生物学杂志

生物学杂志 ›› 2025, Vol. 42 ›› Issue (2): 84-.doi: 10.3969/j.issn.2095-1736.2025.02.084

• 研究报告 • 上一篇    下一篇

非洲爪蟾变态发育中尾部胶原的降解过程

鲁　慧1,2， 张　扬2， 高建萍2， 邢芳毓2， 张天阳2， 罗　希2， 张贵锋2   

  1. 1. 中国科学院大学 化学工程学院， 北京 100049；
    2. 中国科学院过程工程研究所生化工程国家重点实验室， 北京 100190
  • 出版日期:2025-04-18 发布日期:2025-04-14
  • 通讯作者: 张贵锋，博士生导师，研究员，研究方向为蛋白质分析检验，E-mail:gfzhang@ipe.ac.cn
  • 基金资助:
    国家重点研发计划项目（2021YFC2400804）； 北京市自然科学基金项目（L234071，2244105）

Collagen degradation in the tail of Xenopus laevis during metamorphosis

LU Hui1,2, ZHANG Yang2, GAO Jianping2, XING Fangyu2, ZHANG Tianyang2,LUO Xi2, ZHANG Guifeng2   

  1. 1. School of Chemical Engineering, University of Chinese Academy of Sciences, Beijing 100049, China; 2. State
    Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences,
    Beijing 100190, China
  • Online:2025-04-18 Published:2025-04-14
  • About author:鲁慧，硕士研究生，研究方向为生物与医药，E-mail:luhui21@ipe.ac.cn

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摘要： 采用生物质谱技术研究非洲爪蟾蝌蚪（Xenopus laevis）变态发育尾部退化过程中不同类型胶原的鉴别方法及其降解过程。在非洲爪蟾变态发育过程的NF 61~65期，截取尾部样品，采用高效液相色谱质谱联用技术（HPLC-MS）进行胶原类型识别，通过特征多肽进行定量分析。分析结果表明，爪蟾尾部样品酶解产物中存在Ⅰ 、Ⅱ 、Ⅲ 、Ⅳ 、Ⅴ 、Ⅵ和Ⅻ等类型的胶原。研究选取Ⅰ型胶原特征多肽GVLGPQGAR作为定量的外标，研究不同生长阶段Ⅰ型胶原的含量变化。采用同样方法分析Ⅲ、Ⅵ和Ⅻ型胶原含量的动态变化。结果表明，在NF 61~63期，伴随着尾部退化，各类型胶原降解速率较快；在NF 64~65期，尾部退化末期，各类型胶原已基本降解完全，其降解速率减慢。在此基础上研究各阶段尾部样品中金属基质蛋白酶（MMPs）的种类，初步探索尾部胶原纤维直径动态变化关系。

关键词: 非洲爪蟾, 胶原, 胶原降解, 特征多肽, HPLC-MS

Abstract: Biological mass spectrometry was employed to investigate the identification of various collagen types and their degradation processes during the tail degeneration ofXenopus laevistadpole metamorphosis development. Tail samples were collected at NF 61－65. The collagen types were identified using high-performance liquid chromatography coupled with tandem mass spectrometer (HPLC-MS), and quantitatively analyzed based on marker peptides. Mass spectrometry analysis revealed the presence of collagen types Ⅰ, Ⅱ, Ⅲ, Ⅳ, Ⅴ, Ⅵ, and Ⅻ in the enzymatic digestion products ofXenopus laevistail samples. Collagen type Ⅰ marker peptide GVLGPQGAR was chosen as an external standard for quantification to investigate changes in its content during different growth stages. Similarly, dynamic changes in collagen content for types Ⅲ, Ⅵ and Ⅻ were also analyzed using the same method. The results demonstrated that each type of collagen exhibited a faster degradation rate during NF 61－63 stage accompanied by tail degeneration; however, in NF 64－65 stage when tail atrophy and degeneration ceased, the degradation rate slowed down significantly. Furthermore, the study investigated matrix metallo proteinase (MMPs) types present in tail samples at different stages, and preliminarily explored the relationship between dynamic changes in diameter of tail collagen fibers.

Key words: Xenopus laevis, collagen, collagen degradation, marker peptides, HPLC-MS

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