Immunoblot detection and expression of enamel proteins at the apical portion of the forming root in porcine permanent incisor tooth germs

2001 ◽  
Vol 19 (4) ◽  
pp. 236-243 ◽  
Author(s):  
Makoto Fukae ◽  
Takako Tanabe ◽  
Yasuo Yamakoshi ◽  
Marie Yamada ◽  
Yuko Ujiie ◽  
...  
1975 ◽  
Vol 54 (3_suppl) ◽  
pp. 72-77 ◽  
Author(s):  
Steven E. Schonfeld

Young adult rabbits were immunized with enamel matrix proteins from embryonic tooth organs of the same strain of rabbit. These proteins elicited an alloimmune response as demonstrated by the specific binding of antiserum to enamel matrix which was visualized by indirect immunofluorescent microscopy. The labial and lingual surfaces of embryonic incisor tooth organs were found to share common antigenic determinants. The observations suggest that enamel proteins could possibly be autoantigens.


1987 ◽  
Vol 1 (2) ◽  
pp. 289-292 ◽  
Author(s):  
M.F. Young ◽  
H.S. Shimokawa ◽  
M.E. Sobel ◽  
J.D. Termine

In order to study the nature of amelogenin mRNA, we isolated ameloblast-rich tissue from the unerupted permanent incisor tooth germs of 18-month-old steers and subjected it to guanidine HC1 solubilization for extraction of mRNA. When poly A+ ameloblast RNA was incubated with radioactive deoxynucleotides and reverse transcriptase, four major transcripts were detected with sizes of 1.9, 1.4, 0.7, and 0.4 kb in length. One of the transcripts (0.7 kb) corresponded precisely in length to that predicted from the size of the major in vitro translated amelogenin proteins (27,000 daltons). To determine whether the transcripts did indeed encode amelogenin mRNA, we constructed a λgt11 cDNA library and isolated several amelogenin cDNA's by screening with amelogenin antibody. Four clones were amplified and insert sizes determined by acrylamide gel electrophoresis. Two of the clones had insert sizes of ~ 0.7 kb (λAm 16, XAm 7), and two had insert sizes of ~ 0.4 kb (λAm 11, λAm 4). When the amelogenin cDNA was radiolabeled and used for northern analysis, two species of amelogenin message (0.75 and 0.45 kb) were evident, both of which showed extensive hybridization to λAm 16 (large) and λAm 11 (small) cDNA. These data indicate that: (1) Amelogenin mRNA is heterogeneous in the bovine tooth germ, having two major species 800 and 400 bases long; and (2) the major species of amelogenin share extensive sequence homology. Based on these data, we suggest that at least part of the heterogeneity of amelogenin matrix protein may arise from the production of heterogeneous amelogenin mRNA's that share some common nucleotide sequences.


1996 ◽  
Vol 70 (7) ◽  
pp. 420-429 ◽  
Author(s):  
S. Matsuo ◽  
Tetsuichiro Inai ◽  
Kojiro Kurisu ◽  
Ken-ichi Kiyomiya ◽  
Masaru Kurebe

2002 ◽  
Vol 50 (9) ◽  
pp. 1229-1236 ◽  
Author(s):  
Otto Baba ◽  
Nobuyuki Takahashi ◽  
Tatsuo Terashima ◽  
Wu Li ◽  
Pamela K. DenBesten ◽  
...  

In addition to seven known exons of the amelogenin gene, recent studies have identified two exons downstream of amelogenin exon 7 in genomic DNA of mouse and rat. Here the spatial and temporal expression of mRNAs and of the translated proteins derived from alternative splicing of the amelogenin gene ending with exon 8 and exon 9 were examined by in situ hybridization (ISH) and immunohistochemistry (IHC). RNA signals for exons 8 and 9 were expressed in the ameloblast layer extending from early presecretory to postsecretory transitional stages of amelogenesis. IHC of amelogenin proteins that include sequences encoded by these exons demonstrated identical localization of these proteins in the ameloblast layer corresponding to RNA signals identified by ISH. There was intense immunostaining of the enamel matrix secreted by these cells. Western blotting analysis of rat enamel proteins revealed three distinct protein bands with sequences encoded by the new exons. These data confirmed the existence of the transcripts of alternatively spliced mRNAs coding for exons 8 and 9 of the amelogenin gene in rat tooth germs and suggest that the translated proteins contribute to the heterogeneity of amelogenins and have some significant roles in enamel formation and mineralization.


1979 ◽  
Vol 58 (2_suppl) ◽  
pp. 1012-1013 ◽  
Author(s):  
D. Moe ◽  
H. Birkedal-Hansen

Partially mineralized enamel matrix removed from bovine incisor tooth germs contains proteolytic activity capable of completely degrading enamel matrix proteins at neutral and slightly alkaline pH. The protease activity also degrades common protease substrates such as casein and azocoll with optimal activity at pH 8-9. Inhibitor studies revealed that the enzyme involved is a serine protease of the chymotrypsin family.


2007 ◽  
Vol 27 (2) ◽  
pp. 53-58 ◽  
Author(s):  
Yoshihiro Miura ◽  
Hiroki S. Ozaki ◽  
Tie-Jun Li ◽  
Masanori Uemura ◽  
Motoo Kitano

Sign in / Sign up

Export Citation Format

Share Document