Matrix Biology最新文献

{"title":"A CNA-35-based high-throughput fibrosis assay reveals ORAI1 as a regulator of collagen release from pancreatic stellate cells","authors":"Rieke Schleinhege ,&nbsp;Ilka Neumann ,&nbsp;Andrea Oeckinghaus ,&nbsp;Albrecht Schwab ,&nbsp;Zoltán Pethő","doi":"10.1016/j.matbio.2024.12.004","DOIUrl":"10.1016/j.matbio.2024.12.004","url":null,"abstract":"<div><h3>Rationale</h3><div>Pancreatic stellate cells (PSCs) produce a collagen-rich connective tissue in chronic pancreatitis and pancreatic ductal adenocarcinoma (PDAC). Ca²⁺-permeable ion channels such as ORAI1 are known to affect PSC proliferation and myofibroblastic phenotype. However, it is unknown whether these channels play a role in collagen secretion.</div></div><div><h3>Methods</h3><div>Using the PSC cell line PS-1, we characterized their cell-derived matrices using staining, mass spectroscopy, and cell migration assays. We developed and validated a high-throughput <em>in vitro</em> fibrosis assay to rapidly determine collagen quantity either with Sirius Red or, in the optimized version, with the collagen-binding peptide CNA-35-tdTomato. We assessed collagen deposition upon stimulating cells with transforming growth factor β1 (TGF-β1) and/or vitamin C without or with ORAI1 modulation. Orai1 expression was assessed by immunohistochemistry in the fibrotic tumor tissue of a murine PDAC model (KPfC).</div></div><div><h3>Results</h3><div>We found that TGF-β1 and vitamin C promote collagen deposition from PSCs. We used small interfering RNA (siRNA) and the inhibitor Synta-66 to demonstrate that ORAI1 regulates collagen secretion of PSCs but not NIH-3T3 fibroblasts. Physiological levels of vitamin C induce a drastic increase of the intracellular [Ca²⁺] in PSCs, with Synta-66 inhibiting Ca²⁺ influx. Lastly, we revealed Orai1 expression in cancer-associated fibroblasts (CAFs) in murine PDAC (KPfC) samples.</div></div><div><h3>Conclusion</h3><div>In conclusion, our study introduces a robust <em>in vitro</em> assay for fibrosis and identifies ORAI1 as being engaged in PSC-driven fibrosis.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"135 ","pages":"Pages 70-86"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142814711","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":"Fibrillin-1 G234D mutation in the hybrid1 domain causes tight skin associated with dysregulated elastogenesis and increased collagen cross-linking in mice","authors":"ASM Sakhawat Hossain ,&nbsp;Maria Thea Rane Dela Cruz Clarin ,&nbsp;Kenichi Kimura ,&nbsp;George Biggin ,&nbsp;Yuki Taga ,&nbsp;Koichiro Uto ,&nbsp;Ayana Yamagishi ,&nbsp;Eri Motoyama ,&nbsp;Narenmandula ,&nbsp;Kazunori Mizuno ,&nbsp;Chikashi Nakamura ,&nbsp;Keiichi Asano ,&nbsp;Sumio Ohtsuki ,&nbsp;Tomoyuki Nakamura ,&nbsp;Sachiko Kanki ,&nbsp;Clair Baldock ,&nbsp;Erna Raja ,&nbsp;Hiromi Yanagisawa","doi":"10.1016/j.matbio.2024.11.006","DOIUrl":"10.1016/j.matbio.2024.11.006","url":null,"abstract":"<div><div>Fibrillin-1, an extracellular matrix (ECM) protein encoded by the <em>FBN1</em> gene, serves as a microfibril scaffold crucial for elastic fiber formation and homeostasis in pliable tissue such as the skin. Aside from causing Marfan syndrome, some mutations in <em>FBN1</em> result in scleroderma, marked by hardened and thicker skin which limits joint mobility. Here, we describe a tight skin phenotype in the <em>Fbn1</em>^G234D/G234D mice carrying a corresponding variant of <em>FBN1</em> in the hybrid1 domain that was identified in a patient with familial aortic dissection. Unlike scleroderma, skin thickness and collagen fiber abundance do not change in the <em>Fbn1</em>^G234D/G234D mutant skin. Instead, increased collagen cross-links were observed. In addition, short elastic fibers were sparsely located underneath the panniculus muscle layer, and an abundance of thin, aberrant elastic fibers was increased within the subcutaneous fascia, which may have tightened skin attachment to the underlying skeletal muscle. Structurally, <em>Fbn1</em>^G234D/G234D microfibrils have a disrupted shoulder region that shares similarities with hybrid1 deletion mutant microfibrils. We then demonstrate the consequence of fibrillin-1 G234D mutation on dermal fibroblast functions. Mutant primary fibroblasts produce fewer elastic fibers, exhibit slower migration and increased cell stiffness. Moreover, secretome from mutant fibroblasts are marked by enhanced secretion of ECM, ECM-modifying enzymes, proteoglycans and cytokines, which are pro-tissue repair/fibrogenic. The transcriptome of mutant fibroblasts displays an increased expression of myogenic developmental and immune-related genes. Our study proposes that imbalanced ECM homeostasis due to a fibrillin-1 G234D mutation impacts fibroblast properties with potential ramifications on skin function.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"135 ","pages":"Pages 24-38"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11747857/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142774141","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":"Anticancer effect of a single-chain variable fragment against pro-matrix metalloproteinase-7 in colon cancer","authors":"Shinhye Min ,&nbsp;Bohee Jang ,&nbsp;Ji-Hye Yun ,&nbsp;Hyeonju Yang ,&nbsp;Jee Young Sung ,&nbsp;Ga-Eun Lim ,&nbsp;Yong-Nyun Kim ,&nbsp;Weontae Lee ,&nbsp;Eok-Soo Oh","doi":"10.1016/j.matbio.2024.12.009","DOIUrl":"10.1016/j.matbio.2024.12.009","url":null,"abstract":"<div><div>Disrupting the interaction between matrix metalloproteinase-7 (MMP-7) and syndecan-2 (SDC-2) can yield anticancer effects in colon cancer cells. Here, a single-chain variable fragment (scFv) targeting the pro-domain of MMP-7 was generated as a potential candidate anticancer agent. Among the generated scFvs, those designated 1B7 and 1C3 showed the strongest abilities to inhibit the ability of MMP-7 pro-domain to directly interact with SDC-2 in vitro and decrease the cancer activities of human HT29 colon adenocarcinoma cells. Consistently, 1B7 and 1C3 inhibited the cell-surface localization of pro-MMP-7, reduced the gelatinolytic activity of MMP-7, and suppressed the cancer activities of metastatic HCT116 human colon carcinoma cells. Notably, 1B7 inhibited the primary tumor growth and lung metastasis of CT26 mouse colon cancer cells in a mouse model. Compared to 1B7, the 1B7-Fc fusion antibody showed better anti-tumorigenic activity against HCT116 cells in culture and a syngeneic mouse model. Together, these data suggest that 1B7-Fc exerts anticancer effects by interfering with the interaction of MMP-7 and SDC-2 and could be a promising therapeutic antibody for colon cancer.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"135 ","pages":"Pages 125-134"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142889269","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":"Corrigendum to “Regulation of extracellular matrix degradation and metastatic spread by IQGAP1 through endothelin-1 receptor signalling in ovarian cancer” [Matrix Biol. 81 (2019) 17-33]","authors":"Lidia Chellini ,&nbsp;Valentina Caprara ,&nbsp;Francesca Spadaro ,&nbsp;Rosanna Sestito ,&nbsp;Anna Bagnato ,&nbsp;Laura Rosanò","doi":"10.1016/j.matbio.2024.11.003","DOIUrl":"10.1016/j.matbio.2024.11.003","url":null,"abstract":"","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"135 ","pages":"Page 161"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142734362","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":"Integrins and integrin-driven secretory pathways as multi-dimensional regulators of tumor-associated macrophage recruitment and reprogramming in tumor microenvironment","authors":"Nibedita Dalpati,&nbsp;Shubham Kumar Rai,&nbsp;Prerna Sharma,&nbsp;Pranita P. Sarangi","doi":"10.1016/j.matbio.2024.12.003","DOIUrl":"10.1016/j.matbio.2024.12.003","url":null,"abstract":"<div><div>Integrins, a group of transmembrane receptors, play a crucial role in mediating the interactions between cells and extracellular matrix (ECM) proteins. The intracellular signaling initiated by these cell-matrix interactions in leukocytes mediates many essential cellular processes such as survival, migration, metabolism, and other immunological functions. Macrophages, as phagocytes, participate in both proinflammatory and anti-inflammatory processes, including progression. Numerous reports have shown that the integrin-regulated secretome, comprising cytokines, chemokines, growth factors, proteases, and other bioactive molecules, is a crucial modulator of macrophage functions in tumors, significantly influencing macrophage programming and reprogramming within the tumor microenvironment (TME) in addition to driving their step-by-step entry process into tumor tissue spaces. Importantly, studies have demonstrated a pivotal role for integrin receptor-mediated secretome and associated signaling pathways in functional reprogramming from anti-tumorigenic to pro-tumorigenic phenotype in tumor-associated macrophages (TAMs). In this comprehensive review, we have provided an in-depth analysis of the latest findings of various key pathways, mediators, and signaling cascades associated with integrin-driven polarization of macrophages in tumors. This manuscript will provide an updated understanding of the modulation of inflammatory monocytes/ macrophages and TAMs by integrin-driven secretory pathways in various functions such as migration, differentiation, and their role in tumor progression, angiogenesis, and metastasis.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"135 ","pages":"Pages 55-69"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142792511","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":"Basement membranes in lung metastasis growth and progression","authors":"Irene Torre-Cea,&nbsp;Patricia Berlana-Galán,&nbsp;Elena Guerra-Paes,&nbsp;Daniel Cáceres-Calle,&nbsp;Iván Carrera-Aguado,&nbsp;Laura Marcos-Zazo,&nbsp;Fernando Sánchez-Juanes ,&nbsp;José M. Muñoz-Félix","doi":"10.1016/j.matbio.2024.12.008","DOIUrl":"10.1016/j.matbio.2024.12.008","url":null,"abstract":"<div><div>The lung is a highly vascularized tissue that often harbors metastases from various extrathoracic malignancies. Lung parenchyma consists of a complex network of alveolar epithelial cells and microvessels, structured within an architecture defined by basement membranes. Consequently, understanding the role of the extracellular matrix (ECM) in the growth of lung metastases is essential to uncover the biology of this pathology and developing targeted therapies. These basement membranes play a critical role in the progression of lung metastases, influencing multiple stages of the metastatic cascade, from the acquisition of an aggressive phenotype to intravasation, extravasation and colonization of secondary sites. This review examines the biological composition of basement membranes, focusing on their core components—collagens, fibronectin, and laminin—and their specific roles in cancer progression. Additionally, we discuss the function of integrins as primary mediators of cell adhesion and signaling between tumor cells, basement membranes and the extracellular matrix, as well as their implications for metastatic growth in the lung. We also explore vascular co-option (VCO) as a form of tumor growth resistance linked to basement membranes and tumor vasculature. Finally, the review covers current clinical therapies targeting tumor adhesion, extracellular matrix remodeling, and vascular development, aiming to improve the precision and effectiveness of treatments against lung metastases.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"135 ","pages":"Pages 135-152"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142886380","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":"Impact of vascular Ehlers-Danlos Syndrome-associated Gly substitutions on structure, function, and mechanics using bacterial collagen","authors":"Sonal Gahlawat ,&nbsp;Jan Siess ,&nbsp;Natalie Losada ,&nbsp;Jennifer Timm ,&nbsp;Vikas Nanda ,&nbsp;David I. Shreiber","doi":"10.1016/j.matbio.2024.12.002","DOIUrl":"10.1016/j.matbio.2024.12.002","url":null,"abstract":"<div><div>Vascular Ehlers-Danlos syndrome (vEDS) arises from mutations in collagen-III, a major structural component of the extracellular matrix (ECM) in vascularized tissues, including blood vessels. Fibrillar collagens form a triple-helix that is characterized by a canonical (Gly-X-Y)_n sequence. The substitution of another amino acid for Gly within this conserved repeating sequence is associated with several hereditary connective tissue disorders, including vEDS. The clinical severity of vEDS depends on the identity of the substituted amino acid and its location. In this study, we engineered recombinant bacterial collagen-like proteins (CLPs) with previously reported Gly→X (X=Ser or Arg) vEDS substitutions within the integrin-binding site. Employing a combination of biophysical techniques, enzymatic digestion assays, integrin binding affinity assays, and computational modeling, we assessed the impact of Gly→X substitutions on structure, stability, function, and mechanical properties. While constructs with Ser or Arg substitutions maintained a triple-helix structure, Arg substitution significantly reduced global thermal stability, heightened susceptibility to trypsin digestion, and altered integrin α2-inserted (α2I) domain binding. Molecular dynamics (MD) simulations also demonstrated distinct effects of different Gly substitutions on the triple-helix structure - Arg substitutions induced notable bulging at the substitution site and disrupted interchain hydrogen bonds compared to Ser substitutions. Additionally, steered MD simulations revealed that Arg substitution led to a significant decrease in the Young's modulus of the triple-helix. Bacterial CLPs have proved to be a powerful model for studying the underlying mechanisms of vEDS-causing mutations in collagen-III. Serine and arginine substitutions differentially perturb cell-matrix interactions and ECM in a manner consistent with clinical vEDS severity.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"135 ","pages":"Pages 87-98"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142792505","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":"AGEing of collagen: The effects of glycation on collagen’s stability, mechanics and assembly","authors":"Daniel Sloseris,&nbsp;Nancy R. Forde","doi":"10.1016/j.matbio.2024.12.007","DOIUrl":"10.1016/j.matbio.2024.12.007","url":null,"abstract":"<div><div>Advanced Glycation End Products (AGEs) are the end result of the irreversible, non-enzymatic glycation of proteins by reducing sugars. These chemical modifications accumulate with age and have been associated with various age-related and diabetic complications. AGEs predominantly accumulate on proteins with slow turnover rates, of which collagen is a prime example. Glycation has been associated with tissue stiffening and reduced collagen fibril remodelling. In this study, we investigate the effects of glycation on the stability of type I collagen, its molecular-level mechanics and its ability to perform its physiological role of self-assembly. Collagen AGEing is induced <em>in vitro</em> by incubation with ribose. We confirm and assess glycation using fluorescence measurements and changes in collagen’s electrophoretic mobility. Susceptibility to trypsin digestion and circular dichroism (CD) spectroscopy are used to probe changes in collagen’s triple helical stability, revealing decreased stability due to glycation. Atomic Force Microscopy (AFM) imaging is used to quantify how AGEing affects collagen flexibility, where we find molecular-scale stiffening. Finally we use microscopy to show that glycated collagen molecules are unable to self-assemble into fibrils. These findings shed light on the molecular mechanisms underlying AGE-induced tissue changes, offering insight into how glycation modifies protein structure and stability.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"135 ","pages":"Pages 153-160"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142911625","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":"George R. Martin: Pioneering matrix biologist","authors":"Andrew Leask ,&nbsp;Richard J. Stratton","doi":"10.1016/j.matbio.2025.01.007","DOIUrl":"10.1016/j.matbio.2025.01.007","url":null,"abstract":"","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"136 ","pages":"Pages 69-70"},"PeriodicalIF":4.5,"publicationDate":"2025-01-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143057377","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":"Spatial localization of collagen hydroxylated proline site variation as an ancestral trait in the breast cancer microenvironment","authors":"Harrison Taylor ,&nbsp;Laura Spruill ,&nbsp;Heather Jensen-Smith ,&nbsp;Denys Rujchanarong ,&nbsp;Taylor Hulahan ,&nbsp;Ashlyn Ivey ,&nbsp;Alex Siougiannis ,&nbsp;Jennifer R. Bethard ,&nbsp;Lauren E. Ball ,&nbsp;George E. Sandusky ,&nbsp;M.A. Hollingsworth ,&nbsp;Jeremy L. Barth ,&nbsp;Anand S. Mehta ,&nbsp;Richard R. Drake ,&nbsp;Jeffrey R. Marks ,&nbsp;Harikrishna Nakshatri ,&nbsp;Marvella Ford ,&nbsp;Peggi M. Angel","doi":"10.1016/j.matbio.2025.01.006","DOIUrl":"10.1016/j.matbio.2025.01.006","url":null,"abstract":"<div><div>Collagen stroma interactions within the extracellular microenvironment of breast tissue play a significant role in breast cancer, including risk, progression, and outcomes. Hydroxylation of proline (HYP) is a common post-translational modification directly linked to breast cancer survival and progression. Changes in HYP status lead to alterations in epithelial cell signaling, extracellular matrix remodeling, and immune cell recruitment. In the present study, we test the hypothesis that the breast cancer microenvironment presents unique PTMs of collagen, which form bioactive domains at these sites that are associated with spatial histopathological characteristics and influence breast epithelial cell signaling. Mass spectrometry imaging proteomics targeting collagens were paired with comprehensive proteomic methods to identify novel breast cancer-related collagen domains based on spatial localization and regulation in 260 breast tissue samples. As ancestry plays a significant role in breast cancer outcomes, these methods were performed on ancestry diverse breast cancer tissues. Lumpectomies from the Cancer Genome Atlas (TCGA; n=10) reported increased levels of prolyl 4-hydroxylase subunit alpha-3 (P4HA3) accompanied by spatial regulation of fibrillar collagen protein sequences. A concise set of triple negative breast cancer lumpectomies (n=10) showed spatial regulation of specific domain sites from collagen alpha-1(I) chain. Tissue microarrays identified proteomic alterations around post-translationally modified collagen sites in healthy breast (n=81) and patient matched normal adjacent (NAT; n=76) and invasive ductal carcinoma (n=83). A collagen alpha-1(I) chain domain encompassing amino acids 506–514 with site-specific proline hydroxylation reported significant alteration between patient matched normal adjacent tissue and invasive breast cancer. Functional testing of domain 506–514 on breast cancer epithelial cells showed proliferation, chemotaxis and cell signaling response dependent on site localization of proline hydroxylation within domain 506–514 variants. These findings support site localized collagen HYP forms novel bioactive domains that are spatially distributed within the breast cancer microenvironment and may play a role in ancestral traits of breast cancer.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"136 ","pages":"Pages 71-86"},"PeriodicalIF":4.5,"publicationDate":"2025-01-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143042706","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}