Journal of Membrane Biology最新文献_第6页

Functional and Physiological Implications of Oligopeptide Transporters: Potential Targets for Pharmacological Interventions. 寡肽转运体的功能和生理意义：药物干预的潜在靶点。

IF 2.6 4区生物学

Journal of Membrane Biology Pub Date : 2025-10-01 Epub Date: 2025-05-29 DOI: 10.1007/s00232-025-00348-1

Tapas Roy, Madhu Nath, Nabanita Halder, Rohit Saxena, Thirumurthy Velpandian

{"title":"Functional and Physiological Implications of Oligopeptide Transporters: Potential Targets for Pharmacological Interventions.","authors":"Tapas Roy, Madhu Nath, Nabanita Halder, Rohit Saxena, Thirumurthy Velpandian","doi":"10.1007/s00232-025-00348-1","DOIUrl":"10.1007/s00232-025-00348-1","url":null,"abstract":"Peptide transporters are important plasma membrane proteins that facilitate the cellular uptake of di- and tripeptides in addition to various peptidomimetic drugs. The proton-coupled oligopeptide transporter (POT) family consists of mainly four transporter proteins, which include two H+ -coupled oligopeptide transporters known as PEPT1 (SLC15A1) and PEPT2 (SLC15A2), along with two peptide/histidine transporters referred to as PHT1 (SLC15A4) and PHT2 (SLC15A3). These transporters play an important role in the drug delivery process in mammalian tissues. They are highly expressed in tissues such as the small intestine, kidney, liver, lung, and eye. PHT1 shows expression in immune cells, especially in B cells and plasmacytoid dendritic cells. The pathophysiological relevance of peptide transporters is emerging to be crucial in various disease conditions, e.g., PEPT1 plays a role in the physiopathology of the gastrointestinal system, particularly in IBD. Upregulated expression of peptide transporters has also been positively related to inflammatory responses. An increasing number of peptide-based drug therapies have been reported to have the potential for development of novel classes of drugs. For example, Carnosine (beta-alanyl-L-histidine) has been demonstrated to act as an antioxidant, antiglycating agent, and neuroprotector. It is transported by PEPT1 and PEPT2, facilitating its protective effects against oxidative stress in neurons and intestinal epithelial cells. Moreover, it has applications in the treatment of multidrug-resistant cancers and has been shown to improve glucose metabolism. This review gives an insight into the functional, physiological and pharmacological importance of proton-coupled oligopeptide transporter.","PeriodicalId":50129,"journal":{"name":"Journal of Membrane Biology","volume":" ","pages":"375-390"},"PeriodicalIF":2.6,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144182279","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Action of the Terminal Complement Pathway on Cell Membranes. 终末补体途径对细胞膜的作用。

IF 2.6 4区生物学

Journal of Membrane Biology Pub Date : 2025-08-01 Epub Date: 2025-03-23 DOI: 10.1007/s00232-025-00343-6

Bill H T Ho, Bradley A Spicer, Michelle A Dunstone

{"title":"Action of the Terminal Complement Pathway on Cell Membranes.","authors":"Bill H T Ho, Bradley A Spicer, Michelle A Dunstone","doi":"10.1007/s00232-025-00343-6","DOIUrl":"10.1007/s00232-025-00343-6","url":null,"abstract":"The complement pathway is one of the most ancient elements of the host's innate response and includes a set of protein effectors that rapidly react against pathogens. The late stages of the complement reaction are broadly categorised into two major outcomes. Firstly, C5a receptors, expressed on membranes of host cells, are activated by C5a to generate pro-inflammatory responses. Secondly, target cells are lysed by a hetero-oligomeric pore known as the membrane attack complex (MAC) that punctures the cellular membrane, causing ion and osmotic flux. Generally, several membrane-bound and soluble inhibitors protect the host membrane from complement damage. This includes inhibitors against the MAC, such as clusterin and CD59. This review addresses the most recent molecular and structural insights behind the activation and modulation of the integral membrane proteins, the C5a receptors (C5aR1 and C5aR2), as well as the regulation of MAC assembly. The second aspect of the review focuses on the molecular basis behind inflammatory diseases that are reflective of failure to regulate the terminal complement effectors. Although each arm is unique in its function, both pathways may share similar outcomes in these diseases. As such, the review outlines potential synergy and crosstalk between C5a receptor activation and MAC-mediated cellular responses.","PeriodicalId":50129,"journal":{"name":"Journal of Membrane Biology","volume":" ","pages":"269-304"},"PeriodicalIF":2.6,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12313776/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143694291","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Pore Formation by Pore Forming Proteins in Lipid Membranes: Structural Insights Through Cryo-EM. 脂质膜中孔隙形成蛋白的孔隙形成：通过低温电子显微镜观察结构。

IF 2.6 4区生物学

Journal of Membrane Biology Pub Date : 2025-08-01 Epub Date: 2025-03-28 DOI: 10.1007/s00232-025-00344-5

Arnab Chatterjee, Prasenjit Naskar, Suman Mishra, Somnath Dutta

{"title":"Pore Formation by Pore Forming Proteins in Lipid Membranes: Structural Insights Through Cryo-EM.","authors":"Arnab Chatterjee, Prasenjit Naskar, Suman Mishra, Somnath Dutta","doi":"10.1007/s00232-025-00344-5","DOIUrl":"10.1007/s00232-025-00344-5","url":null,"abstract":"Many pathogenic bacteria utilize their complicated appalling arsenal, bacterial virulence factors, to attack host cells by damaging the host cell membrane and neutralizing host defense mechanisms. Bacterial pore-forming proteins (PFPs) are one of them, they include a distinct class of secreted soluble toxin monomers, which binds to the specific cell surface receptors and /or lipids, oligomerizes as an amphipathic transmembrane pore complex on host cell membranes, and deforms the integrity of the plasma membrane. Researchers have focused on characterizing the structure and function of different Pore Forming Toxins (PFTs) from various organisms, where most of the structural studies employed X-ray crystallography, single-particle cryo-EM, and cryo-electron tomography. However, historically, most of these previous studies focused on using detergent to solubilize and oligomerize the PFTs. Additionally, previous studies have also shown that lipid membranes and lipid components, including cell surface receptors, play a critical role in pore formation and oligomerization. However, there are limited studies available that aim to resolve the structure and function of PFTs in liposomes. In this review article, we majorly focused on structural and functional studies of pore-forming toxins in the presence of detergents, lipid nanodiscs, and liposomes. We will also discuss the challenges and benefits of using liposomes to study pore-forming proteins in more biologically relevant membrane environments.","PeriodicalId":50129,"journal":{"name":"Journal of Membrane Biology","volume":" ","pages":"305-322"},"PeriodicalIF":2.6,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143744156","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Introduction to Special Issue on Role of Membranes in the Pore-Formation Mechanism of Pore-Forming Proteins and Toxins. 《膜在成孔蛋白和毒素的成孔机制中的作用》特刊导论。

IF 2.6 4区生物学

Journal of Membrane Biology Pub Date : 2025-08-01 DOI: 10.1007/s00232-025-00353-4

Kausik Chattopadhyay

引用次数: 0

Correction to: Introduction to Special Issue on Role of Membranes in the Pore-Formation Mechanism of Pore-Forming Proteins and Toxins. 更正：《膜在成孔蛋白和毒素的成孔机制中的作用》特刊导言。

IF 2.9 4区生物学

Journal of Membrane Biology Pub Date : 2025-08-01 DOI: 10.1007/s00232-025-00356-1

Kausik Chattopadhyay

引用次数: 0

Oxysterols Outcompete Cholesterol Binding to the Membrane-Inserted Cytolysin A Pore Complex. 氧甾醇与胆固醇在膜插入细胞溶解素A孔复合物上的结合。

IF 2.6 4区生物学

Journal of Membrane Biology Pub Date : 2025-08-01 Epub Date: 2025-06-09 DOI: 10.1007/s00232-025-00349-0

Samlesh Choudhury, Bharath Desikan, K Ganapathy Ayappa

{"title":"Oxysterols Outcompete Cholesterol Binding to the Membrane-Inserted Cytolysin A Pore Complex.","authors":"Samlesh Choudhury, Bharath Desikan, K Ganapathy Ayappa","doi":"10.1007/s00232-025-00349-0","DOIUrl":"10.1007/s00232-025-00349-0","url":null,"abstract":"Pore-forming toxins (PFTs) belong to a class of proteins expressed by bacteria to initiate infections by unregulated pore formation on the plasma membrane of host cells. Although cholesterol is a key sterol motif that promotes toxin activity, the influence of oxysterols, upregulated in senescent cells or in other inflammatory disorders, on lytic activity has not received much attention. Using all-atom molecular dynamics simulations, we study the changes to the sterol binding landscape of membrane-inserted cytolysin A (ClyA), an <math><mi>α</mi></math> -PFT expressed by E. coli, in the presence of tail-oxidized 25-hydroxycholesterol (25-HC) in a palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC):cholesterol:25-HC (70:20:10) membrane. 25-HC was found to entirely replace previously identified cholesterol binding hotspots [PNAS,115 7323-7330] between the membrane-inserted <math><mi>β</mi></math> -tongue motifs with binding lifetimes on the order of microseconds. Although the overall sterol occupancy is lower for the N-terminal helix motif that forms the lining of the water channel, 25-HC binding is less when compared with cholesterol. The presence of the additional OH group on the 25th carbon enhances interactions with polar residues of the <math><mi>β</mi></math> -tongue, increasing 25-HC binding times by several fold when compared with cholesterol. We discuss the implications of this enhanced oxysterol interaction on pore formation of the <math><mi>α</mi></math> family of toxins such as ClyA, in contrast with the cholesterol-dependent cytolysins, where oxysterols have been shown to be detrimental to pore formation.","PeriodicalId":50129,"journal":{"name":"Journal of Membrane Biology","volume":" ","pages":"341-352"},"PeriodicalIF":2.6,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144250608","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Hetero-Oligomeric Protein Pores for Single-Molecule Sensing. 用于单分子传感的异聚寡聚蛋白孔。

IF 2.6 4区生物学

Journal of Membrane Biology Pub Date : 2025-08-01 Epub Date: 2024-12-19 DOI: 10.1007/s00232-024-00331-2

Remya Satheesan, Asuma Janeena, Kozhinjampara R Mahendran

{"title":"Hetero-Oligomeric Protein Pores for Single-Molecule Sensing.","authors":"Remya Satheesan, Asuma Janeena, Kozhinjampara R Mahendran","doi":"10.1007/s00232-024-00331-2","DOIUrl":"10.1007/s00232-024-00331-2","url":null,"abstract":"Protein nanopores are emerging as versatile single-molecule sensors with broad applications in DNA and protein sequencing. However, their narrow size restricts the range of detectable analytes, necessitating the development of advanced nanopores to broaden their applications in biotechnology. This review highlights a natural hetero-oligomeric porin, Nocardia farcinica porin AB (NfpAB), based on the Gram-positive mycolata, Nocardia farcinica. The pore comprises two subunits, NfpA and NfpB, that combine to form a stable structure with a unique pore geometry, asymmetrical shape, and charge distribution. Single-channel electrical recordings demonstrate that NfpAB forms stable, high-conductance channels suitable for sensing charged molecules, particularly cationic polypeptides and cyclic sugars. This pore offers advantages such as enhanced control over molecular interactions due to densely crowded charged residues, thus allowing the quantification of voltage-dependent translocation kinetics. Notably, NfpAB contains intrinsic cysteines in the pore lumen, providing an accessible site for thiol-based reactions and attachment of molecular adapters. We propose that such hetero-oligomeric pores will be effective for several applications in nanopore technology for biomolecular detection and sequencing.","PeriodicalId":50129,"journal":{"name":"Journal of Membrane Biology","volume":" ","pages":"257-267"},"PeriodicalIF":2.6,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142856535","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Interaction of an Oomycete Nep1-like Cytolysin with Natural and Plant Cell-Mimicking Membranes. 一种类似于卵菌 Nep1 的细胞溶解素与天然膜和植物细胞模拟膜的相互作用

IF 2.6 4区生物学

Journal of Membrane Biology Pub Date : 2025-08-01 Epub Date: 2024-12-18 DOI: 10.1007/s00232-024-00330-3

Tina Snoj, Tjaša Lukan, Kristina Gruden, Gregor Anderluh

{"title":"Interaction of an Oomycete Nep1-like Cytolysin with Natural and Plant Cell-Mimicking Membranes.","authors":"Tina Snoj, Tjaša Lukan, Kristina Gruden, Gregor Anderluh","doi":"10.1007/s00232-024-00330-3","DOIUrl":"10.1007/s00232-024-00330-3","url":null,"abstract":"Plants are attacked by various pathogens that secrete a variety of effectors to damage host cells and facilitate infection. One of the largest and so far understudied microbial protein families of effectors is necrosis- and ethylene-inducing peptide-1-like proteins (NLPs), which are involved in important plant diseases. Many NLPs act as cytolytic toxins that cause cell death and tissue necrosis by disrupting the plant's plasma membrane. Their mechanism of action is unique and leads to the formation of small, transient membrane ruptures. Here, we capture the interaction of the cytotoxic model NLP from the oomycete Pythium aphanidermatum, NLPPya, with plant cell-mimicking membranes of giant unilamellar vesicles (GUVs) and tobacco protoplasts using confocal fluorescence microscopy. We show that the permeabilization of GUVs by NLPPya is concentration- and time-dependent, confirm the small size of the pores by observing the inability of NLPPya monomers to pass through them, image the morphological changes of GUVs at higher concentrations of NLPPya and confirm its oligomerization on the membrane of GUVs. In addition, NLPPya bound to plasma membranes of protoplasts, which showed varying responses. Our results provide new insights into the interaction of NLPPya with model lipid membranes containing plant-derived sphingolipids.","PeriodicalId":50129,"journal":{"name":"Journal of Membrane Biology","volume":" ","pages":"323-339"},"PeriodicalIF":2.6,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12313774/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142848053","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Role of Ion Channels in Alzheimer's Disease Pathophysiology. 离子通道在阿尔茨海默病病理生理中的作用。

IF 2.6 4区生物学

Journal of Membrane Biology Pub Date : 2025-06-01 Epub Date: 2025-05-01 DOI: 10.1007/s00232-025-00341-8

Ranjit Bhoi, Tuhina Mitra, Kallam Tejaswi, Vaishnav Manoj, Swagata Ghatak

引用次数: 0

The Effect of Xenon on the Voltage‒Current Characteristics of Tethered Lipid Bilayers. 氙对系留脂质双分子层电压电流特性的影响。

IF 2.6 4区生物学

Journal of Membrane Biology Pub Date : 2025-06-01 Epub Date: 2025-04-28 DOI: 10.1007/s00232-025-00346-3

Hadeel Alobeedallah, Bruce Cornell, Hans Coster

引用次数: 0