Volume 27 Issue 1
Jan.  2006
Turn off MathJax
Article Contents

ZHANG Yun*. Amphibian Skin Secretions and Bio-adaptive Significance —Implications from Bombina maxima Skin Secretion Proteome. Zoological Research, 2006, 27(1): 101-112.
Citation: ZHANG Yun*. Amphibian Skin Secretions and Bio-adaptive Significance —Implications from Bombina maxima Skin Secretion Proteome. Zoological Research, 2006, 27(1): 101-112.

Amphibian Skin Secretions and Bio-adaptive Significance —Implications from Bombina maxima Skin Secretion Proteome

  • Received Date: 2005-09-16
  • Rev Recd Date: 1900-01-01
  • Publish Date: 2006-02-22
  • The studies on Bombina maxima revealed the rich molecular and functional diversity of amphibian skin secretion proteins and peptides. Discovered peptides from B. maxima skin secretions are three classes of antimicrobial peptides, bradykinin analogs and its gene associated peptides with diverse biological functions, proline-rich bombesin and its gene associated peptides, neuromedin U analog, Bv8 peptides, trefoil factors and protease inhibitors. The molecular and functional diversity, gene formation mechanisms and expression patterns of the peptides in B. maxima skin well reflect the molecular basis of bio-adaptation of the frog in certain living environments. In addition, B. maxima albumin with a heme b cofactor is widely distributed around the membranes of epithelial layer cells and within the stratum spongiosum of dermis in the skin, indicating its important roles in skin physiological functions, like water economy, metabolite exchange and osmoregulation, etc. The extraordinary complexity of peptides found in amphibian skin, coupled with the high probability of their novel molecular structures and possible counterparts in mammals, make amphibians an important target group in biomedical research and new drug development. Meanwhile, amphibian skin functional genome should be a nice model to study molecular biology of bio-adaptation, new gene formation and evolution.
  • 加载中
  • 加载中
通讯作者: 陈斌, bchen63@163.com
  • 1. 

    沈阳化工大学材料科学与工程学院 沈阳 110142

  1. 本站搜索
  2. 百度学术搜索
  3. 万方数据库搜索
  4. CNKI搜索

Article Metrics

Article views(2448) PDF downloads(2727) Cited by()

Related
Proportional views

Amphibian Skin Secretions and Bio-adaptive Significance —Implications from Bombina maxima Skin Secretion Proteome

Abstract: The studies on Bombina maxima revealed the rich molecular and functional diversity of amphibian skin secretion proteins and peptides. Discovered peptides from B. maxima skin secretions are three classes of antimicrobial peptides, bradykinin analogs and its gene associated peptides with diverse biological functions, proline-rich bombesin and its gene associated peptides, neuromedin U analog, Bv8 peptides, trefoil factors and protease inhibitors. The molecular and functional diversity, gene formation mechanisms and expression patterns of the peptides in B. maxima skin well reflect the molecular basis of bio-adaptation of the frog in certain living environments. In addition, B. maxima albumin with a heme b cofactor is widely distributed around the membranes of epithelial layer cells and within the stratum spongiosum of dermis in the skin, indicating its important roles in skin physiological functions, like water economy, metabolite exchange and osmoregulation, etc. The extraordinary complexity of peptides found in amphibian skin, coupled with the high probability of their novel molecular structures and possible counterparts in mammals, make amphibians an important target group in biomedical research and new drug development. Meanwhile, amphibian skin functional genome should be a nice model to study molecular biology of bio-adaptation, new gene formation and evolution.

ZHANG Yun*. Amphibian Skin Secretions and Bio-adaptive Significance —Implications from Bombina maxima Skin Secretion Proteome. Zoological Research, 2006, 27(1): 101-112.
Citation: ZHANG Yun*. Amphibian Skin Secretions and Bio-adaptive Significance —Implications from Bombina maxima Skin Secretion Proteome. Zoological Research, 2006, 27(1): 101-112.

Catalog

    /

    DownLoad:  Full-Size Img  PowerPoint
    Return
    Return