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Title: Human mast cell tryptase: Multiple cDNAs and genes reveal a multigene serine protease family

Abstract

Three different cDNAs and a gene encoding human skin mast cell tryptase have been cloned and sequenced in their entirety. The deduced amino acid sequences reveal a 30-amino acid prepropeptide followed by a 245-amino acid catalytic domain. The C-terminal undecapeptide of the human preprosequence is identical in dog tryptase and appears to be part of a prosequence unique among serine proteases. The differences among the three human tryptase catalytic domains include the loss of a consensus N-glycosylation site in one cDNA, which may explain some of the heterogeneity in size and susceptibility to deglycosylation seen in tryptase preparations. All three tryptase cDNAs are distinct from a recently reported cDNA obtained from a human lung mast cell library. A skin tryptase cDNA was used to isolate a human tryptase gene, the exons of which match one of the skin-derived cDNAs. The organization of the {approx}1.8-kilobase-pair tryptase gene is unique and is not closely related to that of any other mast cell or leukocyte serine protease. The 5{prime} regulatory regions of the gene share features with those of other serine proteases, including mast cell chymase, but are unusual in being separated from the protein-coding sequence by an intron. High-stringency hybridization of amore » human genomic DNA blot with a fragment of the tryptase gene confirms the presence of multiple tryptase genes. These findings provide genetic evidence that human mast cell tryptases are the products of a multigene family.« less

Authors:
; ; ; ;  [1]
  1. (Univ. of California, San Francisco (USA))
Publication Date:
OSTI Identifier:
5322959
Resource Type:
Journal Article
Resource Relation:
Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (United States); Journal Volume: 87:10
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; RECOMBINANT DNA; DNA SEQUENCING; SERINE PROTEINASES; AMINO ACID SEQUENCE; GENES; LYMPHOCYTES; MAST CELLS; PHOSPHORUS 32; SKIN; ANIMAL CELLS; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; BIOLOGICAL MATERIALS; BLOOD; BLOOD CELLS; BODY; BODY FLUIDS; CONNECTIVE TISSUE CELLS; DAYS LIVING RADIOISOTOPES; DNA; ENZYMES; HYDROLASES; ISOTOPES; LEUKOCYTES; LIGHT NUCLEI; MATERIALS; MOLECULAR STRUCTURE; NUCLEI; NUCLEIC ACIDS; ODD-ODD NUCLEI; ORGANIC COMPOUNDS; ORGANS; PEPTIDE HYDROLASES; PHOSPHORUS ISOTOPES; RADIOISOTOPES; SOMATIC CELLS; STRUCTURAL CHEMICAL ANALYSIS; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Vanderslice, P., Ballinger, S.M., Tam, E.K., Goldstein, S.M., Craik, C.S., and Caughey, G.H. Human mast cell tryptase: Multiple cDNAs and genes reveal a multigene serine protease family. United States: N. p., 1990. Web. doi:10.1073/pnas.87.10.3811.
Vanderslice, P., Ballinger, S.M., Tam, E.K., Goldstein, S.M., Craik, C.S., & Caughey, G.H. Human mast cell tryptase: Multiple cDNAs and genes reveal a multigene serine protease family. United States. doi:10.1073/pnas.87.10.3811.
Vanderslice, P., Ballinger, S.M., Tam, E.K., Goldstein, S.M., Craik, C.S., and Caughey, G.H. Tue . "Human mast cell tryptase: Multiple cDNAs and genes reveal a multigene serine protease family". United States. doi:10.1073/pnas.87.10.3811.
@article{osti_5322959,
title = {Human mast cell tryptase: Multiple cDNAs and genes reveal a multigene serine protease family},
author = {Vanderslice, P. and Ballinger, S.M., Tam, E.K. and Goldstein, S.M. and Craik, C.S. and Caughey, G.H.},
abstractNote = {Three different cDNAs and a gene encoding human skin mast cell tryptase have been cloned and sequenced in their entirety. The deduced amino acid sequences reveal a 30-amino acid prepropeptide followed by a 245-amino acid catalytic domain. The C-terminal undecapeptide of the human preprosequence is identical in dog tryptase and appears to be part of a prosequence unique among serine proteases. The differences among the three human tryptase catalytic domains include the loss of a consensus N-glycosylation site in one cDNA, which may explain some of the heterogeneity in size and susceptibility to deglycosylation seen in tryptase preparations. All three tryptase cDNAs are distinct from a recently reported cDNA obtained from a human lung mast cell library. A skin tryptase cDNA was used to isolate a human tryptase gene, the exons of which match one of the skin-derived cDNAs. The organization of the {approx}1.8-kilobase-pair tryptase gene is unique and is not closely related to that of any other mast cell or leukocyte serine protease. The 5{prime} regulatory regions of the gene share features with those of other serine proteases, including mast cell chymase, but are unusual in being separated from the protein-coding sequence by an intron. High-stringency hybridization of a human genomic DNA blot with a fragment of the tryptase gene confirms the presence of multiple tryptase genes. These findings provide genetic evidence that human mast cell tryptases are the products of a multigene family.},
doi = {10.1073/pnas.87.10.3811},
journal = {Proceedings of the National Academy of Sciences of the United States of America; (United States)},
number = ,
volume = 87:10,
place = {United States},
year = {Tue May 01 00:00:00 EDT 1990},
month = {Tue May 01 00:00:00 EDT 1990}
}