Matrix Biology最新文献

{"title":"Extracellular matrix integrity regulates GABAergic plasticity in the hippocampus","authors":"Jadwiga Jabłońska ,&nbsp;Grzegorz Wiera ,&nbsp;Jerzy W. Mozrzymas","doi":"10.1016/j.matbio.2024.11.001","DOIUrl":"10.1016/j.matbio.2024.11.001","url":null,"abstract":"<div><div>The brain's extracellular matrix (ECM) is crucial for neural circuit functionality, synaptic plasticity, and learning. While the role of the ECM in excitatory synapses has been extensively studied, its influence on inhibitory synapses, particularly on GABAergic long-term plasticity, remains poorly understood. This study aims to elucidate the effects of ECM components on inhibitory synaptic transmission and plasticity in the hippocampal CA1 region. We focus on the roles of chondroitin sulfate proteoglycans (CSPGs) and hyaluronic acid in modulating inhibitory postsynaptic currents (IPSCs) at two distinct inhibitory synapses formed by somatostatin (SST)-positive and parvalbumin (PV)-positive interneurons onto pyramidal cells (PCs). Using optogenetic stimulation in brain slices, we observed that acute degradation of ECM constituents by hyaluronidase or chondroitinase-ABC did not affect basal inhibitory synaptic transmission. However, short-term plasticity, particularly burst-induced depression, was enhanced at PV→PC synapses following enzymatic treatments. Long-term plasticity experiments demonstrated that CSPGs are essential for NMDA-induced iLTP at SST→PC synapses, whereas the digestion of hyaluronic acid by hyaluronidase impaired iLTP at PV→PC synapses. This indicates a synapse-specific role of CSPGs and hyaluronic acid in regulating GABAergic plasticity. Additionally, we report the presence of cryptic GABAergic plasticity at PV→PC synapses induced by prolonged NMDA application, which became evident after CSPG digestion and was absent under control conditions. Our results underscore the differential impact of ECM degradation on inhibitory synaptic plasticity, highlighting the synapse-specific interplay between ECM components and specific GABAergic synapses. This offers new perspectives in studies on learning and critical period timing.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"134 ","pages":"Pages 184-196"},"PeriodicalIF":4.5,"publicationDate":"2024-11-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142570349","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effects of hydrostatic pressure, osmotic pressure, and confinement on extracellular matrix associated responses in the nucleus pulposus cells ex vivo","authors":"Hayato L. Mizuno ,&nbsp;James D. Kang ,&nbsp;Shuichi Mizuno","doi":"10.1016/j.matbio.2024.10.005","DOIUrl":"10.1016/j.matbio.2024.10.005","url":null,"abstract":"<div><div>Spinal movement in both upright and recumbent positions generates changes in physicochemical stresses including hydrostatic pressure (HP), deviatoric stress, and confinement within the intradiscal compartment. The nucleus pulposus (NP) of the intervertebral disc is composed of highly negatively charged extracellular matrix (ECM), which increases osmotic pressure (OP) and generates tissue swelling. In pursuing regenerative therapies for intervertebral disc degeneration, the effects of HP on the cellular responses of NP cells and the ECM environment remain incompletely understood. We hypothesized that anabolic turnover of ECM in NP tissue is maintained under HP and confinement. We first clarified the effects of the relationships among HP, OP, and confinement on swelling NP explants isolated from bovine caudal intervertebral discs over 12 h. We found that the application of confinement and constant HP significantly inhibits the free swelling of NP (<em>p</em> &lt; 0.01) and helps retain the sulfated glycosaminoglycan. Since confinement and HP inhibited swelling, we incubated confined NPs under HP in high-osmolality medium mimicking ECM-associated OP for 7 days and demonstrated the effects of HP on metabolic turnover of ECM molecules in NP cells. The aggrecan core protein gene was significantly upregulated under confinement and constant HP compared to confinement and no HP (<em>p</em> &lt; 0.01). We also found that confinement and constant HP helped to significantly retain smaller cell area (<em>p</em> &lt; 0.01) and significantly prevent the severing of actin filaments compared to no confinement and HP (<em>p</em> &lt; 0.01). Thus, we suggest that NP's metabolic turnover and cellular responses are regulated by the configuration of intracellular actin and fibrillar ECMs under HP.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"134 ","pages":"Pages 162-174"},"PeriodicalIF":4.5,"publicationDate":"2024-10-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142479184","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Fibroblast integrin α11β1 is a collagen assembly receptor in mechanoregulated fibrillar adhesions","authors":"Moses Musiime ,&nbsp;Pugazendhi Murugan Erusappan ,&nbsp;Edna Cukierman ,&nbsp;Joan Chang ,&nbsp;Anders Molven ,&nbsp;Uwe Hansen ,&nbsp;Cédric Zeltz ,&nbsp;Donald Gullberg","doi":"10.1016/j.matbio.2024.10.006","DOIUrl":"10.1016/j.matbio.2024.10.006","url":null,"abstract":"<div><div>Solid epithelial cancers with significant desmoplasia are characterized by an excessive deposition of collagen-based matrix, which often supports tumor progression. However, the mechanism of how collagen receptors mediate collagen fibrillogenesis still remains mostly unclear.</div><div>We show that the collagen-binding integrin α11β1 can co-localize with tensin-1 and deposited collagen I in human pancreatic ductal adenocarcinoma (PDAC) stroma. In addition to the canonical fibrillar adhesion integrin α5β1 expressed by human PDAC cancer-associated fibroblasts (CAFs), tensin-1-positive fibrillar adhesions contained α11β1 but lacked α1β1 and α2β1. CAFs lacking α5β1 expression displayed mechanoregulated and tensin-1 dependent α11β1 fibrillar adhesions, suggesting independent roles of the two integrins with regards to fibrillar adhesions-based de novo fibrillogenesis. Further, we demonstrate that cell surface-associated collagen I assembly necessitated α11β1, but not α5β1 expression.</div><div>In summary, α11β1 integrin is a novel component of fibrillar adhesions, which is strategically positioned to mediate de novo collagen fibrillogenesis at the cell surface under pro-fibrotic conditions.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"134 ","pages":"Pages 144-161"},"PeriodicalIF":4.5,"publicationDate":"2024-10-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142479185","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"COL8A2 activation enhances function of corneal endothelial cells through HIPPO signaling/mitochondria pathway","authors":"Yunkyoung Ryu ,&nbsp;Je Hyun Seo ,&nbsp;Hak Su Kim ,&nbsp;Youn Joo Nam ,&nbsp;Kyung Bo Noh ,&nbsp;Sun-Hee Oh ,&nbsp;Jin Sun Hwang ,&nbsp;Young Joo Shin","doi":"10.1016/j.matbio.2024.10.001","DOIUrl":"10.1016/j.matbio.2024.10.001","url":null,"abstract":"<div><div>Corneal endothelial cells (CECs) are essential for maintaining corneal transparency and hydration through their barrier and pump functions. The <em>COL8A2</em> gene encodes a component of the extracellular matrix of the cornea, which is crucial for the normal functioning of these cells. Mutations in <em>COL8A2</em> are linked to corneal dystrophies, emphasizing the gene's importance in corneal health. The purpose of this research is to explore the effects of <em>COL8A2</em> activation within CECs, to understand its contribution to cellular behavior and health. <em>COL8A2</em> CRISPR/dCas9 activation system (aCOL8A2) was used to activate the <em>COL8A2</em>. In rats, wound healing and mitochondrial function were assessed after <em>COL8A2</em> activation. As a result, aCOL8A2 promoted wound healing of rat corneal endothelium by increasing mitochondrial membrane potential. In cultured human CECs, proteomic analysis was performed to screen and identify the differential protein profiles between control and aCOL8A2 cells. Western blot was used to validate the differential proteins from both cells. Mitochondrial function and intracellular distribution were assessed by measuring ATP production and mitochondrial membrane potential. In cultured human CECs, aCOL8A2 increased COL8A2 and phospho-YAP levels. Transendothelial electrical resistance (TEER) was increased and actin cytoskeleton was attenuated by aCOL8A2. Gene ontology analysis revealed that the proteins were mainly involved in the regulation of folate biosynthesis, ECM-receptor interaction, cell differentiation, NADP activity and cytoskeleton. ATP production was increased, mitochondrial membrane potential was polarized and mitochondrial distribution was widespread in the aCOL8A2 group. In conclusion, aCOL8A2 induces a regulatory cascade affecting mitochondrial positioning and efficiency, mediated by alterations in the cytoskeletal architecture and the YAP signaling pathway. This sequence of events serves to bolster the functional capacities of corneal endothelial cells, including their pump and barrier functions, essential for corneal health and transparency.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"134 ","pages":"Pages 119-131"},"PeriodicalIF":4.5,"publicationDate":"2024-10-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142442008","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"OSCC-derived EVs educate fibroblasts and remodel collagen landscape","authors":"Cheng Miao ,&nbsp;Liu Liu ,&nbsp;Yubin Cao ,&nbsp;Zhishen Jiang ,&nbsp;Zhangfan Ding ,&nbsp;Yafei Chen ,&nbsp;Honglin Li ,&nbsp;Zhongkai Ma ,&nbsp;Pingchuan Ma ,&nbsp;Gaowei Zhang ,&nbsp;Longjiang Li ,&nbsp;Chunjie Li","doi":"10.1016/j.matbio.2024.10.004","DOIUrl":"10.1016/j.matbio.2024.10.004","url":null,"abstract":"<div><div>Cancer-associated myofibroblasts (mCAFs) represent a significant component of the tumor microenvironment due to their contributions to extracellular matrix (ECM) remodeling. The pro-tumor mechanisms of extracellular vesicles (EVs) by regulating mCAFs and related collagens remain poorly understood in oral squamous cell carcinoma (OSCC). In this study, through analysis of single-cell sequencing data and immunofluorescence staining, we confirmed the increased presence of mCAFs and enrichment of specific collagen types in OSCC tissues. Furthermore, we demonstrated that OSCC-derived EVs promote the transformation of fibroblasts into mCAFs, leading to tumor invasion. Proteomic analysis identified the presence of TGF-β1 in EVs and revealed its role in inducing mCAFs via the TGF-β1/SMAD signaling pathway. Experiments <em>in vivo</em> confirmed that EVs, particularly those carrying TGF-β1, trigger COL18^high COL5^high matrix deposition, thereby forming the pro-tumor ECM in OSCC. In summary, our investigation unveils the significant involvement of OSCC-derived EVs in orchestrating the differentiation of fibroblasts into mCAFs and modulating specific collagen types within the ECM. Therefore, this study provides a theoretical basis for targeting the EV-mediated TGF-β1 signaling pathway as a potential therapeutic strategy for OSCC.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"134 ","pages":"Pages 132-143"},"PeriodicalIF":4.5,"publicationDate":"2024-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142407110","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Loss of MMP9 disturbs cranial suture fusion via suppressing cell proliferation, chondrogenesis and osteogenesis in mice","authors":"Ming Liu ,&nbsp;Hanshu Zhang ,&nbsp;Yuanyuan Li ,&nbsp;Delan Huang ,&nbsp;Huanyan Zuo ,&nbsp;Jingwen Yang ,&nbsp;Zhi Chen","doi":"10.1016/j.matbio.2024.10.003","DOIUrl":"10.1016/j.matbio.2024.10.003","url":null,"abstract":"<div><div>Cranial sutures function as growth centers for calvarial bones. Abnormal suture closure will cause permanent cranium deformities. MMP9 is a member of the gelatinases that degrades components of the extracellular matrix. MMP9 has been reported to regulate bone development and remodeling. However, the function of MMP9 in cranial suture development is still unknown. Here, we identified that the expression of <em>Mmp9</em> was specifically elevated during fusion of posterior frontal (PF) suture compared with other patent sutures in mice. Interestingly, inhibition of MMP9 <em>ex vivo</em> or knockout of <em>Mmp9</em> in mice (<em>Mmp9^-/-</em>) disturbed the fusion of PF suture. Histological analysis showed that knockout of <em>Mmp9</em> resulted in wider distance between osteogenic fronts, suppressed cell condensation and endocranial bone formation in PF suture. Proliferation, chondrogenesis and osteogenesis of suture cells were decreased in <em>Mmp9^-/-</em> mice, leading to the PF suture defects. Moreover, transcriptome analysis of PF suture revealed upregulated ribosome biogenesis and downregulated IGF signaling associated with abnormal closure of PF suture in <em>Mmp9^-/-</em> mice. Inhibition of the ribosome biogenesis partially rescued PF suture defects caused by <em>Mmp9</em> knockout. Altogether, these results indicate that MMP9 is critical for the fusion of cranial sutures, thus suggesting MMP9 as a potential therapeutic target for cranial suture diseases.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"134 ","pages":"Pages 93-106"},"PeriodicalIF":4.5,"publicationDate":"2024-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142394779","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Myeloid deficiency of heparan sulfate 6-O-endosulfatases impairs bone marrow hematopoiesis","authors":"Anna K. Whitehead ,&nbsp;Zhangjie Wang ,&nbsp;Rebecca-Joe Boustany ,&nbsp;Romain R. Vivès ,&nbsp;Eric Lazartigues ,&nbsp;Jian Liu ,&nbsp;Robert W. Siggins ,&nbsp;Xinping Yue","doi":"10.1016/j.matbio.2024.10.002","DOIUrl":"10.1016/j.matbio.2024.10.002","url":null,"abstract":"<div><div>The heparan sulfate (HS) 6-<em>O</em>-endosulfatases or the Sulfs (Sulf1 and Sulf2) are the only known enzymes that can modify HS sulfation status extracellularly and have been shown to regulate diverse biological processes. The role of the Sulfs in bone marrow (BM) hematopoiesis is not known. In this study, we generated a novel mouse line with myeloid-specific deletion of the Sulfs by crossing Sulf1/2 double floxed mice with the <em>LysM-cre</em> line. The <em>LysM-Sulf</em> knockout (KO) male mice exhibited age-dependent expansion of hematopoietic stem cells and the granulocyte-monocyte lineages in the BM, whereas common lymphoid progenitors and B lymphocyte populations were significantly reduced. Although megakaryocytic and erythroid progenitors were not reduced in the BM, the <em>LysM-Sulf</em> KO males suffered age-dependent reduction of red blood cells (RBCs) and platelets in the peripheral blood, suggesting that the production of RBCs and platelets was arrested at later stages. In addition, <em>LysM-Sulf</em> KO males displayed progressive splenomegaly with extramedullary hematopoiesis. Compared to males, <em>LysM-Sulf</em> KO females exhibited a much-reduced phenotype, and ovariectomy had little effect. Mechanistically, reduced TGF-β/Smad2 but enhanced p53/p21 signaling were observed in male but not female <em>LysM-Sulf</em> KO mice. Finally, HS disaccharide analysis via LC-MS/MS revealed increased HS 6-<em>O</em>-sulfation in the BM from both male and female <em>LysM-Sulf</em> KO mice, however, the distribution of 6-<em>O</em>-sulfated motifs were different between the sexes with compensatory increase in Sulf1 expression observed only in <em>LysM-Sulf</em> KO females. In conclusion, our study reveals that myeloid deficiency of the Sulfs leads to multilineage abnormalities in BM hematopoiesis in an age- and sex-dependent manner.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"134 ","pages":"Pages 107-118"},"PeriodicalIF":4.5,"publicationDate":"2024-10-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142378505","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Matrix vesicles from osteoblasts promote atherosclerotic calcification","authors":"Xiaoli Wang ,&nbsp;Jie Ren ,&nbsp;Fei Fang ,&nbsp;Erxiang Wang ,&nbsp;Jianwei Li ,&nbsp;Weihong He ,&nbsp;Zhen Zhang ,&nbsp;Yang Shen ,&nbsp;Xiaoheng Liu","doi":"10.1016/j.matbio.2024.09.003","DOIUrl":"10.1016/j.matbio.2024.09.003","url":null,"abstract":"<div><div>Atherosclerotic calcification often coincides with osteoporosis, suggesting a potential interplay between bone and vascular mineralization. Osteoblast-derived matrix vesicles (Ost-MVs), pivotal in bone mineralization, have emerged as potential contributors to ectopic vascular calcification. However, the precise role of Ost-MVs in vascular calcification and the underlying mechanisms remain elusive. In this study, we observed a concomitant increase in atherosclerotic calcification and bone loss, accompanied by elevated release of Ost-MVs into circulation. We demonstrate that circulating Ost-MVs target plaque lesions in the setting of atherosclerosis. Mechanistically, vascular injury facilitates transendothelial transport of Ost-MVs, collagen І remodeling promotes Ost-MVs aggregation, and vascular smooth muscle cell (VSMC) phenotypic switching enhances MV uptake. These pathological changes during atherosclerosis collectively contribute to Ost-MVs recruitment into the vasculature. Furthermore, Ost-MVs and VSMC-derived matrix vesicles (VSMC-MVs) exacerbate calcification via the Ras-Raf-ERK pathway. Our findings unveil a novel Ost-MVs-mediated mechanism participating in vascular calcification and enriching our understanding of bone-vascular crosstalk.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"134 ","pages":"Pages 79-92"},"PeriodicalIF":4.5,"publicationDate":"2024-09-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142327452","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Inhibition of osteosarcoma metastasis in vivo by targeted downregulation of MMP1 and MMP9","authors":"Ofri Doppelt-Flikshtain ,&nbsp;Thabet Asbi ,&nbsp;Amin Younis ,&nbsp;Ofir Ginesin ,&nbsp;Ziv Cohen ,&nbsp;Tal Tamari ,&nbsp;Tal Berg ,&nbsp;Chen Yanovich ,&nbsp;Dvir Aran ,&nbsp;Yaniv Zohar ,&nbsp;Yehuda G. Assaraf ,&nbsp;Hadar Zigdon-Giladi","doi":"10.1016/j.matbio.2024.09.002","DOIUrl":"10.1016/j.matbio.2024.09.002","url":null,"abstract":"<div><p>Osteosarcoma (OS) mortality stems from lung metastases. Matrix metalloproteinases (MMPs) facilitate metastatic dissemination by degrading extracellular matrix components. Herein we studied the impact of targeted MMP downregulation on OS metastasis. Differential gene expression analysis of human OS cell lines revealed high MMP9 expression in the majority of OS cell lines. Furthermore, 143B, a metastatic OS cell line, exhibited increased MMP1 and MMP9 mRNA levels. Gene set enrichment analysis on metastatic and non-metastatic OS patient specimens indicated epithelial-mesenchymal transition as the most enriched gene set, with MMP9 displaying strong association to genes in this network. Using the same dataset, Kaplan-Meier analysis revealed a correlation between MMP1 expression and dismal patient survival. Hence, we undertook targeted suppression of MMP1 and MMP9 gene expression in OS cell lines. The ability of OS cells to migrate and form colonies was markedly reduced upon MMP1 and MMP9 downregulation, whereas their cell proliferation capacity remained intact. MMP9 downregulation decreased tumor growth and lung metastases area in an orthotopic mouse OS model. Consistently, human OS lung metastasis specimens displayed marked MMP9 protein expression. Our findings highlight the role of MMP1 and MMP9 in OS metastasis, warranting further exploration of simultaneous inhibition of MMPs for future OS therapeutics.</p></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"134 ","pages":"Pages 48-58"},"PeriodicalIF":4.5,"publicationDate":"2024-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142238487","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"PCPE-2 (procollagen C-proteinase enhancer-2): The non-identical twin of PCPE-1","authors":"Manon Napoli,&nbsp;Julien Bauer,&nbsp;Christelle Bonod,&nbsp;Sandrine Vadon-Le Goff,&nbsp;Catherine Moali","doi":"10.1016/j.matbio.2024.09.001","DOIUrl":"10.1016/j.matbio.2024.09.001","url":null,"abstract":"<div><div>PCPE-2 was discovered at the beginning of this century, and was soon identified as a close homolog of PCPE-1 (procollagen C-proteinase enhancer 1). After the demonstration that it could also stimulate the proteolytic maturation of fibrillar procollagens by BMP-1/tolloid-like proteinases (BTPs), PCPE-2 did not attract much attention as it was thought to fulfill the same functions as PCPE-1 which was already well-described. However, the tissue distribution of PCPE-2 shows both common points and significant differences with PCPE-1, suggesting that their activities are not fully overlapping. Also, the recently established connections between PCPE-2 (gene name <em>PCOLCE2</em>) and several important diseases such as atherosclerosis, inflammatory diseases and cancer have highlighted the need for a thorough reappraisal of the <em>in vivo</em> roles of this regulatory protein. In this context, the recent finding that, while retaining the ability to bind fibrillar procollagens and to activate their C-terminal maturation, PCPE-2 can also bind BTPs and inhibit their activity has substantially extended its potential functions. In this review, we describe the current knowledge about PCPE-2 with a focus on collagen fibrillogenesis, lipid metabolism and inflammation, and discuss how we could further advance our understanding of PCPE-2-dependent biological processes.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"134 ","pages":"Pages 59-78"},"PeriodicalIF":4.5,"publicationDate":"2024-09-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0945053X24001136/pdfft?md5=9dc9c6cca3ca66f81f90fa581c90b323&pid=1-s2.0-S0945053X24001136-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142299626","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}