Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides.
The matrix metalloproteinase (MMP)/matrixin family has been implicated in both normal tissue remodeling and a variety of diseases associated with abnormal turnover of extracellular matrix components. To better understand MMP behaviors and to aid in the design of MMP inhibitors, a variety of sequence specificity studies have been performed using collagen sequence-based peptides and MMP family members. Results of these studies have been valuable for defining the differences in MMPs and for creating fluorogenic substrates that can continuously monitor MMP activity. However, these studies have also demonstrated that these peptides may not be very good models of native MMP substrates, and that the additivity principle is not always applicable for designing synthetic MMP substrates.
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Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City 66103, USA.
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D000595:Amino Acid Sequence; D003094:Collagen / Q000737:chemistry*; D005109:Extracellular Matrix / Q000201:enzymology*; D006801:Humans; D008666:Metalloendopeptidases / Q000378:metabolism*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D013379:Substrate Specificity
D010455:Peptides; D003094:Collagen; D008666:Metalloendopeptidases