Sandbox Reserved 468: Difference between revisions
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In MMPs, the catalytic domain is followed by a domain consisting of 15–65 amino acid residues referred to as the <scene name='Sandbox_Reserved_468/Linker_region/3'>Linker Region</scene> or the hinge region. The length of this region varies between MMPs and does not have a well-determined structure. In MMP-1, the linker region is 16 residues long (242-258). This region is typically rich in proline residues. Interestingly, the replacement of those with alanine | In MMPs, the catalytic domain is followed by a domain consisting of 15–65 amino acid residues referred to as the <scene name='Sandbox_Reserved_468/Linker_region/3'>Linker Region</scene> or the hinge region. The length of this region varies between MMPs and does not have a well-determined structure. In MMP-1, the linker region is 16 residues long (242-258). This region is typically rich in proline residues. Interestingly, research suggests that the replacement of those proline residues with alanine substantially reduced the collagenolytic activity of some MMPs. This could indicate that there must be a correct linker structure in order for collagenolysis to occur properly <ref name="cope">http://www.copewithcytokines.de/cope.cgi?key=MMP-1</ref>. | ||
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MMP-1 gene expression has also been shown to have implications with cancer treatment. MMP-1 can be used as a candidate marker that may be useful for identification of breast lesions that can develop into cancer. As such, the medical implications of MMP-1 go beyond just what happens if the enzyme functions improperly but the enzyme, well rather the gene that encodes the enzyme, can also aid the diagnosis and subsequent treatment of breast cancer <ref name="nagase">Nagase, H. (2006). Structure and function of matrix metalloproteinases and timps. Cardiovascular Research, 69(3), 562-573. Retrieved from http://cardiovascres.oxfordjournals.org/content/69/3/562.full</ref>. | MMP-1 gene expression has also been shown to have implications with cancer treatment. MMP-1 can be used as a candidate marker that may be useful for identification of breast lesions that can develop into cancer. As such, the medical implications of MMP-1 go beyond just what happens if the enzyme functions improperly but the enzyme, well rather the gene that encodes the enzyme, can also aid the diagnosis and subsequent treatment of breast cancer <ref name="nagase">Nagase, H. (2006). Structure and function of matrix metalloproteinases and timps. Cardiovascular Research, 69(3), 562-573. Retrieved from http://cardiovascres.oxfordjournals.org/content/69/3/562.full</ref>. | ||
