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Matrixmetalloprotease‐2 cleaves metallothionein in vitro
Author(s) -
Koksoy Ayse Aslihan,
Turan Belma
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a279-a
Subject(s) - metallothionein , cleavage (geology) , matrix metalloproteinase , amino acid , chemistry , in vitro , metalloproteinase , biochemistry , extracellular , incubation , intracellular , microbiology and biotechnology , biology , gene , paleontology , fracture (geology)
Diabetes is reportedly associated with decreased metallothionein (MT) levels and increased matrix metalloprotease activities of MMP‐2 and MMP‐9. Previous data from our lab showed that diabetes induced a 45% reduction in cardiac MT levels (Ayaz M, Turan B. Am J Physiol Heart Circ Physiol 290: H1071‐H1080, 2006) We have hypothesized that the reduction of MT levels could be due to the cleavage of this protein by MMP‐2. When we compared the amino acid squence of MT with various MMP‐2 cleavage recognition sequences (CRS) (Turk BE, Huang LL, Piro ET, Cantley LC. Nat. Biotechnol. 19:661– 667, 2001) we obtained one site between amino acids 36 and 44. This site had 80% identity by 5 amino acids overlap to MMP‐2 CRS by using LALIGN tool. A 62% identity between coding sequences was observed by using EMBOSS tool. To assess whether MT can be a substrate for MMP‐2 in vitro, 40μg of MT was treated with active MMP‐2. Cleavage products appeared after 30 minutes of incubation and were analysed by Coomassie blue staining after 18% SDS‐PAGE. Since MMP‐2 cleavage of a variety of substrates both intracellular and extracellular, have been reported previously our data suggest that MT could be another addition to the list. This study was funded by Turkish Academy of Sciences (TUBA)‐Young Investigator Award and Ankara University Scientific Reasearch Projects Fund (AU‐BAP) .