Matrix Biology Plus最新文献

英文中文

Convergence research in matrix biology and biomaterials science 基质生物学与生物材料科学的融合研究

Q1 Medicine

Matrix Biology Plus

Pub Date : 2025-12-01 Epub Date: 2025-06-24 DOI: 10.1016/j.mbplus.2025.100180

Daniel L. Alge , Ashley Brown

引用次数: 0

Corrigendum to “Presence of type IIB procollagen in mouse articular cartilage and growth plate is revealed by immuno-histochemical analysis with a novel specific antibody” [Matrix Biol. Plus 18 (2023) 100130] “用一种新的特异性抗体进行免疫组织化学分析，发现小鼠关节软骨和生长板中存在IIB型前胶原蛋白”[Matrix Biol]的更正。加18 (2023)100130]

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Matrix Biology Plus

Pub Date : 2025-12-01 Epub Date: 2025-06-14 DOI: 10.1016/j.mbplus.2025.100177

Emeline Perrier-Groult, Shérine Moustaghfir, Marielle Pasdeloup, Jean-Daniel Malcor, Jérôme Lafont, Frédéric Mallein-Gerin

引用次数: 0

Corrigendum to “Obesity-driven changes in breast extracellular matrix exhibit a pro-angiogenic phenotype” [Matrix Biol. Plus 24 (2024) 100162] “肥胖驱动的乳腺细胞外基质变化表现出促血管生成表型”的更正[基质生物学]。加24 (2024)100162]

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Matrix Biology Plus

Pub Date : 2025-12-01 Epub Date: 2025-06-17 DOI: 10.1016/j.mbplus.2025.100178

Ellen E. Bamberg , Mark Maslanka , Kiran Vinod-Paul , Sharon Sams , Erica Pollack , Matthew Conklin , Peter Kabos , Kirk C. Hansen

引用次数: 0

Exosome enriched serum enhances engineered ligament mechanics and collagen content with no additional benefit of resistance exercise. 外泌体富集血清增强工程韧带力学和胶原蛋白含量，没有额外的好处阻力运动。

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Matrix Biology Plus

Pub Date : 2025-08-08 eCollection Date: 2025-08-01 DOI: 10.1016/j.mbplus.2025.100181

Kevin J M Paulussen, Christopher M T Hayden, Taylor Griffin, Keith Baar

Following resistance exercise, systemic changes foster improved functionality of tendons and ligaments. Post-exercise, muscle tissue releases exosomes that are thought to facilitate inter-tissue communication. To determine the potential role of exosomes in the exercise-induced adaptations of tendons and ligaments, we modified our engineered human ligament (EHL) model to work with exosome-enriched serum. Treatment of the EHLs with exosomes enriched from fetal bovine serum (fbEXO) resulted in enhanced ligament mechanics and increased collagen content in a dose-response fashion (maximum tensile load [MTL]: 10 %: 0.196 ± 0.138 N, 20 %: 0.278 ± 0.103 N, 40 %: 0.840 ± 0.092 N; r² = 0.858, P < 0.0001; collagen content: 10 %: 1.073 ± 12.49 µg, 20 %: 86.43 ± 71.65 µg, 40 %: 145.7 ± 84.11 µg; r² = 0.4735, P = 0.0046). After optimizing an exosome enriched feeding protocol using fbEXO, we confirmed that exosomes enriched from human serum (hsEXO) could sustain EHL function. Subsequently, twelve healthy, recreationally active volunteers (22 ± 3 y, 1,68 ± 0.10 m, 65.6 ± 27.8 kg; 6F/6M) performed a single bout of resistance exercise. Serum samples were collected prior to and 15 min post-exercise, and exosomes were enriched from these samples for treatment of EHLs. EHL function and collagen content did not differ when treated with hsEXO obtained at rest or post-resistance exercise (MTL: 1.30 ± 0.36 vs. 1.20 ± 0.36 N, P = 0.3950; collagen content: 424.6 ± 47.68 vs. 425.2 ± 44.46 µg, P = 0.9663). This model provides a novel way to determine the role of exosomes in connective tissue development and adaptation. The identification of circulating exercise factors that enhance tendon and ligament function remains to be fully elucidated.

在抗阻运动之后，全身的变化促进了肌腱和韧带功能的改善。运动后，肌肉组织释放被认为促进组织间交流的外泌体。为了确定外泌体在运动诱导的肌腱和韧带适应性中的潜在作用，我们修改了我们的工程人韧带（EHL）模型，使其与外泌体富集的血清一起工作。胎牛血清富外泌体（fbEXO）处理EHLs后，韧带力学增强，胶原含量呈剂量-效应增加（最大拉伸载荷[MTL]: 10%: 0.196±0.138 N, 20%: 0.278±0.103 N, 40%: 0.840±0.092 N; r2 = 0.858, p2 = 0.4735, P = 0.0046）。在使用fbEXO优化了外泌体富集喂养方案后，我们证实了从人血清中富集的外泌体（hsEXO）可以维持EHL功能。随后，12名健康、娱乐活动的志愿者（22±3岁、1、68±0.10米、65.6±27.8公斤；6F/6M）进行单次阻力运动。在运动前和运动后15分钟收集血清样本，并从这些样本中富集外泌体用于治疗EHLs。静息或阻力运动后获得的hsEXO对EHL功能和胶原含量无显著影响（MTL: 1.30±0.36 vs 1.20±0.36 N, P = 0.3950；胶原含量：424.6±47.68 vs 425.2±44.46µg, P = 0.9663）。该模型为确定外泌体在结缔组织发育和适应中的作用提供了一种新的方法。增强肌腱和韧带功能的循环运动因子的鉴定仍有待充分阐明。

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引用次数: 0

Proteomic characterization of type I collagen N-terminal crosslinked peptides I型胶原n端交联肽的蛋白质组学特征

Q1 Medicine

Matrix Biology Plus

Pub Date : 2025-08-01 Epub Date: 2025-06-19 DOI: 10.1016/j.mbplus.2025.100179

Zsuzsanna Darula , Maxwell C. McCabe , Alex Barrett , Lauren R. Schmitt , Mark D. Maslanka , Anthony J Saviola , Joseph Orgel , Alma Burlingame , Claudia A. Staab-Weijnitz , Kurt Stenmark , Valerie Weaver , Robert J. Chalkley , Kirk C. Hansen

Collagen cross-links mediated by the lysyl oxidase and lysyl hydroxylase families of enzymes significantly contribute to the biomechanical strength and rigidity of tissues, influencing cell signaling and the downstream cell phenotype. In the clinic, the proteolytically liberated N-terminal cross-linked peptide of collagen I (NTX) is used as a biomarker of bone and connective tissue turnover, which is altered in several disease processes. Despite the clinical utility of these collagen breakdown products, the majority of the cross-linked peptide species have not been identified in proteomic datasets. Here, we evaluate several parameters for the preparation and identification of these peptides from the collagen I-rich Achilles tendon. Our refined approach, which involves chemical digestion for protein solubilization coupled with mass spectrometry, enables the identification of NTX cross-links in a range of modification states. We then applied a spectral library approach to identify differences in collagen cross-links in bovine pulmonary hypertension. The presented method offers unique opportunities to understand extracellular matrix remodeling events in development, aging, wound healing, and fibrotic disease that modulate collagen architecture through lysyl hydroxylase and lysyl oxidase enzymes.

由赖氨酸氧化酶和赖氨酸羟化酶家族介导的胶原交联显著促进组织的生物力学强度和刚度，影响细胞信号传导和下游细胞表型。在临床上，蛋白水解释放的I型胶原蛋白n端交联肽（NTX）被用作骨和结缔组织转换的生物标志物，在几种疾病过程中发生改变。尽管这些胶原蛋白分解产物具有临床应用价值，但大多数交联肽种类尚未在蛋白质组学数据集中被鉴定出来。在这里，我们评估了从富含胶原i的跟腱中制备和鉴定这些肽的几个参数。我们的改进方法，包括化学消化蛋白溶解与质谱结合，能够识别一系列修饰状态下的NTX交联。然后，我们应用光谱库方法来识别牛肺动脉高压中胶原交联的差异。所提出的方法提供了独特的机会来了解细胞外基质重塑事件在发育、衰老、伤口愈合和纤维化疾病中，通过赖基羟化酶和赖基氧化酶调节胶原结构。

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引用次数: 0

Small Integrin binding Ligand N-linked Glycoproteins, prostate-specific antigen and time to prostate cancer diagnosis 小整合素结合配体n -连接糖蛋白，前列腺特异性抗原和前列腺癌诊断的时间

Q1 Medicine

Matrix Biology Plus

Pub Date : 2025-06-01 Epub Date: 2025-03-23 DOI: 10.1016/j.mbplus.2025.100171

Alka Jain , Ying Ni , Daisy Zhang , Eleanor M. Simonsick , E. Jeffrey Metter , Kalu U. Ogbureke , Larry W. Fisher , Neal S. Fedarko

Background: Small Integrin Binding Ligand N-linked Glycoproteins (SIBLINGs¹) were associated with cancer in cross-sectional studies. Whether SIBLINGs associate with preclinical disease is unknown. Methods: A retrospective longitudinal case control study was performed to determine the association of SIBLINGs and prostate-specific antigen (PSA) with preclinical disease. Paired serum samples from 109 cancer-free Baltimore Longitudinal Study on Aging participants were divided into those that were either most distal or proximal to diagnosis (cases) or censored (controls). Dentin sialophosphoprotein (DSPP), bone sialoprotein (BSP), osteopontin (OPN), and PSA were measured by immunoassay and dichotomized into low or high based on their respective cut-off values. Associations of time to diagnosis or death, modeled as disease-free survival (DFS) or overall survival (OS), were assessed using Kaplan Meier and Cox proportional hazard survival estimates on individual and aggregated biomarkers in distal or proximal sets separately. Models were adjusted for relevant covariates. A false discovery rate analysis assessed significance of hazard ratios (HRs) in sets. Results: Biomarkers/aggregates identified as true discoveries for DFS included DSPP + PSA, OPN + PSA, DSPP + BSP + PSA, DSPP + OPN + PSA, where unadjusted distal HRs ranged between 11 and 27 and after adjusting for age from 7 to 15, while proximal HRs ranged between 6 and 10 unadjusted and 5 to 12 after adjusting for age. For proximal OS, true discoveries included DSPP + BSP, DSPP + OPN, DSPP + BSP + OPN, and DSPP + OPN + PSA where unadjusted HRs ranged between 6 and 20 while age-adjusted HRs ranged between 5 and 12. Conclusions: These observations support SIBLINGs as biomarkers that associate with DFS and OS in prediagnosis samples.

背景：在横断面研究中，小整合素结合配体n -连接糖蛋白（SIBLINGs1）与癌症相关。兄弟姐妹是否与临床前疾病相关尚不清楚。方法：进行回顾性纵向病例对照研究，以确定兄弟姐妹和前列腺特异性抗原（PSA）与临床前疾病的关系。来自109名无癌症巴尔的摩纵向衰老研究参与者的配对血清样本被分为离诊断最远或最近的（病例）或被删除的（对照组）。采用免疫分析法测定牙本质唾液蛋白（DSPP）、骨唾液蛋白（BSP）、骨桥蛋白（OPN）和PSA，并根据各自的临界值将其分为低或高。以无病生存期（DFS）或总生存期（OS）为模型，分别使用Kaplan Meier和Cox比例风险生存估计对远端或近端组的个体和聚合生物标志物进行评估。对模型进行相关协变量调整。错误发现率分析评估了组间风险比（hr）的显著性。结果：确定为DFS的真正发现的生物标志物/聚集物包括DSPP + PSA， OPN + PSA, DSPP + BSP + PSA, DSPP + OPN + PSA，其中未调整的远端hr介于11至27之间，调整年龄为7至15岁，而近端hr介于6至10之间，调整年龄后为5至12。对于近端OS，真正的发现包括DSPP + BSP， DSPP + OPN， DSPP + BSP + OPN和DSPP + OPN + PSA，未调整的hr范围在6至20之间，而年龄调整的hr范围在5至12之间。结论：这些观察结果支持兄弟姐妹在诊断前样本中作为与DFS和OS相关的生物标志物。

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引用次数: 0

The staphylococcal collagen adhesin CNA35 effectively detects collagen and its fragments in blots after SDS-PAGE 葡萄球菌胶原粘连蛋白CNA35在SDS-PAGE后可有效检测胶原及其片段的印迹

Q1 Medicine

Matrix Biology Plus

Pub Date : 2025-06-01 Epub Date: 2025-05-15 DOI: 10.1016/j.mbplus.2025.100174

Elena N. Pokidysheva , Jennifer Diaz Sales , Shinomi Yagi , Tomonori Ueno , Kanako Sasai , Alice Makarenko , Hans Peter Bächinger , Kazunori Mizuno , Sergei P. Boudko

Collagens are a diverse family of proteins present in the extracellular matrix (ECM) of all animals. They play crucial roles in providing structural support to tissues, forming scaffolds for ECM suprastructures, and signaling cells. Certain collagen-binding proteins from pathogenic bacteria, such as CollageN Adhesin (CNA) from Staphylococcus aureus, interact with the collagen triple helix to promote host invasion. The extracellular portion of CNA, known as CNA35, which has a molecular weight of 35 kDa, has been used for in vitro, ex vivo, and in vivo staining of various collagen types in tissues.

Detecting various types of collagens necessitates the use of type- and specie-specific antibodies, which typically exhibit weak affinities for the triple helical regions of collagens. Additionally, the fragmentation of collagens can lead to a loss of detection due to the limited number of available epitopes. Furthermore, antibodies can be expensive, require secondary identification methods, and are often suitable for either immunohistochemistry or western blotting. Although successful procedures for staining collagens in tissues have been implemented, the detection of collagens and their fragments using CNA35 has not been reported for protein blots.

In this study, we examined the detection capabilities of a trimeric form of CNA35 for protein blots following SDS-PAGE. We successfully tested collagens I through VI, as well as fragments of collagen IV, under various conditions. Additionally, we investigated the impact of blocking solutions, incubation time, ligand concentration, and CNA35 concentration on sensitivity.

We achieved superior detection of all tested collagens and collagen IV fragments, including the 7S domain, which is a highly crosslinked complex composed of four triple-helical strands. The method we developed serves as a universal tool for detecting collagens and collagen-containing peptides in protein blots. It offers several advantages, including sub-nanogram sensitivity, low cost, and compatibility with standard western blotting techniques.

胶原蛋白是存在于所有动物细胞外基质（ECM）中的多种蛋白质家族。它们在为组织提供结构支持，形成ECM上层结构的支架和信号细胞中起着至关重要的作用。来自致病菌的某些胶原结合蛋白，如来自金黄色葡萄球菌的胶原粘连素（CNA），与胶原三螺旋相互作用，促进宿主入侵。CNA的细胞外部分被称为CNA35，分子量为35 kDa，已被用于组织中各种胶原类型的体外、离体和体内染色。检测各种类型的胶原需要使用类型和物种特异性抗体，这些抗体通常对胶原的三螺旋区域表现出弱亲和力。此外，由于可用的表位数量有限，胶原的碎片化可能导致检测损失。此外，抗体可能很昂贵，需要二次鉴定方法，并且通常适用于免疫组织化学或免疫印迹。虽然已经成功地实现了组织中胶原染色的方法，但使用CNA35检测胶原及其片段的蛋白印迹尚未见报道。在这项研究中，我们检测了三聚体形式的CNA35在SDS-PAGE之后对蛋白质印迹的检测能力。我们在各种条件下成功测试了I - VI胶原蛋白，以及IV胶原蛋白的片段。此外，我们还研究了阻断溶液、孵育时间、配体浓度和CNA35浓度对敏感性的影响。我们对所有被测试的胶原和IV型胶原片段，包括7S结构域，这是一个由四条三螺旋链组成的高度交联的复合物，都实现了出色的检测。我们开发的方法可作为检测胶原蛋白和含胶原蛋白肽的通用工具。它具有几个优点，包括亚纳克灵敏度、低成本和与标准western印迹技术的兼容性。

{"title":"The staphylococcal collagen adhesin CNA35 effectively detects collagen and its fragments in blots after SDS-PAGE","authors":"Elena N. Pokidysheva , Jennifer Diaz Sales , Shinomi Yagi , Tomonori Ueno , Kanako Sasai , Alice Makarenko , Hans Peter Bächinger , Kazunori Mizuno , Sergei P. Boudko","doi":"10.1016/j.mbplus.2025.100174","DOIUrl":"10.1016/j.mbplus.2025.100174","url":null,"abstract":"<div><div>Collagens are a diverse family of proteins present in the extracellular matrix (ECM) of all animals. They play crucial roles in providing structural support to tissues, forming scaffolds for ECM suprastructures, and signaling cells. Certain collagen-binding proteins from pathogenic bacteria, such as CollageN Adhesin (CNA) from <em>Staphylococcus aureus</em>, interact with the collagen triple helix to promote host invasion. The extracellular portion of CNA, known as CNA35, which has a molecular weight of 35 kDa, has been used for <em>in vitro</em>, <em>ex vivo</em>, and <em>in vivo</em> staining of various collagen types in tissues.</div><div>Detecting various types of collagens necessitates the use of type- and specie-specific antibodies, which typically exhibit weak affinities for the triple helical regions of collagens. Additionally, the fragmentation of collagens can lead to a loss of detection due to the limited number of available epitopes. Furthermore, antibodies can be expensive, require secondary identification methods, and are often suitable for either immunohistochemistry or western blotting. Although successful procedures for staining collagens in tissues have been implemented, the detection of collagens and their fragments using CNA35 has not been reported for protein blots.</div><div>In this study, we examined the detection capabilities of a trimeric form of CNA35 for protein blots following SDS-PAGE. We successfully tested collagens I through VI, as well as fragments of collagen IV, under various conditions. Additionally, we investigated the impact of blocking solutions, incubation time, ligand concentration, and CNA35 concentration on sensitivity.</div><div>We achieved superior detection of all tested collagens and collagen IV fragments, including the 7S domain, which is a highly crosslinked complex composed of four triple-helical strands. The method we developed serves as a universal tool for detecting collagens and collagen-containing peptides in protein blots. It offers several advantages, including sub-nanogram sensitivity, low cost, and compatibility with standard western blotting techniques.</div></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"26 ","pages":"Article 100174"},"PeriodicalIF":0.0,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144135126","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Crosstalk between T cells and fibroblasts in biomaterial-mediated fibrosis 生物材料介导纤维化中T细胞和成纤维细胞间的串扰

Q1 Medicine

Matrix Biology Plus

Pub Date : 2025-06-01 Epub Date: 2025-03-23 DOI: 10.1016/j.mbplus.2025.100172

Mathew Kibet, Daniel Abebayehu

Biomaterial implants are a critical aspect of our medical therapies and biomedical research and come in various forms: stents, implantable glucose sensors, orthopedic implants, silicone implants, drug delivery systems, and tissue engineered scaffolds. Their implantation triggers a series of biological responses that often times lead to the foreign body response and subsequent fibrotic encapsulation, a dense ECM-rich capsule that isolates the biomaterial and renders it ineffective. These responses lead to the failure of biomaterials and is a major hurdle to overcome and in promoting their success. Much attention has been given to macrophage populations for the inflammatory component of these responses to biomaterials but recent work has identified an important role of T cells and their ability to modulate fibroblast activity and vice versa. In this review, we focus on T cell-fibroblast crosstalk by exploring T cell subsets, critical signaling pathways, and fibroblast populations that have been shown to dictate biomaterial-mediated fibrosis. We then highlight emerging technologies and model systems that enable new insights and avenues to T cell-fibroblast crosstalk that will improve biomaterial outcomes.

生物材料植入物是我们医学治疗和生物医学研究的一个重要方面，有各种形式：支架、植入式葡萄糖传感器、骨科植入物、硅胶植入物、药物输送系统和组织工程支架。它们的植入引发了一系列的生物反应，通常会导致异物反应和随后的纤维化包封，这是一种致密的富含ecm的胶囊，可以隔离生物材料并使其失效。这些反应导致生物材料的失败，是克服和促进其成功的主要障碍。巨噬细胞群体对这些生物材料反应的炎症成分受到了很多关注，但最近的工作已经确定了T细胞及其调节成纤维细胞活性的能力的重要作用，反之亦然。在这篇综述中，我们通过探索T细胞亚群、关键信号通路和已被证明决定生物材料介导的纤维化的成纤维细胞群体，重点关注T细胞与成纤维细胞的串扰。然后，我们重点介绍了新兴技术和模型系统，这些技术和模型系统可以为T细胞-成纤维细胞串扰提供新的见解和途径，从而改善生物材料的结果。

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引用次数: 0

Development of an in vitro platform for epithelial-stromal interactions: A basement membrane-containing scaffold from decellularized porcine bladders 上皮-间质相互作用的体外平台的开发：从脱细胞的猪膀胱中提取含基底膜的支架

Q1 Medicine

Matrix Biology Plus

Pub Date : 2025-06-01 Epub Date: 2025-02-22 DOI: 10.1016/j.mbplus.2025.100169

J.A. Ramirez , S. Estrada , M.C. Harmsen , P.K. Sharma

The first organized extracellular matrix that appears during mammalian embryogenesis is a basement membrane (BM), BM is present in all adult epithelia, endothelia, muscle, nerve and fat tissues. BM is a sub-micrometer thick compact lattice of macromolecules that is maintained by the adhered cells. Systems such as collagen gels, Matrigel® or synthetic polymeric scaffolds have been proposed to mimic the BM and to study the interactions between different cell types, but all lack a structured BM. Here we aimed to obtain and characterize a natural, thin basement membrane-containing scaffold from pig urinary bladders that are subjected to blunt dissection of layers and decellularization steps, preserving the near native BM with a few layers of underlying connective tissue to maintain its structural integrity. The scanning electron microscopy, confocal multiphoton microscopy and immunohistochemistry helped confirm the presence of the BM. A veil-like network composed of thin fibers was present on top of a course network, and glycosaminoglycans, collagen and basement membrane proteins were present. The scaffold’s ability to repopulation and basement membrane barrier function were further confirmed when HaCaT and MRC5 cells attached and remained respectively on the epithelial and mesenchymal side without any crossover. Cells remained viable till 2 weeks. This BM-containing scaffold allows to create in vitro models of epithelial-mesenchymal tissues through a structured basement membrane and investigate basement membrane dynamics. The basement membrane-containing scaffold was found to be isotropic under uniaxial tension with a failure strain of 0.25 allowing its use to investigate strain induced basement membrane dynamics.

在哺乳动物胚胎发生过程中出现的第一个有组织的细胞外基质是基底膜（BM），基底膜存在于所有成人上皮、内皮、肌肉、神经和脂肪组织中。BM是一种亚微米厚的紧密的大分子晶格，由粘附的细胞维持。胶原凝胶、Matrigel®或合成聚合物支架等系统已被提出用于模拟基质并研究不同细胞类型之间的相互作用，但都缺乏结构化的基质。在这里，我们旨在从猪膀胱中获得并表征一种天然的、含有薄基底膜的支架，该支架经过钝性层剥离和脱细胞步骤，保留了接近天然的基底膜和几层底层结缔组织，以保持其结构完整性。扫描电镜，共聚焦多光子显微镜和免疫组织化学证实了BM的存在。在层状网络的顶部有一个由薄纤维组成的面纱状网络，并存在糖胺聚糖、胶原蛋白和基底膜蛋白。当HaCaT和MRC5细胞分别附着并停留在上皮和间质侧而没有任何交叉时，进一步证实了支架的再生能力和基底膜屏障功能。细胞存活至2周。这种含bm的支架可以通过结构基膜创建上皮-间质组织的体外模型，并研究基膜动力学。发现含有基底膜的支架在单轴拉伸下具有各向同性，破坏应变为0.25，允许其用于研究应变诱导的基底膜动力学。

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引用次数: 0

Erratum to “Proteomic profiling of the extracellular matrix in the human adrenal cortex” [Matrix Biology Plus 23 (2024) 100158] 对“人类肾上腺皮质细胞外基质的蛋白质组学分析”的勘误[matrix Biology Plus 23 (2024) 100158]

Q1 Medicine

Matrix Biology Plus

Pub Date : 2025-06-01 Epub Date: 2025-04-25 DOI: 10.1016/j.mbplus.2025.100173

Jean Lucas Kremer , Henrique Sanchez Ortega , Talita Souza-Siqueira , Claudia Blanes Angeli , Leo Kei Iwai , Giuseppe Palmisano , Claudimara Ferini Pacicco Lotfi

引用次数: 0

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