Characterization of the mouse and human PRSS17 genes, their relationship to other serine proteases, and the expression of PRSS17 in developing mouse incisors
Jcc. Hu et al., Characterization of the mouse and human PRSS17 genes, their relationship to other serine proteases, and the expression of PRSS17 in developing mouse incisors, GENE, 251(1), 2000, pp. 1-8
The human PRSS17 (serine protease 17) gene, which is located on chromosome
19q in a cluster of genes encoding serine proteases, has been variously des
ignated enamel matrix serine proteinase 1 (EMSP1), prostase, KLK4, and KLK-
L1. We have cloned and characterized the mouse and human PRSS17 genes. Both
have six exons and five introns. The mouse PRSS17 gene sequence is 10 134
bp; the human sequence is 7115 bp. Computer analysis of the mouse PRSS17 ge
ne sequence upstream of the translation initiation codon identified two pot
ential transcription initiation sites, at nucleotides 2878 and 2336. The fi
rst nucleotide of the reported mouse PRSS17 cDNA sequence corresponds to po
sition 2352 on the gene, only 16 bases downstream from one of the putative
transcription initiation sites. Repetitive DNA sequences from the MSR1 fami
ly are found in both the mouse and human PRSS17 genes. Additionally, the hu
man PRSS17 gene contains Tigger2, MER8, and Alu repetitive sequences. Phylo
genetic analyses of human and rodent proteases suggest that the PRSS17 prot
ein is not a member of the kallikrein family of serine proteases but that t
he PRSS17 gene may have originated prior to the divergence of the kallikrei
n and trypsin families of proteases. To better characterize the timing of P
RSS17 expression in developing teeth, we performed in-situ hybridization on
postnatal day 3 developing mouse mandibular incisors. PRSS17 mRNA was not
detected in secretory stage ameloblasts but could be detected in odontoblas
ts, while transition-stage and maturation-stage ameloblasts were strongly p
ositive. This pattern supports a role for the PRSS17 protein in the degrada
tion of enamel proteins. (C) 2000 Published by Elsevier Science B.V. All ri
ghts reserved.