tryptase Clara

from rat lung; preferentially recognizes a single arginine cleavage site cleaving Boc-Gln-Ala-Arg-4-methylcoumaryl-7-amide most efficiently; possible activator of inactive viral fusion glycoprotein in the respiratory tract and thus responsible for pneumopathogenicity of the virus

Networked: 8 relevant articles (0 outcomes, 1 trials/studies)

Bio-Agent Context: Research Results

Related Diseases

1.	Infections 04/01/1994 - "In this study, we investigated changes in the subcellular localization of tryptase Clara in rat bronchioles with progression of Sendai virus infection. " 03/01/1997 - "These findings indicate that tryptase Clara in the airway is a primary determinant of Sendai virus infection and that proteolytic activation occurs extracellularly. " 04/01/1994 - "Sendai virus infection changes the subcellular localization of tryptase Clara in rat bronchiolar epithelial cells." 05/10/1993 - "Intranasal infection of rats with Sendai virus was shown to stimulate secretion of tryptase Clara without changing the amount of surfactant in the bronchial lumen, resulting in a preferable condition for proteolytic viral activation and multiplication." 01/01/1996 - "Intranasal infection of rats with active (infectious) Sendai virus enhances secretion of tryptase Clara, a Sendai virus-activating protease, into the bronchial lumen by Clara cells of the bronchial epitheliums, and inversely suppresses secretion of pulmonary surfactant, an inhibitor of the protease, into the lumen [Kido H et al. (1993) FEBS Lett 322: 115-119]. "
2.	Human Influenza (Influenza) 01/01/1999 - "We report here that human mucus protease inhibitor (MPI), a major inhibitor of granulocyte elastase in the lining fluid of the human respiratory tract, significantly inhibited induction of the infectivity of influenza A and Sendai viruses by tryptase Clara in vitro and multicycles of mouse-adapted influenza A virus replication in rat lungs in vivo. " 02/01/1997 - "We report here that human mucus protease inhibitor (MPI), a major inhibitor of granulocyte elastase in the lining fluids of the human respiratory tract, significantly inhibited proteolytic activation of the infectivity of influenza A and Sendai viruses by tryptase Clara in vitro and multi-cycles of mouse-adapted influenza A virus replication in rat lungs in vitro. " 01/01/1996 - "Here we described the host cellular processing proteases, tryptase Clara and tryptase TL2, which proteolytically activate the infectivity of influenza A and Sendai viruses in the respiratory tract and HIV-1 in human CD4+ T cells, respectively. " 01/01/1999 - "Tryptase Clara, a trypsin-like protease localized exclusively in and secreted by Clara cells of the bronchial epithelium, is a prime host factor that processes viral envelope glycoproteins and determines the infectivity of influenza A and Sendai viruses (H. " 01/01/1993 - "The intracellular localization in rat bronchiolar epithelial cells of a novel trypsin-like protease named tryptase Clara, a possible activator of inactive viral fusion glycoprotein of influenza A and wild-type Sendai virus in the respiratory tract, was examined by electron microscopy. "
3.	Virus Diseases (Viral Diseases) 01/01/1999 - "Recombinant MPI and the C- but not the N-terminal domain of MPI inhibited both the activity of tryptase Clara and the induction of virus infection by tryptase Clara. " 02/01/1997 - "Recombinant MPI and the C- but not the N-terminal domain of the MPI inhibited both the proteolytic activity of tryptase Clara and the activation of virus infection. " 04/01/1994 - "These immunohistochemical results support our previous findings that in the bronchial lavage fluid tryptase Clara is significantly increased both in amount and activity after viral infection. "

Related Drugs and Biologics

1.	Peptide Hydrolases (Proteases)
2.	Secretory Leukocyte Peptidase Inhibitor
3.	Leukocyte Elastase (Neutrophil Elastase)
4.	Trypsin
5.	Viral Fusion Proteins
6.	Viral Envelope Proteins
7.	Surface-Active Agents (Surfactants)
8.	Pulmonary Surfactants (Pulmonary Surfactant)
9.	Phenobarbital (Luminal)
10.	Glycoproteins (Glycoprotein)