caa a22 4500 475774000 CHVBK 20180406123625.0 cr unu---uuuuu 170329e20000701xx s 000 0 eng 10.1007/s004180000163 doi (NATIONALLICENCE)springer-10.1007/s004180000163 Localization of porcine trappin-2 (SKALP/elafin) in trachea and large intestine by in situ hybridization and immunohistochemistry [Elektronische Daten] [Yohko Suzuki, Makoto Furukawa, Jumpei Abe, Masahide Kashiwagi, Shigehisa Hirose] Abstract.: Trappin-2 (SKALP/elafin), an elastase inhibitor, belongs to a unique family of proteinase inhibitors that are covalently anchored at the site of action through their transglutaminase substrate domain and are collectively called trappins. The transglutaminase substrate domain is therefore called "cementoin moiety". Currently, human, porcine, and bovine trappin-2 (SKALP/elafin) have been characterized. Previously, we showed that porcine trappin-2 (SKALP/elafin) occurs mainly in the trachea and large intestine. To determine the localization of trappin-2 (SKALP/elafin) at the cellular level, we carried out in situ hybridization and immunohistochemistry using the porcine trachea and large intestine and found that trappin-2 (SKALP/elafin) is produced in the goblet cells of the tracheal epithelium and of the large intestinal crypts. These locations suggest that trappin-2 (SKALP/elafin) is secreted onto the luminal surface of the trachea and crypts of Lieberkühn and plays a protective role against destructive bacterial proteinases. Springer-Verlag, 2000 Trappin Cementoin SKALP Elafin Goblet cell nationallicence Suzuki Yohko Department of Biological Sciences, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midoriku, Yokohama 226-8501, Japan aut Furukawa Makoto Department of Biological Sciences, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midoriku, Yokohama 226-8501, Japan aut Abe Jumpei Department of Biological Sciences, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midoriku, Yokohama 226-8501, Japan aut Kashiwagi Masahide Department of Biological Sciences, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midoriku, Yokohama 226-8501, Japan aut Hirose Shigehisa Department of Biological Sciences, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midoriku, Yokohama 226-8501, Japan aut https://doi.org/10.1007/s004180000163 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s004180000163 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Suzuki Yohko Department of Biological Sciences, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midoriku, Yokohama 226-8501, Japan aut NATIONALLICENCE 700 1- Furukawa Makoto Department of Biological Sciences, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midoriku, Yokohama 226-8501, Japan aut NATIONALLICENCE 700 1- Abe Jumpei Department of Biological Sciences, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midoriku, Yokohama 226-8501, Japan aut NATIONALLICENCE 700 1- Kashiwagi Masahide Department of Biological Sciences, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midoriku, Yokohama 226-8501, Japan aut NATIONALLICENCE 700 1- Hirose Shigehisa Department of Biological Sciences, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midoriku, Yokohama 226-8501, Japan aut Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer