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   Apatite reduces amelogenin proteolysis by MMP-20 and KLK4 in vitro  
   
نویسنده sun z. ,carpiaux w. ,fan d. ,fan y. ,lakshminarayanan r. ,moradian-oldak j.
منبع journal of dental research - 2010 - دوره : 89 - شماره : 4 - صفحه:344 -348
چکیده    Two enamel proteases,matrix metalloproteinase-20 (mmp-20) and kallikrein 4 (klk4),are known to cleave amelogenin and are necessary for proper enamel formation. however,the effect of hydroxyapatite (hap) on the proteolytic activity of these enzymes remains unclear. to investigate whether apatite affects normal amelogenin proteolysis,we used 2 different isoforms of amelogenin combined with the appropriate enzymes to analyze proteolytic processing rates in the presence or absence of synthetic hydroxyapatite (hap) crystals (n = 3). we found a distinct dose-dependent relationship between the amount of hap present in the proteolysis mixture and the rate of rp172 degradation by rpmmp-20,whereas the effect of hap on proteolysis of either rp172 or rp148 by rhklk4 was less prominent.
کلیدواژه Amelogenin; Apatite.; Enamel; KLK4; MMP-20
آدرس center for craniofacial molecular biology,university of southern california,school of dentistry,2250 alcazar st.,los angeles,ca 90033, United States, center for craniofacial molecular biology,university of southern california,school of dentistry,2250 alcazar st.,los angeles,ca 90033, United States, center for craniofacial molecular biology,university of southern california,school of dentistry,2250 alcazar st.,los angeles,ca 90033, United States, school of dentistry,louisiana state university health science center,box-137,1100 florida ave.,new orleans,la 70119, United States, singapore eye research institute,7 hospital drive block c,02-02,singapore 169611, Singapore, center for craniofacial molecular biology,university of southern california,school of dentistry,2250 alcazar st.,los angeles,ca 90033, United States
 
     
   
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