Identification of a new member of the tryptase family of mouse and human mast cell proteases which possesses a novel COOH-terminal hydrophobic extension

Guang William Wong, Yinzi Tang, Eric Feyfant, Andrej Šali, Lixin Li, Yong Li, Chifu Huang, Daniel S. Friend, Steven A. Krilis, Richard L. Stevens

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)30784-30793
Number of pages10
JournalJournal of Biological Chemistry
Volume274
Issue number43
DOIs
StatePublished - Oct 22 1999
Externally publishedYes

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Tryptases
Mast Cells
Peptide Hydrolases
Genes
Tissue
Chromosomes, Human, Pair 17
Serine Proteases
Human Genome
Mammals
Substrate Specificity
Substrates
Chromosomes
RNA
Physical properties
Membranes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Identification of a new member of the tryptase family of mouse and human mast cell proteases which possesses a novel COOH-terminal hydrophobic extension. / Wong, Guang William; Tang, Yinzi; Feyfant, Eric; Šali, Andrej; Li, Lixin; Li, Yong; Huang, Chifu; Friend, Daniel S.; Krilis, Steven A.; Stevens, Richard L.

In: Journal of Biological Chemistry, Vol. 274, No. 43, 22.10.1999, p. 30784-30793.

Research output: Contribution to journalArticle

Wong, Guang William ; Tang, Yinzi ; Feyfant, Eric ; Šali, Andrej ; Li, Lixin ; Li, Yong ; Huang, Chifu ; Friend, Daniel S. ; Krilis, Steven A. ; Stevens, Richard L. / Identification of a new member of the tryptase family of mouse and human mast cell proteases which possesses a novel COOH-terminal hydrophobic extension. In: Journal of Biological Chemistry. 1999 ; Vol. 274, No. 43. pp. 30784-30793.
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abstract = "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.",
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AU - Friend, Daniel S.

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AU - Stevens, Richard L.

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