LOCALIZATION OF TYPE-I AND TYPE-III COLLAGEN AND FIBRONECTIN PRODUCTION IN INJURED GASTROCNEMIUS-MUSCLE

被引:0
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作者
HURME, T
KALIMO, H
SANDBERG, M
LEHTO, M
VUORIO, E
机构
[1] UNIV TURKU,DEPT MED BIOCHEM,SF-20520 TURKU 52,FINLAND
[2] UNIV TURKU,CENT HOSP,SF-20520 TURKU 52,FINLAND
[3] UNIV CENT HOSP TAMPERE,DEPT SURG,TAMPERE,FINLAND
关键词
MUSCLE INJURY; REGENERATION; INSITU HYBRIDIZATION; NORTHERN BLOT; IMMUNOHISTOCHEMISTRY;
D O I
暂无
中图分类号
R-3 [医学研究方法]; R3 [基础医学];
学科分类号
1001 ;
摘要
The healing of muscle rupture consists of two simultaneous processes, regeneration of disrupted muscle fibers and production of connective tissue scar. These two processes are at the same time supportive to the competitive with each other. Their balanced progression is necessary for optimal healing. Synthesis of three connective tissue proteins, collagen types I and III and fibronectin, was analyzed during the regeneration process from 2 days to 3 weeks by Northern blot and in situ hybridization and immunohistochemistry. For this purpose a partial standard rupture of the gastrocnemius muscle was induced in 56 rats by a strike with a blunt spring-loaded hammer. Northern blot analysis of the specific mRNAs during the healing process revealed distinctly different expression patterns for fibronection and type I and III collagens. During the early stages (days 2 and 3) fibronectin, derived mainly from plasma, was abundant in the traumatized area, but local production of fibronectin mRNA by fibroblasts had also already started by day 2, closely followed by that of type III collagen. This early active synthesis of type III collagen and fibronectin was followed by a decrease after 1 week. The production of type I collagen mRNAs was activated somewhat later and remained elevated for at least 3 weeks. The muscle cells did not contain procollagen mRNAs. The observed sequence of connective tissue proteins reflects the particular function that each carriers out during muscle wound healing (e.g., fibronectin in fibroblast trapping, type III collagen in plasticity/flexibility, and type I collagen in tensile strength).
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页码:76 / 84
页数:9
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