中国组织工程研究

中国组织工程研究 ›› 2010, Vol. 14 ›› Issue (41): 7657-7660.doi: 10.3969/j.issn.1673-8225.2010.41.014

• 组织构建与生物活性因子 tissue construction and bioactive factors • 上一篇    下一篇

碱性成纤维细胞生长因子与瘢痕成纤维细胞Ⅰ、Ⅲ型胶原蛋白的代谢

谢举临1，卞徽宁2，李厚东1，舒  斌1，祁少海1，唐锦明1，徐盈斌1，利天增1，刘旭盛1   

  1. 1中山大学附属第一医院烧伤科，广东省广州市，510080；2广东省人民医院烧伤科，广东省广州市，510080
  • 出版日期:2010-10-08 发布日期:2010-10-08
  • 作者简介:谢举临☆，男， 1973年生， 江西省瑞金县人，汉族，博士，副教授。主要从事创面愈合和瘢痕形成方面的研究。 xiejl90@sina.com

Basic fibroblast growth factor and metabolism of I and III collagen protein in scar fibroblasts

Xie Ju-lin1, Bian Hui-ning2, Li Hou-dong1, Shu Bin1, Qi Shao-hai1, Tang Jin-ming1, Xu Ying-bin1, Li Tian-zeng1, Liu Xu-sheng1   

  1. 1 epartment of Burn, First Affiliated Hospital, Sun Yat-Sen University, Guangzhou  510080, Guangdong Province, China; 2 epartment of Burn, Guangdong People’s Hospital, Guangzhou  510080, Guangdong Province, China
  • Online:2010-10-08 Published:2010-10-08
  • About author:Xie Ju-lin☆, Doctor, Associate professor, Department of Burn, First Affiliated Hospital, Sun Yat-Sen University, Guangzhou 510080, Guangdong Province, China xiejl90@sina.com

PDF

342

被引次数

16

摘要：

背景：研究证实碱性成纤维细胞生长因子有促进创面愈合的作用，然而其在促进创面愈合的同时是否会引起成纤维细胞的增殖而导致瘢痕增生已受到学者的广泛关注。
目的：探讨碱性成纤维细胞生长因子对瘢痕成纤维细胞Ⅰ、Ⅲ型胶原蛋白合成和降解的调控作用。
方法：增生性瘢痕组织取自中山大学附属第一医院烧伤科行瘢痕整复术的患者，组织块法培养瘢痕成纤维细胞。取第2代细胞，采用氯胺T法、RT-PCR和Western blot法检测不同浓度(0~500 µg/L)碱性成纤维细胞生长因子对瘢痕来源的成纤维细胞Ⅰ、Ⅲ型胶原蛋白及细胞基质金属蛋白酶1合成和分泌的影响。
结果与结论：碱性成纤维细胞生长因子对瘢痕成纤维细胞羟脯氨酸及Ⅰ、Ⅲ型胶原蛋白mRNA的表达均无促进作用。低质量浓度碱性成纤维细胞生长因子对细胞基质金属蛋白酶1的表达无明显影响，但随着质量浓度的升高表现为增高趋势，以50，100，500 µg/L组增高最显著(P < 0.05或P < 0.01)。同时，细胞基质金属蛋白酶1的表达在细胞与上清中变化一致。说明高质量浓度碱性成纤维细胞生长因子可以通过增加细胞基质金属蛋白酶1的合成来促进胶原蛋白降解，从而避免细胞外基质的过度沉积。

关键词: 碱性成纤维细胞生长因子, 成纤维细胞, 细胞基质金属蛋白酶1, 瘢痕, 胶原蛋白

Abstract:

BACKGROUND: Studies have confirmed that basic fibroblast growth factor (bFGF) can promote wound surface healing. Scholars have paid great attention on whether bFGF can induce fibroblastic proliferation and lead to scar hyperplasia during wound surface healing.
OBJECTIVE: To investigate the regulatory effects of bFGF on the synthesis and degradation of fibroblast I and III collagen protein.
METHODS: Hyperplastic scar tissue was obtained from patients undergoing scar plasty at the Department of Burn, First Affiliated Hospital, Sun Yat-Sen University. Fibroblasts of scar tissue were cultured by tissue block method. The second passage of cells was collected. Effects of bFGF (0-500 µg/L) on synthesis and secretion of I and III collagen protein and cell matrix metalloproteinase 1 in scar-derived fibroblasts were measured by chloramines T, RT-PCR and Western blot assay.
RESULTS AND CONCLUSION: bFGF stimulation had no effect on hydroxyproline, I and III collagen protein mRNA expression. Low mass concentration of bFGF did not affect cell matrix metalloproteinase 1 expression, but cell matrix metalloproteinase 1 expression was increased with increased mass concentration of bFGF, especially 50, 100, 500 µg/L groups (P < 0.05 or P < 0.01). Simultaneously, changes in cell matrix metalloproteinase 1 expression were identical in cells and supernatant. Results have suggested that high mass concentration of bFGF contributes to degradation of collagen protein by increasing cell matrix metalloproteinase 1 synthesis, resulting in avoiding excessive deposition of extracellular matrix.

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