The hind limbs of anaesthetized rats were exposed to vibration trauma (81 Hz; amplitude peak to peak 0.50 mm) for 4 hours during 2 consecutive days. The animals were examined in groups of 4 immediately after the last exposure, and after 1, 2, 3, 5, 7, 10, 14 and 28 days. The Achilles tendons and the tendons of the anterior tibialis muscles were sampled and processed to demonstrate IGF-I immunoreactivity. In the normal Achilles tendon and in the tendon of the anterior tibial muscle, slight IGF-I immunoreactivity was seen in many of the long slender fibroblasts between the collagen bundles. A strong increase in the IGF-I immunoreactivity appeared in the anterior tibialis muscle tendon 3 days after the last vibration exposure. In addition, the tendon fibroblasts became hypertrophic. A similar but less striking increase in IGF-I immunoreactivity appeared in the Achilles tendon. The peak intensity and frequency of stained cells were achieved after 7 days for both tendons. The intensity then levelled off, and was normalized after 28 days. It is concluded that acute exposure to vibrations induces reactive changes in fibroblasts in tendons, which may reflect a change to a more active synthesising state, as a response to the vibration trauma. The transiently altered expression of IGF-I immunoreactivity forms a link in a chain of events regulating the functional activity level of fibroblasts in response to a trauma.
The gene for Staphylococcal protein A was fused to the coding sequence of bacterial beta‐galactosidase, alkaline phosphatase and human insulin‐like growth factor I (IGF‐I). The fusion proteins, expressed in bacteria, were purified by affinity chromatography on IgG‐Sepharose and antibodies were raised in rabbits. All three fusion proteins elicited specific antibodies against both the inserted protein sequences and the protein A moiety. In the case of IGF‐I, the protein A moiety in the fusion protein may act as an adjuvant since native IGF‐I alone is a poor immunogen. The results suggest that the protein A fusion system can be used for efficient antibody production against peptides or proteins expressed from cloned or synthetic genes. To facilitate such gene fusions a set of optimized vectors have been constructed.
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