Use this URL to cite or link to this record in EThOS:
Title: Inhibition of collagenase by the angiotensin-converting enzyme inhibitors captopril & enalapril
Author: Beaton, Nigel Alexander
Awarding Body: The University of Strathclyde
Current Institution: University of Strathclyde
Date of Award: 2009
Availability of Full Text:
Access from EThOS:
Collagen scaffolds provide a biocompatible matrix within tissue engineering and have already found many clinical uses. Two key requirements are that they are biologically Stable and mechanically strong. However, once seeded with cells or implanted in vivo collagen scaffolds are constantly being degraded and rebuilt. The balance of these two processes determines the matrix integrity. Studies have found that excessive degradation leads to mechanically weak matrices. The collagenases, members of the matrix metalloproteinase (MMP) family, play a vital role in matrix degradation. Collagenase inhibition should allow collagen scaffolds to retain their desirable qualities of mechanical strength and biological compatibility. Previous research has discovered that angiotensin converting enzyme (ACE) inhibitors, common hypertension drugs, inhibit MMP activity, MMP-9 specifically. The collagenases (MMP-1, MMP-8 and MMP-13) are members of the same family and are structurally similar to MMP-9 so these drugs may also inhibit collagenases.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available