TAILIEUCHUNG - Báo cáo khoa học: Activity of matrix metalloproteinase-9 against native collagen types I and III

Interstitial collagen types I, II and III are highly resistant to proteolytic attack, due to their triple helical structure, but can be cleaved by matrix metalloproteinase (MMP) collagenases at a specific site, approximately three-quarters of the length from the N-terminus of each chain. | ễFEBS Journal Activity of matrix metalloproteinase-9 against native collagen types I and III Heather F. Bigg1 Andrew D. Rowan1 Michael D. Barker2 and Tim E. Cawston1 1 MusculoskeletalResearch Group Institute of Cellular Medicine The Medical School Newcastle University UK 2 Division of Genomic Medicine Academic Unit of Pathology University of Sheffield Medical School UK Keywords arthritis collagen I collagen III collagenase matrix metalloproteinase-9 Correspondence T. E. Cawston Musculoskeletal Research Group 4th Floor Catherine Cookson Building The Medical School Framlington Place Newcastle University Newcastle-upon-Tyne NE2 4HH UK Fax 44 191 2225455 Tel 44 191 2225397 E-mail Website http medi research rheumatology Received 3 November 2006 revised 20 December 2006 accepted 22 December 2006 doi Interstitial collagen types I II and III are highly resistant to proteolytic attack due to their triple helical structure but can be cleaved by matrix metalloproteinase MMP collagenases at a specific site approximately three-quarters of the length from the N-terminus of each chain. MMP-2 and -9 are closely related at the structural level but MMP-2 and not MMP-9 has been previously described as a collagenase. This report investigates the ability of purified recombinant human MMP-9 produced in insect cells to degrade native collagen types I and III. Purified MMP-9 was able to cleave the soluble monomeric forms of native collagen types I and III at 37 C and 25 C respectively. Activity against collagens I and III was abolished by metalloproteinase inhibitors and was not present in the concentrated crude medium of mock-transfected cells demonstrating that it was MMP-9-derived. Mutated collagenase-resistant type I collagen was not digested by MMP-9 indicating that the three-quarters one-quarter locus was the site of initial attack. Digestion of type III collagen generated a three-quarter fragment as shown by .

• Báo cáo khoa học
• Report medicine
• traditional medicine
• scientific reports
• biochemical studies
• environmental medicine
• Crystal structure
• medical knowledge
• medical research
• analysis of cytoplasmic
• oxidation
• bacteria
• hemoglobin
• medicine
• cell proliferation
• breast cancer
• chemical reaction
• gastric cancer
• hormone medicine
• tumor cells