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解锁胶原酶的潜力:结构、功能及新兴治疗前景

Unlocking the Potential of Collagenases: Structures, Functions, and Emerging Therapeutic Horizons.

作者信息

Wang Zhen-Zhen, Wang Kang, Xu Ling-Feng, Su Chang, Gong Jin-Song, Shi Jin-Song, Ma Xu-Dong, Xie Nan, Qian Jian-Ying

机构信息

School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, PR China.

Cytori Therapeutics LLC., Shanghai 201802, PR China.

出版信息

Biodes Res. 2024 Oct 8;6:0050. doi: 10.34133/bdr.0050. eCollection 2024.

Abstract

Collagenases, a class of enzymes that are specifically responsible for collagen degradation, have garnered substantial attention because of their pivotal roles in tissue repair, remodeling, and medical interventions. This comprehensive review investigates the diversity, structures, and mechanisms of collagenases and highlights their therapeutic potential. First, it provides an overview of the biochemical properties of collagen and highlights its importance in extracellular matrix function. Subsequently, it meticulously analyzes the sources of collagenases and their applications in tissue engineering and food processing. Notably, this review emphasizes the predominant role played by microbial collagenases in commercial settings while discussing their production and screening methods. Furthermore, this study elucidates the methodology employed for determining collagenase activity and underscores the importance of an accurate evaluation for both research purposes and clinical applications. Finally, this review highlights the future research prospects for collagenases, with a particular focus on promoting wound healing and treating scar tissue formation and fibrotic diseases.

摘要

胶原酶是一类专门负责胶原蛋白降解的酶,由于它们在组织修复、重塑和医学干预中发挥着关键作用,因此受到了广泛关注。这篇综述全面研究了胶原酶的多样性、结构和作用机制,并强调了它们的治疗潜力。首先,它概述了胶原蛋白的生化特性,并强调了其在细胞外基质功能中的重要性。随后,它详细分析了胶原酶的来源及其在组织工程和食品加工中的应用。值得注意的是,本综述在讨论微生物胶原酶的生产和筛选方法的同时,强调了它们在商业环境中的主要作用。此外,这项研究阐明了测定胶原酶活性所采用的方法,并强调了准确评估对于研究目的和临床应用的重要性。最后,这篇综述突出了胶原酶未来的研究前景,特别关注促进伤口愈合以及治疗瘢痕组织形成和纤维化疾病。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab8e/11458858/d484f44e5541/bdr.0050.fig.001.jpg

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