Localization of porcine trappin-2 (SKALP/elafin) in trachea and large intestine by in situ hybridization and immunohistochemistry
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 c...
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2000 |
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| Umfang: |
6 |
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| Reproduktion: |
Springer Online Journal Archives 1860-2002 |
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| Übergeordnetes Werk: |
in: Histochemistry and cell biology - 1958, 114(2000) vom: Jan., Seite 15-20 |
| Übergeordnetes Werk: |
volume:114 ; year:2000 ; month:01 ; pages:15-20 ; extent:6 |
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| 245 | 1 | 0 | |a Localization of porcine trappin-2 (SKALP/elafin) in trachea and large intestine by in situ hybridization and immunohistochemistry |
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| 520 | |a 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. | ||
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(DE-627)NLEJ204371732 DE-627 ger DE-627 rakwb eng Localization of porcine trappin-2 (SKALP/elafin) in trachea and large intestine by in situ hybridization and immunohistochemistry 2000 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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 Online Journal Archives 1860-2002 Suzuki, Yohko oth Furukawa, Makoto oth Abe, Jumpei oth Kashiwagi, Masahide oth Hirose, Shigehisa oth in Histochemistry and cell biology 1958 114(2000) vom: Jan., Seite 15-20 (DE-627)NLEJ188988467 (DE-600)1398345-3 1432-119X nnns volume:114 year:2000 month:01 pages:15-20 extent:6 http://dx.doi.org/10.1007/s004180000163 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 114 2000 1 15-20 6 |
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(DE-627)NLEJ204371732 DE-627 ger DE-627 rakwb eng Localization of porcine trappin-2 (SKALP/elafin) in trachea and large intestine by in situ hybridization and immunohistochemistry 2000 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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 Online Journal Archives 1860-2002 Suzuki, Yohko oth Furukawa, Makoto oth Abe, Jumpei oth Kashiwagi, Masahide oth Hirose, Shigehisa oth in Histochemistry and cell biology 1958 114(2000) vom: Jan., Seite 15-20 (DE-627)NLEJ188988467 (DE-600)1398345-3 1432-119X nnns volume:114 year:2000 month:01 pages:15-20 extent:6 http://dx.doi.org/10.1007/s004180000163 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 114 2000 1 15-20 6 |
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(DE-627)NLEJ204371732 DE-627 ger DE-627 rakwb eng Localization of porcine trappin-2 (SKALP/elafin) in trachea and large intestine by in situ hybridization and immunohistochemistry 2000 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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 Online Journal Archives 1860-2002 Suzuki, Yohko oth Furukawa, Makoto oth Abe, Jumpei oth Kashiwagi, Masahide oth Hirose, Shigehisa oth in Histochemistry and cell biology 1958 114(2000) vom: Jan., Seite 15-20 (DE-627)NLEJ188988467 (DE-600)1398345-3 1432-119X nnns volume:114 year:2000 month:01 pages:15-20 extent:6 http://dx.doi.org/10.1007/s004180000163 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 114 2000 1 15-20 6 |
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(DE-627)NLEJ204371732 DE-627 ger DE-627 rakwb eng Localization of porcine trappin-2 (SKALP/elafin) in trachea and large intestine by in situ hybridization and immunohistochemistry 2000 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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 Online Journal Archives 1860-2002 Suzuki, Yohko oth Furukawa, Makoto oth Abe, Jumpei oth Kashiwagi, Masahide oth Hirose, Shigehisa oth in Histochemistry and cell biology 1958 114(2000) vom: Jan., Seite 15-20 (DE-627)NLEJ188988467 (DE-600)1398345-3 1432-119X nnns volume:114 year:2000 month:01 pages:15-20 extent:6 http://dx.doi.org/10.1007/s004180000163 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 114 2000 1 15-20 6 |
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(DE-627)NLEJ204371732 DE-627 ger DE-627 rakwb eng Localization of porcine trappin-2 (SKALP/elafin) in trachea and large intestine by in situ hybridization and immunohistochemistry 2000 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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 Online Journal Archives 1860-2002 Suzuki, Yohko oth Furukawa, Makoto oth Abe, Jumpei oth Kashiwagi, Masahide oth Hirose, Shigehisa oth in Histochemistry and cell biology 1958 114(2000) vom: Jan., Seite 15-20 (DE-627)NLEJ188988467 (DE-600)1398345-3 1432-119X nnns volume:114 year:2000 month:01 pages:15-20 extent:6 http://dx.doi.org/10.1007/s004180000163 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 114 2000 1 15-20 6 |
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localization of porcine trappin-2 (skalp/elafin) in trachea and large intestine by in situ hybridization and immunohistochemistry |
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Localization of porcine trappin-2 (SKALP/elafin) in trachea and large intestine by in situ hybridization and immunohistochemistry |
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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. |
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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. |
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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. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ204371732</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706151318.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070528s2000 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ204371732</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Localization of porcine trappin-2 (SKALP/elafin) in trachea and large intestine by in situ hybridization and immunohistochemistry</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2000</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">6</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">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.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Springer Online Journal Archives 1860-2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Suzuki, Yohko</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Furukawa, Makoto</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Abe, Jumpei</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kashiwagi, Masahide</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hirose, Shigehisa</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Histochemistry and cell biology</subfield><subfield code="d">1958</subfield><subfield code="g">114(2000) vom: Jan., Seite 15-20</subfield><subfield code="w">(DE-627)NLEJ188988467</subfield><subfield code="w">(DE-600)1398345-3</subfield><subfield code="x">1432-119X</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:114</subfield><subfield code="g">year:2000</subfield><subfield code="g">month:01</subfield><subfield code="g">pages:15-20</subfield><subfield code="g">extent:6</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1007/s004180000163</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SOJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">114</subfield><subfield code="j">2000</subfield><subfield code="c">1</subfield><subfield code="h">15-20</subfield><subfield code="g">6</subfield></datafield></record></collection>
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