Bacterial pneumonia causes augmented expression of the secretory leukoprotease inhibitor gene in the murine lung

The cDNA of murine secretory leukoprotease inhibitor (SLPI) was cloned from a mouse lung cDNA library. The amino acid sequence deduced from the cDNA showed 58 and 51% homology with those of human and porcine SLPI, respectively. A two-domain structure with similar amino acid sequences, four intradoma...

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Veröffentlicht in:American journal of respiratory and critical care medicine 1997-10, Vol.156 (4), p.1235-1240
Hauptverfasser: ABE, T, TOMINAGA, Y, KIKUCHI, T, WATANABE, A, SATOH, K, WATANABE, Y, NUKIWA, T
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container_issue 4
container_start_page 1235
container_title American journal of respiratory and critical care medicine
container_volume 156
creator ABE, T
TOMINAGA, Y
KIKUCHI, T
WATANABE, A
SATOH, K
WATANABE, Y
NUKIWA, T
description The cDNA of murine secretory leukoprotease inhibitor (SLPI) was cloned from a mouse lung cDNA library. The amino acid sequence deduced from the cDNA showed 58 and 51% homology with those of human and porcine SLPI, respectively. A two-domain structure with similar amino acid sequences, four intradomain disulfide bonds, and high proline content, which are characteristics common to human and porcine SLPI, was also found in the mouse protein. The amino acid residues for the signal sequence and active site are also conserved in mouse SLPI. RNase protection assay showed the expression of the SLPI gene in liver, intestine, spleen, and epididymis, suggesting the distribution of SLPI in tissues other than lung and seminal vesicles. In the lung infected with Streptococcus pneumoniae strain FP1284, 10 h after inoculation of bacteria the number of SLPI mRNA transcripts was three times higher than baseline. The increased level of expression remained constant for at least 48 h. This result clearly contrasts to that obtained for spleen, in which the SLPI mRNA transcript level was mostly unchanged during the course of pneumonia. These facts suggested the local regulation of the SLPI gene expression in vivo in response to inflammatory stimuli at the site of inflammation.
doi_str_mv 10.1164/ajrccm.156.4.9701075
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The amino acid sequence deduced from the cDNA showed 58 and 51% homology with those of human and porcine SLPI, respectively. A two-domain structure with similar amino acid sequences, four intradomain disulfide bonds, and high proline content, which are characteristics common to human and porcine SLPI, was also found in the mouse protein. The amino acid residues for the signal sequence and active site are also conserved in mouse SLPI. RNase protection assay showed the expression of the SLPI gene in liver, intestine, spleen, and epididymis, suggesting the distribution of SLPI in tissues other than lung and seminal vesicles. In the lung infected with Streptococcus pneumoniae strain FP1284, 10 h after inoculation of bacteria the number of SLPI mRNA transcripts was three times higher than baseline. The increased level of expression remained constant for at least 48 h. This result clearly contrasts to that obtained for spleen, in which the SLPI mRNA transcript level was mostly unchanged during the course of pneumonia. 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The amino acid sequence deduced from the cDNA showed 58 and 51% homology with those of human and porcine SLPI, respectively. A two-domain structure with similar amino acid sequences, four intradomain disulfide bonds, and high proline content, which are characteristics common to human and porcine SLPI, was also found in the mouse protein. The amino acid residues for the signal sequence and active site are also conserved in mouse SLPI. RNase protection assay showed the expression of the SLPI gene in liver, intestine, spleen, and epididymis, suggesting the distribution of SLPI in tissues other than lung and seminal vesicles. In the lung infected with Streptococcus pneumoniae strain FP1284, 10 h after inoculation of bacteria the number of SLPI mRNA transcripts was three times higher than baseline. The increased level of expression remained constant for at least 48 h. This result clearly contrasts to that obtained for spleen, in which the SLPI mRNA transcript level was mostly unchanged during the course of pneumonia. 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TOMINAGA, Y ; KIKUCHI, T ; WATANABE, A ; SATOH, K ; WATANABE, Y ; NUKIWA, T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c362t-4cb3b4b071f040bd3783dba7f2c1ab6b8f9b41a96382ce0f203749b1221fc3bc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino Acid Sequence</topic><topic>Animal bacterial diseases</topic><topic>Animals</topic><topic>Bacterial diseases</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Blotting, Northern</topic><topic>Blotting, Southern</topic><topic>Cells, Cultured</topic><topic>Disease Models, Animal</topic><topic>DNA Probes - chemistry</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Humans</topic><topic>Infectious diseases</topic><topic>Lung - enzymology</topic><topic>Lung - pathology</topic><topic>Male</topic><topic>Medical sciences</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Molecular Sequence Data</topic><topic>Pneumonia, Pneumococcal - enzymology</topic><topic>Pneumonia, Pneumococcal - pathology</topic><topic>Polymerase Chain Reaction</topic><topic>Protein Biosynthesis</topic><topic>Proteinase Inhibitory Proteins, Secretory</topic><topic>Proteins - genetics</topic><topic>RNA, Messenger - analysis</topic><topic>Secretory Leukocyte Peptidase Inhibitor</topic><topic>Serine Proteinase Inhibitors - biosynthesis</topic><topic>Serine Proteinase Inhibitors - genetics</topic><topic>Spleen - enzymology</topic><topic>Spleen - pathology</topic><topic>Streptococcus pneumoniae</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>ABE, T</creatorcontrib><creatorcontrib>TOMINAGA, Y</creatorcontrib><creatorcontrib>KIKUCHI, T</creatorcontrib><creatorcontrib>WATANABE, A</creatorcontrib><creatorcontrib>SATOH, K</creatorcontrib><creatorcontrib>WATANABE, Y</creatorcontrib><creatorcontrib>NUKIWA, T</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>American journal of respiratory and critical care medicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>ABE, T</au><au>TOMINAGA, Y</au><au>KIKUCHI, T</au><au>WATANABE, A</au><au>SATOH, K</au><au>WATANABE, Y</au><au>NUKIWA, T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bacterial pneumonia causes augmented expression of the secretory leukoprotease inhibitor gene in the murine lung</atitle><jtitle>American journal of respiratory and critical care medicine</jtitle><addtitle>Am J Respir Crit Care Med</addtitle><date>1997-10-01</date><risdate>1997</risdate><volume>156</volume><issue>4</issue><spage>1235</spage><epage>1240</epage><pages>1235-1240</pages><issn>1073-449X</issn><eissn>1535-4970</eissn><abstract>The cDNA of murine secretory leukoprotease inhibitor (SLPI) was cloned from a mouse lung cDNA library. The amino acid sequence deduced from the cDNA showed 58 and 51% homology with those of human and porcine SLPI, respectively. A two-domain structure with similar amino acid sequences, four intradomain disulfide bonds, and high proline content, which are characteristics common to human and porcine SLPI, was also found in the mouse protein. The amino acid residues for the signal sequence and active site are also conserved in mouse SLPI. RNase protection assay showed the expression of the SLPI gene in liver, intestine, spleen, and epididymis, suggesting the distribution of SLPI in tissues other than lung and seminal vesicles. In the lung infected with Streptococcus pneumoniae strain FP1284, 10 h after inoculation of bacteria the number of SLPI mRNA transcripts was three times higher than baseline. The increased level of expression remained constant for at least 48 h. This result clearly contrasts to that obtained for spleen, in which the SLPI mRNA transcript level was mostly unchanged during the course of pneumonia. These facts suggested the local regulation of the SLPI gene expression in vivo in response to inflammatory stimuli at the site of inflammation.</abstract><cop>New York, NY</cop><pub>American Lung Association</pub><pmid>9351627</pmid><doi>10.1164/ajrccm.156.4.9701075</doi><tpages>6</tpages></addata></record>
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source MEDLINE; Journals@Ovid Complete; American Thoracic Society (ATS) Journals Online; EZB-FREE-00999 freely available EZB journals
subjects Amino Acid Sequence
Animal bacterial diseases
Animals
Bacterial diseases
Base Sequence
Biological and medical sciences
Blotting, Northern
Blotting, Southern
Cells, Cultured
Disease Models, Animal
DNA Probes - chemistry
Gene Expression Regulation, Enzymologic
Humans
Infectious diseases
Lung - enzymology
Lung - pathology
Male
Medical sciences
Mice
Mice, Inbred C57BL
Molecular Sequence Data
Pneumonia, Pneumococcal - enzymology
Pneumonia, Pneumococcal - pathology
Polymerase Chain Reaction
Protein Biosynthesis
Proteinase Inhibitory Proteins, Secretory
Proteins - genetics
RNA, Messenger - analysis
Secretory Leukocyte Peptidase Inhibitor
Serine Proteinase Inhibitors - biosynthesis
Serine Proteinase Inhibitors - genetics
Spleen - enzymology
Spleen - pathology
Streptococcus pneumoniae
Swine
title Bacterial pneumonia causes augmented expression of the secretory leukoprotease inhibitor gene in the murine lung
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