Molecular and Cellular Biochemistry最新文献

{"title":"Long-chain chlorinated paraffins exposure induces premature ovarian failure by disrupting the balance of mitochondrial fission.","authors":"Chenhui Xu, Haochu Deng, Xue Tian, Shuang Ma, Yuebing Kong, Ruoting Zhang, Shiyu Yao, Hainan Lan","doi":"10.1007/s11010-026-05696-7","DOIUrl":"10.1007/s11010-026-05696-7","url":null,"abstract":"<p><p>Long-chain chlorinated paraffins (LCCPs) accumulate in reproductive organs due to their high persistence and bioaccumulation potential; however, the molecular mechanisms underlying their ovarian toxicity remain unclear. In this study, we used primary mouse granulosa cells, a human SVOG cell line, and an oral exposure model in female mice to systematically evaluate the ovarian damage effects of LCCPs and investigate the underlying signaling pathways. The results showed that concentrations of 0.02-2 µg/mL of LCCPs concentration-dependently reduced granulosa cell survival rates (by 12%-58%, P < 0.05), while significantly upregulating oxidative stress (MDA, ROS), inflammatory cytokines (IL-6, TNF-α), and aging markers (SA-β-gal activity). In vivo exposure led to morphological degeneration of ovarian tissue and a reduction in the number of primordial follicles, accompanied by decreased serum estradiol and elevated follicle-stimulating hormone (FSH) levels; these changes resemble the phenotype of clinical ovarian dysfunction. At the mechanistic level, LCCPs induce excessive mitochondrial fission by blocking the interaction between Drp1 and Parkin, leading to the leakage of mitochondrial DNA into the cytoplasm, which in turn activates the cGAS-STING pathway and ultimately drives granulosa cell senescence. These findings reveal a novel mechanism by which LCCPs mediate ovarian toxicity via the \"excessive mitochondrial fragmentation- mtDNA leakage- cGAS- STING- cellular senescence\" axis, providing direct experimental evidence for assessing the risks of persistent organic pollutants to female reproductive health.</p>","PeriodicalId":18724,"journal":{"name":"Molecular and Cellular Biochemistry","volume":" ","pages":"4813-4828"},"PeriodicalIF":4.7,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148795529","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Anemoside B4 upregulates DDAH2 and attenuates oxidative stress induced endothelial dysfunction.","authors":"Shuxian Lu, Yao Yi, Qin Chen, Luling He, Margaret Baldini, Dan Shan, Limin Gong, Liang Qiu, Shumin Ma, Manman Qin, Yanyun Fang, Yifeng Zhang, Jun Yu","doi":"10.1007/s11010-026-05690-z","DOIUrl":"10.1007/s11010-026-05690-z","url":null,"abstract":"<p><p>Endothelial dysfunction, involving diminished nitric oxide (NO) bioavailability and vascular inflammation, plays a pivotal role in cardiovascular disease progression. Anemoside B4 (AB4), a major bioactive component extracted from Pulsatilla chinensis, has been reported to exert anti-inflammatory, anti-tumor, and antiviral effects. However, its potential role in regulating endothelial function remains largely unexplored. Integrating RNA-seq analysis, we revealed that AB4 may exert anti-atherosclerotic effects by upregulating DDAH2 expression and improving endothelial NO production. Using an H₂O₂-induced endothelial cell dysfunction model, we found that AB4 significantly reversed H₂O₂-induced impairments in endothelial cell viability and migration, while attenuating apoptosis and reducing monocyte adhesion. In addition, AB4 upregulated DDAH2 protein expression, restored eNOS phosphorylation, and increased NO production under oxidative stress conditions. Pharmacological perturbation of DDAH2 protein expression with PD404182 attenuated the AB4-mediated restoration of eNOS-NO signaling and weakened its inhibitory effects on monocyte-endothelial adhesion and ICAM-1/VCAM-1 expression. Consistently, in a mouse model of oxidative stress-induced endothelial dysfunction, AB4 increased endothelial DDAH2 protein expression, enhanced NO production, and suppressed endothelial ICAM-1 and VCAM-1 expression. These effects were attenuated by PD404182, supporting the involvement of DDAH2 regulation in the endothelial protective effects of AB4. Taken together, these results suggest that AB4 restores endothelial eNOS-NO signaling and counteracts oxidative stress-induced endothelial dysfunction, evidenced by enhanced viability, improved migration, and reduced apoptosis and inflammation, with these effects being associated with DDAH2 upregulation.</p>","PeriodicalId":18724,"journal":{"name":"Molecular and Cellular Biochemistry","volume":" ","pages":"4857-4871"},"PeriodicalIF":4.7,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148795435","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Erastin-sensitive VDAC2 contributes to time-course peritoneal fibrosis via ferroptosis signaling induction.","authors":"Wenfeng Wei, Yanping Qiu, Rong Luo, Yangping Feng","doi":"10.1007/s11010-026-05694-9","DOIUrl":"10.1007/s11010-026-05694-9","url":null,"abstract":"<p><p>Peritoneal dialysis (PD) is a renal replacement therapy for patients with end-stage renal disease, but long-term treatment often leads to peritoneal fibrosis, compromising dialysis efficacy. This study aimed to elucidate the role of ferroptosis in peritoneal fibrosis (PF) and to clarify the regulatory function of the voltage-dependent anion channel 2 (VDAC2). Mesothelial cell subpopulations were identified from the single-cell dataset GSE130888, followed by differential gene expression analysis to screen ferroptosis-related genes. In vitro and in vivo models were used to validate the involvement of ferroptosis in PF. siRNA-mediated VDAC2 knockdown, combined with the ROS scavenger NAC, was applied to assess its role in regulating mitochondrial ROS during ferroptosis and fibrosis. Single-cell analysis revealed ferroptosis-related gene alterations in both short-term (ST) and long-term (LT) PD, with VDAC2 expression positively associated with dialysis duration. Erastin significantly reduced MET‑5 A cell viability, increased apoptosis, elevated ROS and lipid peroxidation, decreased GSH levels, and upregulated VDAC2, ACSL4, and fibrosis‑related proteins. These effects were reversed by Fer‑1. In vivo, Erastin exacerbated peritoneal dysfunction, collagen deposition, and tissue iron accumulation in mice, and caused complete collapse of cellular architecture, dissolution of organelles, nuclear envelope rupture, and chromatin fragmentation, whereas Fer‑1 improved peritoneal pathology and iron deposition. VDAC2 knockdown restored MET‑5 A cell viability, reduced ROS and lipid peroxidation, increased GSH levels, and downregulated ferroptosis- and fibrosis-related proteins; co‑treatment with NAC further enhanced these protective effects. VDAC2 promotes peritoneal mesothelial cell injury and fibrosis by driving mitochondrial ROS-dependent ferroptosis. Targeting VDAC2 or inhibiting ferroptosis may provide a potential therapeutic strategy to delay peritoneal dialysis-associated fibrosis.</p>","PeriodicalId":18724,"journal":{"name":"Molecular and Cellular Biochemistry","volume":" ","pages":"4829-4842"},"PeriodicalIF":4.7,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148795477","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Actin polymerization drives endogenous MMP-9 upregulation and blood-brain barrier disruption in ischemic brain endothelial cells.","authors":"Yiyin Zhao, Songbin He, Yiming Wang, Meng Jin, Yichao Fu, Xiaojing Zhou","doi":"10.1007/s11010-026-05706-8","DOIUrl":"10.1007/s11010-026-05706-8","url":null,"abstract":"<p><p>Blood-brain barrier (BBB) disruption is a critical early event in ischemic stroke. Matrix metalloproteinase-9 (MMP-9) drives BBB breakdown through proteolytic degradation of junctional proteins; however, the upstream mechanisms triggering endogenous MMP-9 upregulation within brain endothelial cells before inflammatory cell infiltration remain poorly understood. Here, we identify actin polymerization as a functional upstream driver of endothelial MMP-9 activation and BBB disruption under ischemic conditions. Using an oxygen-glucose deprivation (OGD) model in bEnd.3 cells, we found that 6 h of OGD induced significant actin remodeling concurrent with upregulation of both MMP-9 expression and enzymatic activity, reduced the total protein levels of occludin, ZO-1, and VE-cadherin, disrupted their membrane localization, and increased transendothelial permeability. Bidirectional pharmacological modulation of actin dynamics using jasplakinolide (an F-actin stabilizer) and latrunculin B (a polymerization inhibitor) correspondingly amplified or attenuated all these changes. Crucially, lentivirus-mediated shRNA knockdown of MMP-9 significantly preserved junctional protein expression, maintained transendothelial electrical resistance, and reduced barrier permeability even under jasplakinolide-enhanced polymerization, establishing MMP-9 as a necessary mediator of actin-driven barrier disruption. MMP-9 knockdown also attenuated F-actin accumulation, suggesting a self-amplifying feedback loop. These findings delineate an endothelial-autonomous actin-MMP-9-BBB disruption axis that operates independently of inflammatory cell infiltration, identifying endothelial actin homeostasis as a potential therapeutic target for early barrier protection in ischemic stroke.</p>","PeriodicalId":18724,"journal":{"name":"Molecular and Cellular Biochemistry","volume":" ","pages":"4987-5007"},"PeriodicalIF":4.7,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148840740","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Quercetin exerts radioprotective effects against radiation-induced intestinal injury with involvement of the PI3K-AKT/Caspase-3 axis.","authors":"Qing Guo, Zhibing Tang, Zhenyu Hou, Ge Yan, Jiaxuan Wang, Man Zhang, Ruige Ma, Juan Wang, Qiong Feng, Zhen Wang, Chunlei Wang, Lin Zhao","doi":"10.1007/s11010-026-05665-0","DOIUrl":"10.1007/s11010-026-05665-0","url":null,"abstract":"<p><p>Radiation-induced intestinal injury (RIII) significantly limits the efficacy of abdominal and pelvic radiotherapy while also impairing patient quality of life. This condition is primarily driven by excessive reactive oxygen species (ROS) and dysregulation of Caspase-dependent apoptosis. Quercetin (QUE), a natural antioxidant flavonoid, exhibits radioprotective potential; however, the key signaling pathways it employs to regulate radiation-induced apoptosis remain to be elucidated. In vitro studies, IEC-6 cells (1-10 µg/mL QUE pretreatment followed by 0-8 Gy X-ray exposure) were conducted to analyze proliferation, clonogenic survival, ROS levels, apoptosis, and expression of RIII-related proteins and genes. Network pharmacology identified 47 overlapping targets associated with QUE and RIII, with AKT1 and CASP3 identified as hub targets, and the PI3K-AKT pathway recognized as a key regulatory pathway. A Caspase-3/7 inhibitor (HY-103346, H10) and AutoDock-Vina docking analysis were used to explore the involvement of Caspase-3-related apoptotic signaling. In vivo experiments using Drosophila melanogaster (W¹¹¹⁸) involved groups subjected to control, 50 Gy irradiation alone, or 50 Gy combined with 1/5/10/50 µg/mL QUE. Lifespan, locomotor capacity, and intestinal ROS levels were assessed, including validation with DCP-1^RNAi transgenic flies (DCP-1: Drosophila Caspase-3 homolog). In vitro findings revealed that QUE enhanced the viability of irradiated IEC-6 cells, reduced ROS and apoptosis, upregulated anti-apoptotic markers (p-AKT, p-PI3K and p-mTOR), and downregulated pro-apoptotic markers (cleaved-Caspase-3 and Cytochrome C), while H10 inhibited the effects of QUE. Molecular docking suggested a potential interaction between QUE and Caspase-3 through hydrogen bonds and hydrophobic interactions to inhibit its activation. In vivo, pre-irradiation gavage of 10 µg/mL QUE mitigated RIII in Drosophila, an effect that was abolished in DCP-1 knockdown flies. In summary, QUE protects against RIII by scavenging ROS and modulating apoptosis-related signaling, with evidence supporting the involvement of the PI3K-AKT/Caspase-3 axis, with the PI3K-AKT/Caspase-3 axis identified as central to these protective effects. This study underscores the clinical potential of QUE for RIII and offers insights into the targeting of apoptosis for radioprotection.</p>","PeriodicalId":18724,"journal":{"name":"Molecular and Cellular Biochemistry","volume":" ","pages":"4337-4354"},"PeriodicalIF":4.7,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148620800","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Trimethylamine N-oxide activates cardiac fibroblasts transformation through NLRP3 inflammasome activation with changes in mitochondrial dynamics and ER-mitochondrial contact under ER stress.","authors":"Huimin Wang, Hanlin Liu, Xinnan Meng, Jiantao Song, Yan Jin, Yuanyuan Bai","doi":"10.1007/s11010-026-05658-z","DOIUrl":"10.1007/s11010-026-05658-z","url":null,"abstract":"<p><p>Trimethylamine N-oxide (TMAO), a gut microbiota-derived metabolite, has been linked to cardiovascular diseases. This study aimed to explore the role of TMAO in cardiac fibrosis by examining its effects on the NLRP3 inflammasome, endoplasmic reticulum stress (ERS), mitochondria-associated membranes (MAMs), and mitochondrial dynamics in cardiac fibroblasts (CFs), alongside clinical data from acute myocardial infarction (AMI) patients and unstable angina (UA) patients and AMI animal model data. Plasma TMAO levels were measured in AMI patients and healthy controls. In vitro, CFs were treated with TMAO to assess cellular activation and fibrosis markers. Western blot, immunofluorescence, and RNA sequencing identified key pathways and proteins related to ERS, NLRP3 inflammasome activation, and mitochondrial dynamics. In vivo, Masson's trichrome staining, Hematoxylin-Eosin (HE) staining and Immunohistochemical were used to evaluate the effects of TMAO on AMI mice. Plasma TMAO levels were significantly higher in the AMI group. TMAO promoted cardiac fibroblast activation and fibrosis by increasing α-SMA and Collagen I expression. It induced ERS, marked by elevated GRP78, p-PERK, and CHOP, and upregulated Sigma-1R, enhancing MAM formation. TMAO also altered mitochondrial dynamics via DRP1 phosphorylation and Mfn2 expression. RNA sequencing identified macrophage migration inhibitory factor (MIF) as a key mediator linking TMAO to NLRP3 inflammasome activation. TMAO exacerbates myocardial injury and fibrotic remodeling in AMI mice. TMAO exacerbates cardiac fibrosis via ERS and NLRP3 activation, with implications for mitochondrial dynamics and MAM formation. Elevated TMAO levels in AMI patients underscore its potential as a therapeutic target for ventricular remodeling fibrosis.</p>","PeriodicalId":18724,"journal":{"name":"Molecular and Cellular Biochemistry","volume":" ","pages":"4157-4180"},"PeriodicalIF":4.7,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148520755","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Heat shock protein family D member 1 (HSPD1) modulates ribosome-related pathways and protein synthesis in lung adenocarcinoma.","authors":"Keerakarn Somsuan, Artitaya Rongjumnong, Wararat Chiangjong, Jatuporn Ngoenkam, Atthapan Morchang, Papawarin Karamart, Jirawan Panachan, Patcharin Kaewboonruang, Wariya Mongkolwat, Somchai Chutipongtanate, Sutatip Pongcharoen, Wim Vanden Berghe, Siripat Aluksanasuwan","doi":"10.1007/s11010-026-05693-w","DOIUrl":"10.1007/s11010-026-05693-w","url":null,"abstract":"<p><p>Lung adenocarcinoma (LUAD) is the most prevalent histological subtype of lung cancer. Heat shock protein family D member 1 (HSPD1 or HSP60), a multifunctional chaperone, has been implicated in promoting lung cancer progression by regulating tumor cell growth, cancer-associated fibroblast activation, and angiogenesis. Despite these roles, the molecular mechanisms underlying its oncogenic activity remain incompletely understood. In this study, we conducted a proteomic analysis and functional investigations on HSPD1-knockdown and control A549 cells. Knockdown of HSPD1 suppressed cell proliferation, disrupted cell-cycle progression, and had no significant effect on apoptosis. Additionally, HSPD1-knockdown cells exhibited reduced colony formation, wound closure, and invasion capabilities. Sequential Window Acquisition of All Theoretical fragment ions (SWATH)-targeted proteomics revealed 21 significantly altered proteins, primarily involved in ribosome-related functions and associated with overall survival in LUAD patients. Reduced levels of ribosomal proteins and translational capacity were further examined by Western blot and protein synthesis assays. A decrease in ribosome abundance was confirmed by immunofluorescence staining of ribosomal protein S3 (RPS3) and by direct visualization under transmission electron microscopy. Quantitative real-time PCR demonstrated downregulation of MTOR in HSPD1-knockdown cells. Moreover, HSPD1 knockdown sensitized cells to homoharringtonine, a chemotherapeutic drug targeting ribosomal activity. These effects on cell proliferation, ribosomal protein levels, and drug sensitivity were validated in an independent LUAD cell line, H1975. Collectively, these findings indicate that HSPD1 acts as an oncogenic driver in LUAD by modulating ribosome-related pathways and protein synthesis.</p>","PeriodicalId":18724,"journal":{"name":"Molecular and Cellular Biochemistry","volume":" ","pages":"4673-4689"},"PeriodicalIF":4.7,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148701904","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bone marrow fibrocytes and endothelial-to-mesenchymal transition drive pathological ECM remodeling in proliferative diabetic retinopathy.","authors":"Ting-Ting Xiao, Bin Wang, Xiao-Yong Qu, Zhi-Peng You","doi":"10.1007/s11010-026-05671-2","DOIUrl":"10.1007/s11010-026-05671-2","url":null,"abstract":"<p><p>Proliferative diabetic retinopathy (PDR) is characterized by pathological neovascularization and fibrovascular membrane (FVM) formation, yet the cellular origins of fibroblasts within FVMs and vitreous collagen metabolism remain poorly understood. Vitreous humor and FVM specimens were collected from PDR patients and non-diabetic controls undergoing vitrectomy. Immunohistochemistry, enzyme-linked immunosorbent assay (ELISA), and enzymatic activity assays were performed. Double-positive staining for cluster of differentiation (CD)45/collagen type I (COL1) and CD45/S100 calcium-binding protein A4 (S100A4) identified bone marrow-derived fibrocytes, while CD31/COL1 co-expression indicated endothelial-to-mesenchymal transition (EndoMT). Fibronectin was significantly elevated in PDR vitreous (p < 0.01). Matrix metalloproteinase (MMP)-2, MMP-3, and MMP-9 activities were markedly increased in PDR (all P < 0.001), alongside elevated lysyl oxidase (LOX) activity (p < 0.001). Collagen IV detection rates were higher in PDR (63.2% vs. 15%, P < 0.01), and beta cross-linked C-telopeptide of type I collagen (β-CTX) levels were significantly increased (p < 0.001). Notably, total procollagen type I N-terminal propeptide (Total-PINP) was paradoxically elevated in PDR vitreous (p < 0.01), suggesting compensatory collagen synthesis during active neovascularization. These findings demonstrate that FVM fibroblasts originate from multiple sources including bone marrow-derived fibrocytes and EndoMT, and that PDR involves simultaneous MMP-mediated collagen degradation and LOX-mediated cross-linking, providing potential targets for anti-fibrotic therapies.</p>","PeriodicalId":18724,"journal":{"name":"Molecular and Cellular Biochemistry","volume":" ","pages":"4873-4885"},"PeriodicalIF":4.7,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13638742/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148795485","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Lactic acid exposure alters lysophosphatidic acid receptor-mediated regulation of growth and motility in pancreatic cancer cells.","authors":"Mao Yamamoto, Miwa Takai, Nanami Shimomura, Eiki Isa, Narumi Yashiro, Moemi Tamura, Shion Nagano, Yuka Kusumoto, Toshifumi Tsujiuchi","doi":"10.1007/s11010-026-05714-8","DOIUrl":"10.1007/s11010-026-05714-8","url":null,"abstract":"<p><p>Lysophosphatidic acid (LPA) receptor signaling contributes to the regulation of cancer cell functions. Lactic acid serves not only as an important energy source for cancer cells but also activates various signaling pathways that influence cancer cell behavior. To investigate the roles of LPA receptors in the malignant behavior of pancreatic cancer PANC-1 cells, PANC-LA1 and PANC-LA5 cells were generated by culturing PANC-1 cells with 1 or 5 mM lactic acid, respectively, for approximately 3 months. LPAR1, LPAR3, and LPAR5 expression levels expression levels were elevated, whereas LPAR2 expression was reduced in PANC-LA1 and PANC-LA5 cells compared with PANC-1 cells. PANC-1 cell growth was inhibited by LPA. Conversely, PANC-LA1 cell growth remained unchanged in response to LPA, and LPA increased PANC-LA5 cell growth. The motility of PANC-LA1 and PAN-LA5 cells was markedly elevated compared with that of PANC-1 cells. LPA further enhanced PANC-LA1 and PAN-LA5 cell motility but did not affect PANC-1 cell motility. In the presence of LPA, AM966 inhibited, whereas TC LPA5 4 stimulated PANC-LA5 cell growth and PANC-LA1 cell motility. Although GRI-977,143 increased PANC-LA5 cell growth, it reduced PANC-LA1 cell motility. (2S)-OMPT increased PANC-LA5 cell growth and PANC-LA1 cell motility. When cells were cultured in serum-free media, the viability of PANC-LA1 and PANC-LA5 cells was higher compared with that of PANC-1 cells. PANC-LA5 cell growth and PANC-LA1 cell motility were inhibited by AZD3965 and galloflavin. These findings indicate that LPA receptor signaling is involved in the regulation of PANC-1 cell behavior induced by long-term lactic acid exposure, with LPA₁ and LPA₃ acting as major positive regulators of proliferation and motility following long-term lactic acid exposure, whereas LPA₂ and LPA₅ exert distinct regulatory effects.</p>","PeriodicalId":18724,"journal":{"name":"Molecular and Cellular Biochemistry","volume":" ","pages":"5087-5099"},"PeriodicalIF":4.7,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13638741/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148851308","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Correction: Carvacrol induces apoptosis, modulates oxidative stress, and promotes G0/G1 cell cycle arrest in colorectal cancer cells.","authors":"Asmaa Abuaisha, Halil Ibrahim Arslan, Emir Nekay, Ramazan Aciroglu, Cuneyd Yavas, Nermin Akcali, Dima Dvaidar, Tugba Bayramoglu, Esra Nazligul, Tarik Mecit, Adem Bayraktar, Selman Emiroglu","doi":"10.1007/s11010-026-05685-w","DOIUrl":"10.1007/s11010-026-05685-w","url":null,"abstract":"","PeriodicalId":18724,"journal":{"name":"Molecular and Cellular Biochemistry","volume":" ","pages":"4901-4908"},"PeriodicalIF":4.7,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148813531","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}