ArticleThe Journal of experimental medicine1997
Secretory granule proteases in rat mast cells. Cloning of 10 different serine proteases and a carboxypeptidase A from various rat mast cell populations.
Article in The Journal of experimental medicine, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 157 citations in OpenAlex.
- Cultures of Human Skin Mast Cells, an Attractive In Vitro Model for Studies of Human Mast Cell Biology.Cells · 2024Article
- Heart Failure in Menopause: Treatment and New Approaches.International journal of molecular sciences · 2022Review
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- Mast Cell and Basophil Granule Proteases -Frontiers in immunology · 2022Review
- The Evolutionary History of theInternational journal of molecular sciences · 2021Review
- Modern Imaging Technologies of Mast Cells for Biology and Medicine (Review).Sovremennye tekhnologii v meditsine · 2021Review
- Extended Cleavage Specificity of the Rat Vascular Chymase, a Potential Blood Pressure Regulating Enzyme Expressed by Rat Vascular Smooth Muscle Cells.International journal of molecular sciences · 2020Article
- Article
- Phenotypic and Functional Diversity of Mast Cells.International journal of molecular sciences · 2020Article
- Article
- Extended cleavage specificities of two mast cell chymase-related proteases and one granzyme B-like protease from the platypus, a monotreme.International journal of molecular sciences · 2020Article
- Novel Insight into the in vivo Function of Mast Cell Chymase: Lessons from Knockouts and Inhibitors.Journal of innate immunity · 2020Review
- Analysis of Mrgprb2 Receptor-Evoked CaFrontiers in immunology · 2020Article
- Estrogen modulates the differential expression of cardiac myocyte chymase isoforms and diastolic function.Molecular and cellular biochemistry · 2019Article
- Chymase uptake by cardiomyocytes results in myosin degradation in cardiac volume overload.Heliyon · 2019Article
- Searching for tryptase in the RBL-2H3 mast cell model: Preparation for comparative mast cell toxicology studies with zebrafish.Journal of applied toxicology : JAT · 2019Article
- Short-term in vitro culture of purity and highly functional rat bone marrow-derived mast cells.In vitro cellular & developmental biology. Animal · 2018Article
- Article
- The Basophil-specific Protease mMCP-8 Provokes an Inflammatory Response in the Skin with Microvascular Hyperpermeability and Leukocyte Infiltration.The Journal of biological chemistry · 2017Article
- Tracing the Origins of IgE, Mast Cells, and Allergies by Studies of Wild Animals.Frontiers in immunology · 2017Review
Corrections and comments
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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
Two of the major rat mast cell proteases, rat mast cell protease 1 (RMCP-1) and RMCP-2, have for many years served as important phenotypic markers for studies of various aspects of mast cell (MC) biology. However, except for these proteases only fragmentary information has been available on the structure and complexity of proteases expressed by different subpopulations of rat MCs. To address these questions, cDNA libraries were constructed from freshly isolated rat peritoneal MCs and from the rat mucosal MC line RBL-1. cDNA clones for 10 different serine proteases (RMCP-1-10), and the MC carboxypeptidase A were isolated and characterized. Six of these proteases have not been isolated previously. Based on their protease content, three separate subpopulations of MCs were identified. Connective tissue MCs (CTMCs) from the ear and peritoneum express the chymases RMCP-1 and -5, the tryptases RMCP-6, and -7 and the carboxypeptidase A. However, based on a large difference in the level of expression of RMCP-7, CTMCs of these two organs may be regarded as two separate subpopulations. RMCP-2 and the three closely related proteases of the RMCP-8 subfamily were identified as the major mucosal MC proteases in rat. In contrast to what has been reported for human MCs, no expression of cathepsin G or cathepsin G-like proteases was detected in any of the rat MC populations. To determine mRNA frequencies for the various proteases expressed by normal tissue MCs, an unamplified peritoneal MC cDNA library was screened with a panel of mono-specific cDNA probes. These results showed that peritoneal MCs are highly specialized effector cells with mRNA frequencies for the major proteases in the range of several percent of the total mRNA pool.
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