PMID- 10077646
OWN - NLM
STAT- MEDLINE
DCOM- 19990520
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 6
DP  - 1999 Mar 16
TI  - Molecular cloning and characterization of prostase, an androgen-regulated serine 
      protease with prostate-restricted expression.
PG  - 3114-9
AB  - The identification of genes with selective expression in specific organs or cell 
      types provides an entry point for understanding biological processes that occur
      uniquely within a particular tissue. Using a subtraction approach designed to
      identify genes preferentially expressed in specific tissues, we have identified
      prostase, a human serine protease with prostate-restricted expression. The
      prostase cDNA encodes a putative 254-aa polypeptide with a conserved serine
      protease catalytic triad and an amino-terminal pre-propeptide sequence,
      indicating a potential secretory function. The genomic sequence comprises five
      exons and four introns and contains multiple copies of a chromosome 19q-specific 
      minisatellite repeat. Northern analysis indicates that prostase mRNA is expressed
      in hormonally responsive normal and neoplastic prostate epithelial tissues, but
      not in prostate stromal constituents. Prostase shares 35% amino acid identity
      with prostate-specific antigen (PSA) and 78% identity with the porcine enamel
      matrix serine proteinase 1, an enzyme involved in enamel matrix degradation and
      with a putative role in the disruption of intercellular junctions.
      Radiation-hybrid-panel mapping localized prostase to chromosome 19q13, a region
      containing several other serine proteases, including protease M, pancreatic/renal
      kallikrein hK1, and the prostate-specific kallikreins hK2 and hK3 (PSA). The
      sequence homology between prostase and other well-characterized serine proteases 
      suggests several potential functional roles for the prostase protein that include
      the degradation of extracellular matrix and the activation of PSA and other
      proteases.
FAU - Nelson, P S
AU  - Nelson PS
AD  - Department of Molecular Biotechnology, University of Washington, Seattle, WA
      98195, USA. psnels@u.washington.edu
FAU - Gan, L
AU  - Gan L
FAU - Ferguson, C
AU  - Ferguson C
FAU - Moss, P
AU  - Moss P
FAU - Gelinas, R
AU  - Gelinas R
FAU - Hood, L
AU  - Hood L
FAU - Wang, K
AU  - Wang K
LA  - eng
SI  - GENBANK/AF113140
SI  - GENBANK/AF113141
GR  - K08 CA75173-01A1/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Androgens)
RN  - EC 3.4.21.- (Serine Endopeptidases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Androgens/metabolism
MH  - Base Sequence
MH  - Cloning, Molecular
MH  - *Gene Expression Regulation, Enzymologic
MH  - Humans
MH  - Male
MH  - Molecular Sequence Data
MH  - Organ Specificity
MH  - Prostate/*enzymology
MH  - Sequence Alignment
MH  - Sequence Analysis, DNA
MH  - Serine Endopeptidases/*genetics/metabolism
PMC - PMC15904
EDAT- 1999/03/17 00:00
MHDA- 1999/03/17 00:01
CRDT- 1999/03/17 00:00
PHST- 1999/03/17 00:00 [pubmed]
PHST- 1999/03/17 00:01 [medline]
PHST- 1999/03/17 00:00 [entrez]
AID - 10.1073/pnas.96.6.3114 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):3114-9. doi: 10.1073/pnas.96.6.3114.