ライフサイエンスコーパス: MMP-20

1 oral epithelial dysplasia were positive for MMP-20.

2 encoded amelogenin isoforms are processed by MMP-20.

3 amples treated with CS-AMEL hydrogel without MMP-20.

4 d in teeth, our data suggest that control of MMP-20 activity is primarily regulated by transcriptiona

5 This suggests that MMP-20 acts either directly or indirectly to facilitate

6 asked if a lack of proteolytic processing by MMP-20 affects amelogenin signaling and consequently alt

7 We propose that Mmp-20 alone processes amelogenin during the secretory s

8 MMP-20 also cleaves DSP at multiple sites, releasing N-t

9 le immunofluorescence showed coexpression of MMP-20 and DSPP.

10 Six fluorescent peptides were digested with MMP-20 and Klk4 and analyzed by RP-HPLC and by mass spec

11 Mmp-20 and Klk4 are the two key enamel proteases.

12 We isolated Mmp-20 and Klk4 from developing pig teeth and used them

13 ration, stepwise processing of amelogenin by MMP-20 and then KLK4 reduces amelogenin-apatite interact

14 amel proteases, matrix metalloproteinase-20 (MMP-20) and kallikrein 4 (KLK4), are known to cleave ame

15 latin and casein zymograms identified MMP-2, MMP-20, and KLK4 in the dentin extracts.

16 ng other MMP-20-SIBLING pairings, identifies MMP-20 as DSPP cognate MMP.

17 tide library screen with Edman sequencing of MMP-20 cleavage products revealed that, among MMPs previ

18 MMP-20 cleaved each peptide exactly at the sites corresp

19 Mmp-20 cleaves amelogenin sequences after Pro(162), Ser(

20 MMP-20 cleaves DSP-DGP to generate DSP and DGP.

21 Mmp-20 cleaves LRAP after Pro(45) and Pro(40), producing

22 ly grown crystals in the sample treated with MMP-20-CS-AMEL hydrogel showed more uniform orientation

23 sed (1.8- and 2.4-fold, respectively) by the MMP-20-CS-AMEL hydrogel.

24 MMP-20-DSPP specific interaction, excluding other MMP-20

25 We tested the hypothesis that MMP-20 (enamelysin) catalyzes the cleavages that generat

26 Matrix metalloproteinase-20 (MMP-20, enamelysin) has a highly restricted pattern of e

27 el development, matrix metalloproteinase-20 (MMP-20, enamelysin) is expressed early during the secret

28 Our goal was to investigate MMP-20 expression and to explore preliminary evidence of

29 We asked if the highly restricted MMP-20 expression pattern was associated with a broad su

30 This shows that MMP-20 generates the 23-kDa AMBN starting at Tyr(223), a

31 vealed that, among MMPs previously screened, MMP-20 had unique substrate preferences.

32 These preferences indicate that MMP-20 has a deep and wide catalytic pocket that can acc

33 Our data provide evidence that MMP-20 has a wider tissue distribution than previously a

34 distributed collagen, and since only active MMP-20 has been observed in teeth, our data suggest that

35 man OSCC tissues showed immunoreactivity for MMP-20 in 18 (86%) and coexpression with DSPP in all 15

36 Stepwise processing of amelogenin by MMP-20 in the CS-AMEL hydrogel prevented undesirable pro

37 nd that amelogenin was gradually degraded by MMP-20 in the presence of chitosan.

38 al role of the metalloproteinase enamelysin (MMP-20) in controlling some of the most critical stages

39 lore the mechanisms and significance of DSPP-MMP-20 interaction in oral carcinogenesis.

40 s occurred in the nearly mature enamel, when MMP-20 is normally no longer expressed.

41 In healthy tissues, MMP-20 is observed in the enamel organ and pulp organ of

42 We conclude that MMP-20 is the enzyme that processes ameloblastin during

43 We tested the hypothesis that MMP-20 is the protease that cleaves AMBN.

44 Enamelysin (MMP-20) is a tooth-specific matrix metalloproteinase tha

45 n (AMTN), tumor-related proteins enamelysin (MMP-20), kallikrein-4 (KLK-4), and odontogenic ameloblas

46 iggest difference in mineral content between MMP-20 null and controls occurred in the nearly mature e

47 roperties of the secretory-/maturation-stage MMP-20 null enamel were significantly different from tho

48 the weight percent of mature mineral in the MMP-20 null mouse enamel was only 7-16% less than that i

49 HEK293-H cells, purified, and digested with MMP-20 or Klk4 (kallikrein 4).

50 Inspired by our recent finding that MMP-20 prevents protein occlusion inside enamel crystals

51 nerated in vitro demonstrates that MMP-2 and MMP-20 process DSPP into smaller subunits in the dentin

52 We conclude that MMP-20 processes ameloblastin in vitro and in vivo.

53 undergo extensive alternative splicing, and MMP-20 processes the isoforms following their secretion.

54 rthermore, the strong DSPP enrichment at the MMP-20 promoter suggests a regulatory role in MMP-20 tra

55 tion revealed a 9-fold enrichment of DSPP at MMP-20 promoter-proximal elements.

56 is on OSCC cell lines showed upregulation of MMP-20 protein and mRNA, respectively, while immunofluor

57 The MMP-20 proteolysis of amelogenin was studied, and the mo

58 at the C- and N- termini by recombinant pig MMP-20 (rpMMP20) and recombinant human kallikrein-4 (rhK

59 0-DSPP specific interaction, excluding other MMP-20-SIBLING pairings, identifies MMP-20 as DSPP cogna

60 nd then confirmed that type V collagen is an MMP-20 substrate.

61 l crystals, we hypothesized that addition of MMP-20 to CS-AMEL hydrogel could reinforce the newly gro

62 MP-20 promoter suggests a regulatory role in MMP-20 transcription.

63 Among the non-tooth tissues assayed, MMP-20 transcripts were identified only in minute quanti

64 Recombinant human MMP-20 was added to the CS-AMEL hydrogel to cleave full-

65 namel regrowth, matrix metalloproteinase-20 (MMP-20) was introduced into the CS-AMEL hydrogel.

66 To identify other tissues that may express MMP-20, we performed a systematic mouse tissue expressio

67 MMP-2 and MMP-20 were purified from over 150 g of porcine dentin p

68 Matrix metalloproteinase 20 (MMP-20), widely regarded as tooth specific, participates

69 Colocalization and potential interaction of MMP-20 with dentin sialoprotein was confirmed by coimmun