PMID- 10634581
OWN - NLM
STAT- MEDLINE
DCOM- 20000201
LR  - 20191103
IS  - 1045-4411 (Print)
IS  - 1045-4411 (Linking)
VI  - 10
IP  - 4
DP  - 1999
TI  - Proteinases in developing dental enamel.
PG  - 425-41
AB  - For almost three decades, proteinases have been known to reside within developing
      dental enamel. However, identification and characterization of these proteinases 
      have been slow and difficult, because they are present in very small quantities
      and they are difficult to purify directly from the mineralizing enamel. Enamel
      matrix proteins such as amelogenin, ameloblastin, and enamelin are cleaved by
      proteinases soon after they are secreted, and their cleavage products accumulate 
      in the deeper, more mature enamel layers, while the full-length proteins are
      observed only at the surface. These results suggest that proteinases are
      necessary for "activating" enamel proteins so the parent proteins and their
      cleavage products may perform different functions. A novel matrix
      metalloproteinase named enamelysin (MMP-20) was recently cloned from tooth
      tissues and was later shown to localize primarily within the most recently formed
      enamel. Furthermore, recombinant porcine enamelysin was demonstrated to cleave
      recombinant porcine amelogenin at virtually all of the sites that have previously
      been described in vivo. Therefore, enamelysin is at least one enzyme that may be 
      important during early enamel development. As enamel development progresses to
      the later stages, a profound decrease in the enamel protein content is observed. 
      Proteinases have traditionally been assumed to degrade the organic matrix prior
      to its removal from the enamel. Recently, a novel serine proteinase named enamel 
      matrix serine proteinase-1 (EMSP1) was cloned from enamel organ epithelia. EMSP1 
      localizes primarily to the early maturation stage enamel and may, therefore, be
      involved in the degradation of proteins prior to their removal from the maturing 
      enamel. Other, as yet unidentified, proteinases and proteinase inhibitors are
      almost certainly present within the forming enamel and await discovery.
FAU - Bartlett, J D
AU  - Bartlett JD
AD  - Department of Biomineralization, Forsyth Institute, Boston, Massachusetts 02115, 
      USA.
FAU - Simmer, J P
AU  - Simmer JP
LA  - eng
GR  - DE 12098/DE/NIDCR NIH HHS/United States
GR  - DE-10721/DE/NIDCR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PT  - Review
PL  - United States
TA  - Crit Rev Oral Biol Med
JT  - Critical reviews in oral biology and medicine : an official publication of the
      American Association of Oral Biologists
JID - 9009999
RN  - 0 (AMBN protein, human)
RN  - 0 (Amelogenin)
RN  - 0 (Dental Enamel Proteins)
RN  - 0 (ameloblastin protein, Sus scrofa)
RN  - 0 (tuftelin)
RN  - EC 3.4.- (Endopeptidases)
RN  - EC 3.4.21.- (Kallikreins)
RN  - EC 3.4.21.- (Serine Endopeptidases)
RN  - EC 3.4.21.- (kallikrein 4)
RN  - EC 3.4.24.- (MMP20 protein, human)
RN  - EC 3.4.24.- (Matrix Metalloproteinase 20)
RN  - EC 3.4.24.- (Matrix Metalloproteinases)
SB  - D
SB  - IM
MH  - Amelogenesis/*physiology
MH  - Amelogenin
MH  - Animals
MH  - Dental Enamel/*enzymology
MH  - Dental Enamel Proteins/isolation & purification/metabolism
MH  - Enamel Organ/enzymology
MH  - Endopeptidases/analysis/*isolation & purification
MH  - Humans
MH  - *Kallikreins
MH  - Matrix Metalloproteinase 20
MH  - Matrix Metalloproteinases/isolation & purification/metabolism
MH  - Serine Endopeptidases/isolation & purification/metabolism
MH  - Swine
MH  - Tooth Germ/metabolism
RF  - 110
EDAT- 2000/01/14 00:00
MHDA- 2000/01/14 00:01
CRDT- 2000/01/14 00:00
PHST- 2000/01/14 00:00 [pubmed]
PHST- 2000/01/14 00:01 [medline]
PHST- 2000/01/14 00:00 [entrez]
AID - 10.1177/10454411990100040101 [doi]
PST - ppublish
SO  - Crit Rev Oral Biol Med. 1999;10(4):425-41. doi: 10.1177/10454411990100040101.