PMID- 10514489
OWN - NLM
STAT- MEDLINE
DCOM- 19991119
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 42
DP  - 1999 Oct 15
TI  - Purification, molecular cloning, and expression of a human stratum corneum
      trypsin-like serine protease with possible function in desquamation.
PG  - 30033-40
AB  - A new human 33-kDa serine protease was purified from human epidermis, and its
      cDNA was cloned from a keratinocyte library, from mRNA from a human keratinocyte 
      line (HaCat) and from mRNA from human skin. Polyclonal antibodies specific for
      the new protein detected three groups of proteins in partially purified extracts 
      of cornified eptihelium of human plantar skin. The three components are proposed 
      to correspond to proenzyme, active enzyme, and proteolytically modified active
      enzyme. After N-deglycosylation, there was a decrease in apparent molecular mass 
      of all detected components. Expression of the cloned cDNA in a eukaryotic
      virus-derived system yielded a recombinant protein that could be converted to an 
      active protease by treatment with trypsin. Polymerase chain reaction analyses of 
      cDNA from a number of human tissues showed high expression of the new enzyme in
      the skin and low expression in brain, placenta, and kidney. Homology searches
      yielded the highest score for porcine enamel matrix protease (55% amino acid
      sequence homology). High scores were also obtained for human and mouse neuropsin 
      and for human stratum corneum chymotryptic enzyme. The function of this new
      protease, tentatively named stratum corneum tryptic enzyme, may be related to
      stratum corneum turnover and desquamation in the epidermis.
FAU - Brattsand, M
AU  - Brattsand M
AD  - Department of Public Health, Umea University, SE-901 85 Umea, Sweden.
FAU - Egelrud, T
AU  - Egelrud T
LA  - eng
SI  - GENBANK/AF168768
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA, Complementary)
RN  - 0 (Recombinant Proteins)
RN  - EC 3.4.21.- (KLK5 protein, human)
RN  - EC 3.4.21.- (Kallikreins)
RN  - EC 3.4.21.- (Serine Endopeptidases)
RN  - EC 3.4.21.4 (Trypsin)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Blotting, Northern
MH  - Cell Line, Transformed
MH  - Chromatography, Liquid
MH  - Cloning, Molecular
MH  - Culture Techniques
MH  - DNA, Complementary
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Epidermis/*enzymology
MH  - Humans
MH  - Kallikreins
MH  - Mice
MH  - Molecular Sequence Data
MH  - Recombinant Proteins/genetics/isolation & purification/metabolism
MH  - Serine Endopeptidases/genetics/*isolation & purification/metabolism
MH  - Skin Diseases/*enzymology
MH  - Trypsin/metabolism
EDAT- 1999/10/09 00:00
MHDA- 1999/10/09 00:01
CRDT- 1999/10/09 00:00
PHST- 1999/10/09 00:00 [pubmed]
PHST- 1999/10/09 00:01 [medline]
PHST- 1999/10/09 00:00 [entrez]
AID - 10.1074/jbc.274.42.30033 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Oct 15;274(42):30033-40. doi: 10.1074/jbc.274.42.30033.