Possible actions of metalloproteinases found in porcine enamel in an early secretory stage.
In an outermost layer of porcine secretory enamel, metalloproteinases were detected by enzymography with gelatin used as a substrate. When the sample extracted from the outermost layer of the secretory enamel was incubated with calcium ions at 37 degrees C prior to electrophoresis, an increase of the 34-kDa proteinase activity and a decrease of the 76- and/or 78-kDa proteinase activities were observed. The results suggest that the metalloproteinases mediate the conversion from 76- and/or 78-kDa proteinases to the 34-kDa proteinase or the activation of a latent type of the 34-kDa proteinase, and that their activities are regulated by free Ca ions.
Tanabe
T
T
Department of Biochemistry, School of Dental Medicine, Tsurumi University, Yokohama, Japan.
Fukae
M
M
Shimizu
M
M
D000818:Animals; D002118:Calcium / Q000378:metabolism; D003743:Dental Enamel / Q000201:enzymology*; D003746:Dental Enamel Proteins / Q000737:chemistry / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D007477:Ions; D008666:Metalloendopeptidases / Q000032:analysis / Q000378:metabolism*; D008970:Molecular Weight; D012697:Serine Endopeptidases / Q000737:chemistry / Q000378:metabolism; D013552:Swine
D003746:Dental Enamel Proteins; D007477:Ions; D012697:Serine Endopeptidases; D008666:Metalloendopeptidases; D002118:Calcium