydrase.","authors":"Clemente Capasso, Claudiu T Supuran","doi":"10.1007/978-3-032-23172-7_1","DOIUrl":"10.1007/978-3-032-23172-7_1","url":null,"abstract":"<p><p>Carbonic anhydrases (CAs) form a widely distributed superfamily of metalloenzymes, characterized by considerable structural diversity. These enzymes catalyze the reversible conversion of carbon dioxide into bicarbonate and protons. While they all perform this fundamental reaction, CAs show notable structural plasticity, with eight classes (α, β, γ, δ, ζ, η, θ, and ι) that have evolved independently to optimize CO₂ hydration under a range of cellular, physiological, and ecological conditions. Their catalytic efficiency plays a crucial role in several biological processes, including acid-base balance, respiratory gas exchange, renal bicarbonate reabsorption, metabolic regulation, and photosynthetic carbon fixation. Isoform-specific expression allows CAs to act in multiple cellular contexts. They contribute to signaling pathways, help maintain pH balance, function within tissue-specific environments. When these enzymes are not properly regulated, they can be associated with a variety of health issues, including renal tubular acidosis, osteopetrosis, neurological disorders, and cancer progression. Evolution has shaped enzymes in different species to have similar active sites, flexible metal use, and varied protein assemblies, all helping them adapt to challenges like limited metal ions availability and changing CO₂ levels. CAs are not just important in biology. These metalloenzymes are also key targets for treating cancer, eye conditions, and infections. Besides, they show great promise as enzymes for capturing CO₂ and for other biotechnological applications. This chapter offers a thorough introduction to CAs, exploring their biology, how their structures and functions have evolved, and their potential applications, showing how these enzymes link the worlds of science, medicine, and the environment.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"123 ","pages":"1-15"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147821182","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":"Rethinking the Yeast Endomembrane System.","authors":"Benjamin S Glick","doi":"10.1007/978-3-032-06936-8_13","DOIUrl":"10.1007/978-3-032-06936-8_13","url":null,"abstract":"<p><p>The budding yeast Saccharomyces cerevisiae is tremendously useful for revealing basic principles of cell biology. An example is the characterization of the endomembrane system, which consists of secretory, endocytic, and autophagic compartments that exchange material by membrane traffic pathways and undergo dynamic transformations. Yeast studies of this topic continue to uncover components and molecular mechanisms. However, questions persist about high-level features of the yeast endomembrane system, including the identities and life cycles of endocytic compartments and the traffic pathways followed by resident proteins of the Golgi apparatus. Time-lapse imaging of endosome and Golgi compartments points to a new synthesis that revises several long-standing assumptions. This updated picture has implications for understanding conserved aspects of the endomembrane system.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"110 ","pages":"313-333"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12834225/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145522911","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}

{"title":"Unlocking the Epigenetic Landscape of Colorectal Cancer: A Step Toward Epigenetics to Precision.","authors":"Maha M Elbrashy, Sally Farouk, Nadia M Hamdy, Hozaifa Metwally, Noha G Bader El Din","doi":"10.1007/978-3-032-08530-6_4","DOIUrl":"10.1007/978-3-032-08530-6_4","url":null,"abstract":"<p><p>Epigenetic modifications function as central controllers of gene expression in cancer, coordinating crucial cellular activities that trigger the initiation and progression of the tumor, besides their importance in therapeutic response. These modifications can control the gene expression without changing the sequence of DNA. In colorectal cancer (CRC), these alterations involving DNA methylation, histone modifications, chromatin rearrangement, and noncoding ribonucleic acids play a significant role in the pathogenesis of CRC. Abnormal DNA methylation silences the tumor suppressor genes, meanwhile leading to the instability of the genome via reduction of the whole methylation. Specific methylation signatures, such as CpG islands, help in categorizing the subtypes of the tumor and predicting the clinical outcomes. In addition, histone-modifying enzymes, including enhancer of zeste homolog 2 and histone deacetylases, are frequently uncontrolled in cancer, leading to alterations in gene expression. Moreover, small regulatory ribonucleic acids such as microRNA-21 and microRNA-143 contribute to the complex networks that regulate cell survival and growth. Collectively, these epigenetic alterations trigger the transition from benign growth to malignant cancer by continuously suppressing crucial genes. Furthermore, the epigenetic markers can be detected in blood and stool specimens, offering promising tools for the early detection of cancer. The major obstacle in cancer treatment is the resistance to chemotherapy drugs, which is mainly caused by epigenetic modifications in cancer cells. Therefore, the new therapeutic ways target the modifications that occur in DNA methylation and histone, mostly in conjunction with conventional therapies. As the metabolites produced by the gut microbiome can alter the host epigenetics, they can promote cancer development. Promising technologies help in the concise proofreading of epigenetic marks, and advanced single-cell analysis is paving the way for personalized treatment approaches. This cutting-edge knowledge of epigenetic regulation mechanisms offers new prospects for enhancing diagnosis, prognosis, and targeted therapies in colorectal cancer.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"114 ","pages":"183-236"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145889714","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":"Golgi Units as Modules in the Ribbon.","authors":"Akihiro Harada","doi":"10.1007/978-3-032-06936-8_2","DOIUrl":"10.1007/978-3-032-06936-8_2","url":null,"abstract":"<p><p>Using super-resolution microscopies, SCLIM and STORM, and CRISPR/Cas9 knockin technology, we show that the Golgi complex is assembled by a number of small \"Golgi units\" that are 1-3 μm in diameter. Each Golgi unit can be considered a functional and morphological module because it contains all sets of glycosylation enzymes that occupy small domains named \"zones.\" Golgi units change shape dynamically. They attach, detach, fuse, and separate from each other. The zones of glycosylation enzymes rapidly move near the rim of the unit. However, the behaviors of N- and O-linked glycosylation enzyme zones differ from those of glycosaminoglycan (GAG)-synthesizing enzyme zones in localization and dynamics. Since depletion of giantin dissociates the Golgi units, it is responsible for their attachment. Giantin depletion also prevents the movement of GAG-synthesizing enzymes between units, leading to incomplete GAG synthesis. Here, we present the model of the Golgi and its glycosylation enzymes that can explain a number of characteristics of the glycosylation processes.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"110 ","pages":"35-42"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145522896","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":"Endocytosis and trans-Golgi Network in Yeast.","authors":"Junko Toshima, Jiro Toshima","doi":"10.1007/978-3-032-06936-8_14","DOIUrl":"10.1007/978-3-032-06936-8_14","url":null,"abstract":"<p><p>Endocytosis is the process by which cells internalize extracellular materials, cell surface proteins, and lipids via vesicles formed by membrane invagination. Endocytosed cargos are first delivered to sorting compartments and then recycled back to the plasma membrane or brought to late endosomal compartments en route to the lysosome/vacuole for degradation. The budding yeast Saccharomyces cerevisiae has been an important model organism for studying the molecular mechanisms involved in the multi-step process of the endocytic pathway, including clathrin-coated vesicle formation, vesicle internalization, cargo sorting, recycling, and degradation. In the yeast endocytic pathway, the mechanisms of formation and internalization of clathrin-coated vesicles are well conserved in relation to those in mammalian cells. Yeast also has mechanisms similar to those in mammalian cells for the regulation of events in the endo-lysosomal pathway, such as endosome maturation, multi-vesicular body formation, and retrograde transport. In contrast, the structure and properties of the endocytic sorting compartment in yeast differ significantly from those in mammalian cells. Recent studies have revealed that a sub-region within the trans-Golgi network (TGN) acts as a sorting compartment in yeast. In this chapter, we summarize recent findings regarding the molecular mechanisms of the endocytic pathway, particularly the involvement of the TGN.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"110 ","pages":"335-358"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145522863","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":"Siamese Twins: The Multimodular Mechanisms of Golgi Maturation and Glycan Synthesis Are Coupled at Their Core.","authors":"Domenico Russo, Seetharaman Parashuraman, Alberto Luini","doi":"10.1007/978-3-032-16833-7_10","DOIUrl":"10.1007/978-3-032-16833-7_10","url":null,"abstract":"<p><p>The Golgi apparatus functions as the central processing hub for proteins and lipids, orchestrating glycosylation, sorting, and secretion. Once viewed as a passive site of bulk enzyme recycling, the Golgi is now recognized as a highly dynamic, multimodular system in which intra-Golgi trafficking and glycan synthesis operate as tightly interdependent \"Siamese twins.\" The classical cisternal maturation model, initially based on uniform COPI-mediated recycling, has evolved into the multimodular cisternal maturation (MCM) framework, revealing the coexistence of multiple, specialized recycling modules. Distinct sets of glycosyltransferases form coherent enzymatic modules, each maintained by dedicated retrograde pathways-some COPI-dependent, others COPI-independent-that ensure compartmental fidelity and enable differential regulation of glycan synthesis. These pathways are coordinated by adaptors, retainers, and lipid identity cues that collectively sustain Golgi polarity and adaptability to cellular and metabolic states. Disruption of this modular recycling logic leads to enzyme mislocalization, defective glycosylation, and disease, ranging from congenital disorders of glycosylation to oncogenic transformation. The transition from bulk to multimodular recycling thus redefines the Golgi as an integrated regulatory platform linking membrane trafficking to metabolic and signaling networks.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"111 ","pages":"221-249"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146259541","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":"Future Directions in Biotechnological and Pharmacological Applications of CAIs.","authors":"Claudiu T Supuran, Neera Raghav","doi":"10.1007/978-3-032-23172-7_10","DOIUrl":"10.1007/978-3-032-23172-7_10","url":null,"abstract":"<p><p>Around 50 different chemotypes were described so far to possess carbonic anhydrase (CA, EC 4.2.1.1) inhibitory action, through five different inhibition mechanisms: zinc coordination, anchoring to the zinc-coordinated water molecule; occluding the active site entrance; out of the active site binding, and halogen bond formation with the proton shuttling residues. It is conceivable that future research will evidence new CA inhibitors (CAIs) and novel mechanisms of inhibition. Presently, the emerging trends in CAI research include, apart the search for new inhibitors, the design of hybrid drugs incorporating CAIs and other pharmacological agents, the design of PROTACs targeting various CA isoforms, as well as expanding the clinical utility of such compounds for the management of tumors, cerebral ischemia, arthritis, neuropathic pain, and infections produced by bacteria, fungi, and protozoans. From the biotechnological viewpoint, CAs may be highly useful for carbon dioxide capture technologies.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"123 ","pages":"195-206"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147821187","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":"Golgi Drivers of Cancer.","authors":"Kyle A Starost, Jagadeeswara R Bommi, Prasenjit Mitra, Seth J Field","doi":"10.1007/978-3-032-16833-7_15","DOIUrl":"10.1007/978-3-032-16833-7_15","url":null,"abstract":"<p><p>Unbiased analyses of cancer genomes, transcriptomes, and proteomes have led to the identification of numerous genes that, when perturbed, contribute to the formation of cancer in humans. These unbiased analyses, by identifying drivers of cancer that localize to and function at the Golgi, have illuminated a previously unappreciated role for the Golgi in driving oncogenic phenotypes. Here we review some of the cancer drivers that act at the Golgi. We highlight the evidence that they are functionally important in cancer, and the evidence that they localize to and function at the Golgi. We also discuss functional interactions between these proteins, and review some of the proposed mechanisms by which they promote oncogenic phenotypes.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"111 ","pages":"351-380"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13429028/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146259442","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}

{"title":"A Comprehensive Guide on Epigenetics' Precision Role in Uncommon \"Rare\" Cancers' Biology and Treatment Frontiers.","authors":"Nadia M Hamdy, Ahmed S Doghish, Nehal I Rizk, Nourhan M Abdelmaksoud, Tohada M Al-Noshokaty, Mohamed Bakr Zaki, John Frederick Kennedy, Ahmed I Abulsoud","doi":"10.1007/978-3-032-08530-6_7","DOIUrl":"10.1007/978-3-032-08530-6_7","url":null,"abstract":"<p><p>The significance of epigenetics and precision medicine in the context of uncommon cancers, referred to as \"rare cancers,\" is investigated in this chapter.A comprehensive review of the current literature on noncoding RNAs (ncRNAs), natural products, and clinical trials specific to uncommon cancers was conducted. The role of ncRNAs in tumor biology is elaborated, revealing their dual influence on tumor suppression and oncogenesis, alongside current therapeutic strategies targeting these molecules. Recent clinical trial outcomes were analyzed to assess therapeutic potentials and innovations. The role of epigenetic mechanisms in rare cancer development and treatment, particularly focusing on how natural products can modify epigenetic mechanisms, such as DNA methylation, histone modifications, and the regulation of ncRNAs, was discussed in detail. The chapter emphasizes the potential of these natural products as therapeutic agents, or \"epi-drugs,\" in cancer prevention and treatment.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"114 ","pages":"355-422"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145889440","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}