Native human collagen type I provides a viable physiologically relevant alternative to xenogeneic sources for tissue engineering applications: A comparative in vitro and in vivo study.
Native human collagen type I provides a viable physiologically relevant alternative to xenogeneic sources for tissue engineering applications: A comparative in vitro and in vivo study.
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天然人 I 型胶原蛋白为组织工程应用提供了一种可行的生理相关替代异种来源：体外和体内比较研究。
DOI：
10.1002/jbm.b.35080
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发表时间：
2022
期刊：
影响因子：
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通讯作者：
Albanna,MohammadZ
中科院分区：
文献类型：
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作者：
Baltazar,Tânia;Kajave,NilabhS;Rodriguez,Marco;Chakraborty,Srija;Jiang,Bo;Skardal,Aleksander;Kishore,Vipuil;Pober,JordanS;Albanna,MohammadZ
由于容易获得，I型胶原蛋白的异种来源仍然是再生医学应用的常见选择。人类和动物来源有一些相似之处，但氨基酸组成的微小变化会影响胶原蛋白的物理性质，细胞反应和组织重塑。这项工作的目的是比较基于人I型胶原蛋白的水凝胶与基于动物源I型胶原蛋白的水凝胶（由市售产品生成）的理化性质以及组织工程和再生医学应用。具体而言，我们评估了天然人皮肤I型胶原蛋白是否可用于该蛋白质的三种最常见的研究应用：作为常规2D细胞培养物的附着和增殖的基质;作为3D细胞培养物的基质来源;以及作为组织工程的基质来源。结果表明，胶原来源的物种和组织特异性变化显著影响胶原水凝胶的物理、化学和生物学性质，包括凝胶化动力学、溶胀比、胶原纤维形态、压缩模量、稳定性和hMSCs的代谢活性。与鼠尾胶原相比，用人皮肤胶原配制的肿瘤构建体显示出对化疗剂的不同反应。人皮肤胶原蛋白对大鼠尾胶原蛋白进行修饰，并使灌注的人血管在体内组装成为可能。尽管胶原蛋白的制造方法和供应形式存在差异，但结果表明，商业上可获得的人胶原蛋白可以代替异种来源来创建功能性支架，但并非所有来源的人胶原蛋白的行为都相似。在开发用于药物筛选和再生医学应用的3D组织时必须考虑这些因素。
Xenogeneic sources of collagen type I remain a common choice for regenerative medicine applications due to ease of availability. Human and animal sources have some similarities, but small variations in amino acid composition can influence the physical properties of collagen, cellular response, and tissue remodeling. The goal of this work is to compare human collagen type I‐based hydrogels versus animal‐derived collagen type I‐based hydrogels, generated from commercially available products, for their physico‐chemical properties and for tissue engineering and regenerative medicine applications. Specifically, we evaluated whether the native human skin type I collagen could be used in the three most common research applications of this protein: as a substrate for attachment and proliferation of conventional 2D cell culture; as a source of matrix for a 3D cell culture; and as a source of matrix for tissue engineering. Results showed that species and tissue specific variations of collagen sources significantly impact the physical, chemical, and biological properties of collagen hydrogels including gelation kinetics, swelling ratio, collagen fiber morphology, compressive modulus, stability, and metabolic activity of hMSCs. Tumor constructs formulated with human skin collagen showed a differential response to chemotherapy agents compared to rat tail collagen. Human skin collagen performed comparably to rat tail collagen and enabled assembly of perfused human vessels in vivo. Despite differences in collagen manufacturing methods and supplied forms, the results suggest that commercially available human collagen can be usedin lieu ofxenogeneic sources to create functional scaffolds, but not all sources of human collagen behave similarly. These factors must be considered in the development of 3D tissues for drug screening and regenerative medicine applications.