Abstract:
:Recently our laboratory has reported, in a lacerated flexor tendon model, that the "early turnover" phase of the repair process extends for a longer period of time in vivo than previously documented. The extensive turnover of the collagenous matrix was consistent with the presence of collagenolytic activity in repairing tendon tissue and suggested a possible regulatory role for neutral metalloproteinases in flexor tendon repair. However, these in vivo observations could not distinguish the relative contribution by the tendon fibroblasts from that of the surrounding sheath and vascular tissue elements. To further define these interrelationships, the present study investigates the repair process of the flexor tendon in an in vitro tissue culture environment. The sequential changes in matrix formation were defined (i.e., proteoglycans/glycosaminoglycans, glycoproteins, and collagenous proteins). The concomitant production of neutral metalloproteinases as well as prostaglandin E2 was determined in relation to net tissue repair. Profundus flexor tendon segments were obtained from young adult Macaca nemestrina monkeys and maintained in organ culture for periods from 4 days through 9 weeks. Initially (at 2 wks) there was an increase in both sulfated and nonsulfated glycosaminoglycans, which preceded the onset of maximal collagen protein formation. By 6 and 9 weeks of in vitro repair, of the lacerated tendon segments, there was a significant increase in net collagen formation. Neutral metalloproteinase activity increased early in the repair period, from the 4th to 9th day, and decreased thereafter through the 9th week of culture. Functionally the enzyme appeared to be a gelatinase. The temporal pattern of in vitro collagen synthesis in relation to the gelatinase activity support the hypothesis that regulation of this enzyme(s) may be a critical factor in mediating the flexor tendon response to injury.
journal_name
Connect Tissue Resjournal_title
Connective tissue researchauthors
Russell JE,Manske PRdoi
10.3109/03008208909103903subject
Has Abstractpub_date
1989-01-01 00:00:00pages
51-64issue
1eissn
0300-8207issn
1607-8438journal_volume
23pub_type
杂志文章abstract::Bone sialoprotein is a 34 kDa phosphorylated and sulphated glycoprotein that is essentially unique to mineralizing connective tissues. Recent studies on the developmental expression of BSP mRNA and the temporo-spatial appearance of the protein during bone formation in vivo and in vitro have demonstrated that BSP is ex...
journal_title:Connective tissue research
pub_type: 杂志文章
doi:10.3109/03008209609029171
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journal_title:Connective tissue research
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更新日期:1998-01-01 00:00:00
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