PMID- 10521469
OWN - NLM
STAT- MEDLINE
DCOM- 19991123
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 43
DP  - 1999 Oct 22
TI  - Identification of a new member of the tryptase family of mouse and human mast 
      cell proteases which possesses a novel COOH-terminal hydrophobic extension.
PG  - 30784-93
AB  - Mapping of the tryptase locus on chromosome 17 revealed a novel gene 2.3 kilobase 
      3' of the mouse mast cell protease (mMCP) 6 gene. This 3.7-kilobase gene encodes 
      the first example of a protease in the tryptase family that contains a 
      membrane-spanning segment located at its COOH terminus. Comparative structural 
      studies indicated that the putative transmembrane tryptase (TMT) possesses a 
      unique substrate-binding cleft. As assessed by RNA blot analyses, mTMT is 
      expressed in mice in both strain- and tissue-dependent manners. Thus, different 
      transcriptional and/or post-transcriptional mechanisms are used to control the 
      expression of mTMT in vivo. Analysis of the corresponding tryptase locus in the 
      human genome resulted in the isolation and characterization of the hTMT gene. The 
      hTMT transcript is expressed in numerous tissues and is also translated. Analysis 
      of the tryptase family of genes in mice and humans now indicates that a 
      primordial serine protease gene duplicated early and often during the evolution 
      of mammals to generate a panel of homologous tryptases in each species that 
      differ in their tissue expression, substrate specificities, and physical 
      properties.
FAU - Wong, G W
AU  - Wong GW
AD  - Department of Medicine, Harvard Medical School, Brigham and Women's Hospital, 
      Boston, Massachusetts 02115, USA.
FAU - Tang, Y
AU  - Tang Y
FAU - Feyfant, E
AU  - Feyfant E
FAU - Sali, A
AU  - Sali A
FAU - Li, L
AU  - Li L
FAU - Li, Y
AU  - Li Y
FAU - Huang, C
AU  - Huang C
FAU - Friend, D S
AU  - Friend DS
FAU - Krilis, S A
AU  - Krilis SA
FAU - Stevens, R L
AU  - Stevens RL
LA  - eng
SI  - GENBANK/AF175522
SI  - GENBANK/AF175523
SI  - GENBANK/AF175759
SI  - GENBANK/AF175760
GR  - AI-23483/AI/NIAID NIH HHS/United States
GR  - GM-54762/GM/NIGMS NIH HHS/United States
GR  - HL-36110/HL/NHLBI NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Recombinant Proteins)
RN  - 0 (Tpsb2 protein, mouse)
RN  - EC 3.4.21.- (Serine Endopeptidases)
RN  - EC 3.4.21.- (chymase 2)
RN  - EC 3.4.21.39 (Chymases)
RN  - EC 3.4.21.59 (Tpsab1 protein, mouse)
RN  - EC 3.4.21.59 (Tryptases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Cell Membrane/enzymology
MH  - *Chromosome Mapping
MH  - Chymases
MH  - Cloning, Molecular
MH  - Female
MH  - Genome, Human
MH  - Humans
MH  - Kinetics
MH  - Male
MH  - Mast Cells/*enzymology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mice, Inbred C57BL
MH  - Molecular Sequence Data
MH  - Organ Specificity
MH  - Protein Biosynthesis
MH  - Recombinant Proteins/chemistry
MH  - Restriction Mapping
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Serine Endopeptidases/chemistry/*genetics
MH  - *Transcription, Genetic
MH  - Tryptases
EDAT- 1999/10/16 00:00
MHDA- 1999/10/16 00:01
CRDT- 1999/10/16 00:00
PHST- 1999/10/16 00:00 [pubmed]
PHST- 1999/10/16 00:01 [medline]
PHST- 1999/10/16 00:00 [entrez]
AID - S0021-9258(19)51749-5 [pii]
AID - 10.1074/jbc.274.43.30784 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Oct 22;274(43):30784-93. doi: 10.1074/jbc.274.43.30784.