The recombinant catalytic domain of mouse collagenase-3 depolymerizes type I collagen by cleaving its aminotelopeptides

Lemaitre, Vincent;Jungbluth, Anne;Eeckhout, Yves
(1997) Biochemical and Biophysical Research Communications — Vol. 230, n° 1, p. 202-205 (1997)

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Abstract
The sequence coding for the catalytic domain of mouse collagenase-3 (MMP-13) was amplified by polymerase chain reaction and expressed in Escherichia coli. The recombinant catalytic domain (CCD), mainly recovered as inclusion bodies, was renatured and purified to homogeneity by preparative SDS-PAGE. The purified CCD degraded gelatin, casein and a synthetic peptide. CCD was not able to cleave the triple-helical domain of type I collagen but conserved the specific property of full-length collagenase-3 to cleave the N-telopeptides. These results show that residues involved in the recognition and cleavage of the aminotelopeptides of type I collagen are located in the catalytic domain of mouse collagenase-3 and that the C-terminal domain is not required for this activity.
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Lemaitre, V., Jungbluth, A., & Eeckhout, Y. (1997). The recombinant catalytic domain of mouse collagenase-3 depolymerizes type I collagen by cleaving its aminotelopeptides. Biochemical and Biophysical Research Communications, 230(1), 202-205. https://doi.org/10.1006/bbrc.1996.5924 (Original work published 1997)