PMID- 17890672
OWN - NLM
STAT- MEDLINE
DCOM- 20071017
LR  - 20220224
IS  - 0022-0345 (Print)
IS  - 0022-0345 (Linking)
VI  - 86
IP  - 10
DP  - 2007 Oct
TI  - Splicing determines the glycosylation state of ameloblastin.
PG  - 962-7
AB  - In developing porcine enamel, the space between enamel rods selectively binds 
      lectins and ameloblastin (Ambn) N-terminal antibodies. We tested the hypothesis 
      that ameloblastin N-terminal cleavage products are glycosylated. Assorted Ambn 
      cleavage products showed positive lectin staining by peanut agglutinin (PNA), 
      Maclura pomifera agglutinin (MPA), and Limulus polyphemus agglutinin (LPA), 
      suggesting the presence of an O-linked glycosylation containing galactose (Gal), 
      N-acetylgalactosamine (GalNAc), and sialic acid. Edman sequencing of the 
      lectin-positive bands gave the Ambn N-terminal sequence: VPAFPRQPGTXGVASLXLE. The 
      blank cycles for Pro(11) and Ser(17) confirmed that these residues are 
      hydroxylated and phosphorylated, respectively. The O-glycosylation site was 
      determined by Edman sequencing of pronase-digested Ambn, which gave HPPPLPXQPS, 
      indicating that Ser(86) is the site of the O-linked glycosylation. This 
      modification is within the 15-amino-acid segment (73-YEYSLPVHPPPLPSQ-87) deleted 
      by splicing in the mRNA encoding the 380-amino-acid Ambn isoform. We conclude 
      that only the N-terminal Ambn products derived from the 395-Ambn isoform are 
      glycosylated.
FAU - Kobayashi, K
AU  - Kobayashi K
AD  - Department of Biologic and Materials Sciences, Dental Research Lab, 1210 
      Eisenhower Place, Ann Arbor, MI 48108, USA.
FAU - Yamakoshi, Y
AU  - Yamakoshi Y
FAU - Hu, J C-C
AU  - Hu JC
FAU - Gomi, K
AU  - Gomi K
FAU - Arai, T
AU  - Arai T
FAU - Fukae, M
AU  - Fukae M
FAU - Krebsbach, P H
AU  - Krebsbach PH
FAU - Simmer, J P
AU  - Simmer JP
LA  - eng
GR  - DE12769/DE/NIDCR NIH HHS/United States
GR  - DE15846/DE/NIDCR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PL  - United States
TA  - J Dent Res
JT  - Journal of dental research
JID - 0354343
RN  - 0 (Dental Enamel Proteins)
RN  - 0 (Lectins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Protein Isoforms)
RN  - 0 (ameloblastin protein, Sus scrofa)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Blotting, Western
MH  - Dental Enamel Proteins/*genetics/*metabolism
MH  - Glycosylation
MH  - Lectins/metabolism
MH  - Peptide Fragments/metabolism
MH  - Protein Isoforms
MH  - Protein Processing, Post-Translational
MH  - RNA Splicing
MH  - Swine
EDAT- 2007/09/25 09:00
MHDA- 2007/10/18 09:00
CRDT- 2007/09/25 09:00
PHST- 2007/09/25 09:00 [pubmed]
PHST- 2007/10/18 09:00 [medline]
PHST- 2007/09/25 09:00 [entrez]
AID - 86/10/962 [pii]
AID - 10.1177/154405910708601009 [doi]
PST - ppublish
SO  - J Dent Res. 2007 Oct;86(10):962-7. doi: 10.1177/154405910708601009.