ArticleProceedings of the National Academy of Sciences of the United States of America2003
Polyserase-I, a human polyprotease with the ability to generate independent serine protease domains from a single translation product.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 59 citations in OpenAlex.
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- RNA sequencing-based analysis of the magnum tissues revealed the novel genes and biological pathways involved in the egg-white formation in the laying hen.BMC genomics · 2021Article
- Combination of whole exome sequencing and animal modeling identifies TMPRSS9 as a candidate gene for autism spectrum disorder.Human molecular genetics · 2020Article
- Substrate specificity of human metallocarboxypeptidase D: Comparison of the two active carboxypeptidase domains.PloS one · 2017Article
- Functional Genomic Analysis of the Impact of Camelina (Camelina sativa) Meal on Atlantic Salmon (Salmo salar) Distal Intestine Gene Expression and Physiology.Marine biotechnology (New York, N.Y.) · 2016Article
- Article
- DESC1 and MSPL activate influenza A viruses and emerging coronaviruses for host cell entry.Journal of virology · 2014Article
- Cleavage specificity analysis of six type II transmembrane serine proteases (TTSPs) using PICS with proteome-derived peptide libraries.PloS one · 2014Article
- TMPRSS9 and GRIN2B are associated with neuroticism: a genome-wide association study in a European sample.Journal of molecular neuroscience : MN · 2013Article
- Autosomal-recessive posterior microphthalmos is caused by mutations in PRSS56, a gene encoding a trypsin-like serine protease.American journal of human genetics · 2011Article
- Membrane-anchored serine proteases in health and disease.Progress in molecular biology and translational science · 2011Review
- Individual carboxypeptidase D domains have both redundant and unique functions in Drosophila development and behavior.Cellular and molecular life sciences : CMLS · 2010Article
- The cutting edge: membrane-anchored serine protease activities in the pericellular microenvironment.The Biochemical journal · 2010Review
- Matriptase-2 (TMPRSS6): a proteolytic regulator of iron homeostasis.Haematologica · 2009Review
- The Degradome database: mammalian proteases and diseases of proteolysis.Nucleic acids research · 2009Article
- Bimodal protein targeting through activation of cryptic mitochondrial targeting signals by an inducible cytosolic endoprotease.Molecular cell · 2008Article
- Human DESC1 serine protease confers tumorigenic properties to MDCK cells and it is upregulated in tumours of different origin.British journal of cancer · 2007Article
- Novel peroxisomal protease Tysnd1 processes PTS1- and PTS2-containing enzymes involved in beta-oxidation of fatty acids.The EMBO journal · 2007Article
- Serase-1B, a new splice variant of polyserase-1/TMPRSS9, activates urokinase-type plasminogen activator and the proteolytic activation is negatively regulated by glycosaminoglycans.The Biochemical journal · 2006Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have identified and cloned a human liver cDNA encoding an unusual mosaic polyprotein, called polyserase-I (polyserine protease-I). This protein exhibits a complex domain organization including a type II transmembrane motif, a low-density lipoprotein receptor A module, and three tandem serine protease domains. This unusual modular architecture is also present in the sequences predicted for mouse and rat polyserase-I. Human polyserase-I gene maps to 19p13, and its last exon overlaps with that corresponding to the 3' UTR of the gene encoding translocase of mitochondrial inner membrane 13. Northern blot analysis showed the presence of a major polyserase-I transcript of 5.4 kb in human fetal and adult tissues and in tumor cell lines. Analysis of processing mechanisms of polyserase-I revealed that it is synthesized as a membrane-associated polyprotein that is further processed to generate three independent serine protease units. Two of these domains are proteolytically active against synthetic peptides commonly used for assaying serine proteases. These proteolytic activities of the polyserase-I units are blocked by serine protease inhibitors. We show an example of generation of separate serine protease domains from a single translation product in human tissues and illustrate an additional mechanism for expanding the complexity of the human degradome, the entire protease complement of human cells and tissues.
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