Reverse Transcription Polymerase Chain Reaction (RT-PCR) Analysis of Proteolytic Enzymes in Cultures of Human Respiratory Epithelial Cells
Pancreatic proteolytic digestive enzymes are a major extracellular barrier to the sucessful systemic delivery of biopharmaceuticals via the oral route, whereas in health in the lungs these powerful proteases are virtually absent from the extracellular fluids. Despite this, the absorption of some (bu...
Gespeichert in:
| Veröffentlicht in: | Journal of aerosol medicine 2011-04, Vol.24 (2), p.89-101 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 101 |
|---|---|
| container_issue | 2 |
| container_start_page | 89 |
| container_title | Journal of aerosol medicine |
| container_volume | 24 |
| creator | BAGINSKI, Leonie TACHON, Gaëlle FALSON, Françoise PATTON, John S BAKOWSKY, Udo EHRHARDT, Carsten |
| description | Pancreatic proteolytic digestive enzymes are a major extracellular barrier to the sucessful systemic delivery of biopharmaceuticals via the oral route, whereas in health in the lungs these powerful proteases are virtually absent from the extracellular fluids. Despite this, the absorption of some (but not all) natural peptides and proteins from the lungs may be poor, and one has to acknowledge that information on the activity and spatial distribution of proteolytic enzymes in the human lung is scarce. Here, we investigated expression patterns of a series of proteolytic enzymes in several human respiratory cell types on mRNA level in an attempt to better understand the fate of inhaled biopharmaceuticals.
The mRNA expression of proteolytic enzymes (i.e., carboxypeptidases: CPA1, CPA2, CPB, CPM; gamma-glutamyltransferases: GGT1, GGT2; angiotensin-converting enzymes: ACE, ACE2; aminopeptidases: APA, APB, APN, APP1, APP2, APP3; endopeptidases: 24.11 (neprilysin), 24.15 (thimet oligopeptidase), 24.18 (meprin A); enteropeptidase; trypsin 1, trypsin 2; neutrophilic elastase; dipeptidyl peptidase 4; gamma-glutamylhydrolase) was investigated by semiquantitative RT-PCR in human bronchial (hBEpC, Calu-3, 16HBE14o-) and alveolar (A549) epithelial cells, respectively. Gastrointestinal Caco-2 cells were used as comparison.
Obvious differences were observed in proteinases' expression pattern between the investigated cell types. Although considered to be of bronchial epithelial phenotype, neither Calu-3 nor 16HBE14o- cells matched the mRNA expression pattern of hBEpC in primary culture. Of all investigated cell lines, Caco-2 expresses the highest number of proteases and peptidases.
Although mRNA expression does not necessarily signify enzyme functionality, our results provide the first comprehensive analysis of peptidase and protease expression and distribution in human lung epithelial cells and are the basis for further investigations. |
| doi_str_mv | 10.1089/jamp.2010.0842 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_861208378</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A254827096</galeid><sourcerecordid>A254827096</sourcerecordid><originalsourceid>FETCH-LOGICAL-c517t-f138cb075ececcc580de0b17e28c1447c678f5660c361bd78a030b433fcbef533</originalsourceid><addsrcrecordid>eNp9kl-L1DAUxYso7rr66qMERVwfZkyatEkfhzK6woLDMD6XNHPjZkibmrTC-BH81N7ujivIInnIn_s7h0vuybKXjC4ZVdWHg-6GZU7xSpXIH2XnrBJskUvKH9-fGTvLnqV0oLRkouRPs7OcCUZ5Xpxnv7bwA2ICsou6Tya6YXShJ5vgjx1EjYX6RruebEGb28rldrfY1Nv3ZNVrf0wukWDJJoYRUDI6Q9b9T5QmgqJ68uMU4Ra5mjo926TBRT2GeCTrwY034J32pAbv0_PsidU-wYvTfpF9_bje1VeL6y-fPter64UpmBwXlnFlWioLMGCMKRTdA22ZhFwZJoQ0pVS2KEtqeMnavVSactoKzq1pwRacX2Tv7nyHGL5PkMamc8lgB7qHMKVGlSynikuF5OV_SUYrLpjg1Yy-_gc9hCniF81-VDKJo0DozR30TXtoXG_DGLWZPZtVXgiFY6tKpJYPULj20DkTerAO3x8SmBhSimCbIbpOxyM22MwpaeaUNHNKmjklKHh1anZqO9jf439igcDbE6CT0d5iNoxLfzmBNiqv-G--9MRF</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>860717941</pqid></control><display><type>article</type><title>Reverse Transcription Polymerase Chain Reaction (RT-PCR) Analysis of Proteolytic Enzymes in Cultures of Human Respiratory Epithelial Cells</title><source>MEDLINE</source><source>Alma/SFX Local Collection</source><creator>BAGINSKI, Leonie ; TACHON, Gaëlle ; FALSON, Françoise ; PATTON, John S ; BAKOWSKY, Udo ; EHRHARDT, Carsten</creator><creatorcontrib>BAGINSKI, Leonie ; TACHON, Gaëlle ; FALSON, Françoise ; PATTON, John S ; BAKOWSKY, Udo ; EHRHARDT, Carsten</creatorcontrib><description>Pancreatic proteolytic digestive enzymes are a major extracellular barrier to the sucessful systemic delivery of biopharmaceuticals via the oral route, whereas in health in the lungs these powerful proteases are virtually absent from the extracellular fluids. Despite this, the absorption of some (but not all) natural peptides and proteins from the lungs may be poor, and one has to acknowledge that information on the activity and spatial distribution of proteolytic enzymes in the human lung is scarce. Here, we investigated expression patterns of a series of proteolytic enzymes in several human respiratory cell types on mRNA level in an attempt to better understand the fate of inhaled biopharmaceuticals.
The mRNA expression of proteolytic enzymes (i.e., carboxypeptidases: CPA1, CPA2, CPB, CPM; gamma-glutamyltransferases: GGT1, GGT2; angiotensin-converting enzymes: ACE, ACE2; aminopeptidases: APA, APB, APN, APP1, APP2, APP3; endopeptidases: 24.11 (neprilysin), 24.15 (thimet oligopeptidase), 24.18 (meprin A); enteropeptidase; trypsin 1, trypsin 2; neutrophilic elastase; dipeptidyl peptidase 4; gamma-glutamylhydrolase) was investigated by semiquantitative RT-PCR in human bronchial (hBEpC, Calu-3, 16HBE14o-) and alveolar (A549) epithelial cells, respectively. Gastrointestinal Caco-2 cells were used as comparison.
Obvious differences were observed in proteinases' expression pattern between the investigated cell types. Although considered to be of bronchial epithelial phenotype, neither Calu-3 nor 16HBE14o- cells matched the mRNA expression pattern of hBEpC in primary culture. Of all investigated cell lines, Caco-2 expresses the highest number of proteases and peptidases.
Although mRNA expression does not necessarily signify enzyme functionality, our results provide the first comprehensive analysis of peptidase and protease expression and distribution in human lung epithelial cells and are the basis for further investigations.</description><identifier>ISSN: 1941-2711</identifier><identifier>ISSN: 1941-2703</identifier><identifier>EISSN: 1941-2703</identifier><identifier>DOI: 10.1089/jamp.2010.0842</identifier><identifier>PMID: 21410325</identifier><language>eng</language><publisher>New Rochelle, NY: Mary Ann Liebert</publisher><subject>Aerosols ; Alveoli ; Aminopeptidase ; Aspartic proteinases ; Biological and medical sciences ; Caco-2 Cells ; Carboxypeptidase ; Cell culture ; Cells, Cultured ; Digestive enzymes ; Drug delivery ; Elastase ; endopeptidase ; Enteropeptidase ; Epithelial cells ; Epithelial Cells - enzymology ; gamma -Glutamyltransferase ; Gene expression ; Gene Expression Profiling - methods ; Gene Expression Regulation, Enzymologic ; General pharmacology ; Genetic aspects ; Health technology assessment ; Humans ; Intestinal Mucosa - enzymology ; Leukocytes (neutrophilic) ; Lung ; Medical sciences ; Meprin A ; Neprilysin ; Pancreas ; peptidase ; Peptide Hydrolases - genetics ; Pharmaceutical technology. Pharmaceutical industry ; Pharmaceuticals ; Pharmacology. Drug treatments ; Physiological aspects ; Polymerase chain reaction ; Practice ; Proteinase ; Proteolysis ; Proteolytic enzymes ; Registered nurses ; Respiration ; Respiratory Mucosa - enzymology ; Reverse Transcriptase Polymerase Chain Reaction ; Reverse transcription ; RNA, Messenger - metabolism ; Spatial distribution ; Thimet oligopeptidase ; Trypsin</subject><ispartof>Journal of aerosol medicine, 2011-04, Vol.24 (2), p.89-101</ispartof><rights>2015 INIST-CNRS</rights><rights>COPYRIGHT 2011 Mary Ann Liebert, Inc.</rights><rights>(©) Copyright 2011, Mary Ann Liebert, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c517t-f138cb075ececcc580de0b17e28c1447c678f5660c361bd78a030b433fcbef533</citedby><cites>FETCH-LOGICAL-c517t-f138cb075ececcc580de0b17e28c1447c678f5660c361bd78a030b433fcbef533</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=24084829$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21410325$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>BAGINSKI, Leonie</creatorcontrib><creatorcontrib>TACHON, Gaëlle</creatorcontrib><creatorcontrib>FALSON, Françoise</creatorcontrib><creatorcontrib>PATTON, John S</creatorcontrib><creatorcontrib>BAKOWSKY, Udo</creatorcontrib><creatorcontrib>EHRHARDT, Carsten</creatorcontrib><title>Reverse Transcription Polymerase Chain Reaction (RT-PCR) Analysis of Proteolytic Enzymes in Cultures of Human Respiratory Epithelial Cells</title><title>Journal of aerosol medicine</title><addtitle>J Aerosol Med Pulm Drug Deliv</addtitle><description>Pancreatic proteolytic digestive enzymes are a major extracellular barrier to the sucessful systemic delivery of biopharmaceuticals via the oral route, whereas in health in the lungs these powerful proteases are virtually absent from the extracellular fluids. Despite this, the absorption of some (but not all) natural peptides and proteins from the lungs may be poor, and one has to acknowledge that information on the activity and spatial distribution of proteolytic enzymes in the human lung is scarce. Here, we investigated expression patterns of a series of proteolytic enzymes in several human respiratory cell types on mRNA level in an attempt to better understand the fate of inhaled biopharmaceuticals.
The mRNA expression of proteolytic enzymes (i.e., carboxypeptidases: CPA1, CPA2, CPB, CPM; gamma-glutamyltransferases: GGT1, GGT2; angiotensin-converting enzymes: ACE, ACE2; aminopeptidases: APA, APB, APN, APP1, APP2, APP3; endopeptidases: 24.11 (neprilysin), 24.15 (thimet oligopeptidase), 24.18 (meprin A); enteropeptidase; trypsin 1, trypsin 2; neutrophilic elastase; dipeptidyl peptidase 4; gamma-glutamylhydrolase) was investigated by semiquantitative RT-PCR in human bronchial (hBEpC, Calu-3, 16HBE14o-) and alveolar (A549) epithelial cells, respectively. Gastrointestinal Caco-2 cells were used as comparison.
Obvious differences were observed in proteinases' expression pattern between the investigated cell types. Although considered to be of bronchial epithelial phenotype, neither Calu-3 nor 16HBE14o- cells matched the mRNA expression pattern of hBEpC in primary culture. Of all investigated cell lines, Caco-2 expresses the highest number of proteases and peptidases.
Although mRNA expression does not necessarily signify enzyme functionality, our results provide the first comprehensive analysis of peptidase and protease expression and distribution in human lung epithelial cells and are the basis for further investigations.</description><subject>Aerosols</subject><subject>Alveoli</subject><subject>Aminopeptidase</subject><subject>Aspartic proteinases</subject><subject>Biological and medical sciences</subject><subject>Caco-2 Cells</subject><subject>Carboxypeptidase</subject><subject>Cell culture</subject><subject>Cells, Cultured</subject><subject>Digestive enzymes</subject><subject>Drug delivery</subject><subject>Elastase</subject><subject>endopeptidase</subject><subject>Enteropeptidase</subject><subject>Epithelial cells</subject><subject>Epithelial Cells - enzymology</subject><subject>gamma -Glutamyltransferase</subject><subject>Gene expression</subject><subject>Gene Expression Profiling - methods</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>General pharmacology</subject><subject>Genetic aspects</subject><subject>Health technology assessment</subject><subject>Humans</subject><subject>Intestinal Mucosa - enzymology</subject><subject>Leukocytes (neutrophilic)</subject><subject>Lung</subject><subject>Medical sciences</subject><subject>Meprin A</subject><subject>Neprilysin</subject><subject>Pancreas</subject><subject>peptidase</subject><subject>Peptide Hydrolases - genetics</subject><subject>Pharmaceutical technology. Pharmaceutical industry</subject><subject>Pharmaceuticals</subject><subject>Pharmacology. Drug treatments</subject><subject>Physiological aspects</subject><subject>Polymerase chain reaction</subject><subject>Practice</subject><subject>Proteinase</subject><subject>Proteolysis</subject><subject>Proteolytic enzymes</subject><subject>Registered nurses</subject><subject>Respiration</subject><subject>Respiratory Mucosa - enzymology</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Reverse transcription</subject><subject>RNA, Messenger - metabolism</subject><subject>Spatial distribution</subject><subject>Thimet oligopeptidase</subject><subject>Trypsin</subject><issn>1941-2711</issn><issn>1941-2703</issn><issn>1941-2703</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9kl-L1DAUxYso7rr66qMERVwfZkyatEkfhzK6woLDMD6XNHPjZkibmrTC-BH81N7ujivIInnIn_s7h0vuybKXjC4ZVdWHg-6GZU7xSpXIH2XnrBJskUvKH9-fGTvLnqV0oLRkouRPs7OcCUZ5Xpxnv7bwA2ICsou6Tya6YXShJ5vgjx1EjYX6RruebEGb28rldrfY1Nv3ZNVrf0wukWDJJoYRUDI6Q9b9T5QmgqJ68uMU4Ra5mjo926TBRT2GeCTrwY034J32pAbv0_PsidU-wYvTfpF9_bje1VeL6y-fPter64UpmBwXlnFlWioLMGCMKRTdA22ZhFwZJoQ0pVS2KEtqeMnavVSactoKzq1pwRacX2Tv7nyHGL5PkMamc8lgB7qHMKVGlSynikuF5OV_SUYrLpjg1Yy-_gc9hCniF81-VDKJo0DozR30TXtoXG_DGLWZPZtVXgiFY6tKpJYPULj20DkTerAO3x8SmBhSimCbIbpOxyM22MwpaeaUNHNKmjklKHh1anZqO9jf439igcDbE6CT0d5iNoxLfzmBNiqv-G--9MRF</recordid><startdate>20110401</startdate><enddate>20110401</enddate><creator>BAGINSKI, Leonie</creator><creator>TACHON, Gaëlle</creator><creator>FALSON, Françoise</creator><creator>PATTON, John S</creator><creator>BAKOWSKY, Udo</creator><creator>EHRHARDT, Carsten</creator><general>Mary Ann Liebert</general><general>Mary Ann Liebert, Inc</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7T5</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>H94</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>20110401</creationdate><title>Reverse Transcription Polymerase Chain Reaction (RT-PCR) Analysis of Proteolytic Enzymes in Cultures of Human Respiratory Epithelial Cells</title><author>BAGINSKI, Leonie ; TACHON, Gaëlle ; FALSON, Françoise ; PATTON, John S ; BAKOWSKY, Udo ; EHRHARDT, Carsten</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c517t-f138cb075ececcc580de0b17e28c1447c678f5660c361bd78a030b433fcbef533</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Aerosols</topic><topic>Alveoli</topic><topic>Aminopeptidase</topic><topic>Aspartic proteinases</topic><topic>Biological and medical sciences</topic><topic>Caco-2 Cells</topic><topic>Carboxypeptidase</topic><topic>Cell culture</topic><topic>Cells, Cultured</topic><topic>Digestive enzymes</topic><topic>Drug delivery</topic><topic>Elastase</topic><topic>endopeptidase</topic><topic>Enteropeptidase</topic><topic>Epithelial cells</topic><topic>Epithelial Cells - enzymology</topic><topic>gamma -Glutamyltransferase</topic><topic>Gene expression</topic><topic>Gene Expression Profiling - methods</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>General pharmacology</topic><topic>Genetic aspects</topic><topic>Health technology assessment</topic><topic>Humans</topic><topic>Intestinal Mucosa - enzymology</topic><topic>Leukocytes (neutrophilic)</topic><topic>Lung</topic><topic>Medical sciences</topic><topic>Meprin A</topic><topic>Neprilysin</topic><topic>Pancreas</topic><topic>peptidase</topic><topic>Peptide Hydrolases - genetics</topic><topic>Pharmaceutical technology. Pharmaceutical industry</topic><topic>Pharmaceuticals</topic><topic>Pharmacology. Drug treatments</topic><topic>Physiological aspects</topic><topic>Polymerase chain reaction</topic><topic>Practice</topic><topic>Proteinase</topic><topic>Proteolysis</topic><topic>Proteolytic enzymes</topic><topic>Registered nurses</topic><topic>Respiration</topic><topic>Respiratory Mucosa - enzymology</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Reverse transcription</topic><topic>RNA, Messenger - metabolism</topic><topic>Spatial distribution</topic><topic>Thimet oligopeptidase</topic><topic>Trypsin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>BAGINSKI, Leonie</creatorcontrib><creatorcontrib>TACHON, Gaëlle</creatorcontrib><creatorcontrib>FALSON, Françoise</creatorcontrib><creatorcontrib>PATTON, John S</creatorcontrib><creatorcontrib>BAKOWSKY, Udo</creatorcontrib><creatorcontrib>EHRHARDT, Carsten</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>ProQuest Central (Corporate)</collection><collection>Immunology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of aerosol medicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>BAGINSKI, Leonie</au><au>TACHON, Gaëlle</au><au>FALSON, Françoise</au><au>PATTON, John S</au><au>BAKOWSKY, Udo</au><au>EHRHARDT, Carsten</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reverse Transcription Polymerase Chain Reaction (RT-PCR) Analysis of Proteolytic Enzymes in Cultures of Human Respiratory Epithelial Cells</atitle><jtitle>Journal of aerosol medicine</jtitle><addtitle>J Aerosol Med Pulm Drug Deliv</addtitle><date>2011-04-01</date><risdate>2011</risdate><volume>24</volume><issue>2</issue><spage>89</spage><epage>101</epage><pages>89-101</pages><issn>1941-2711</issn><issn>1941-2703</issn><eissn>1941-2703</eissn><abstract>Pancreatic proteolytic digestive enzymes are a major extracellular barrier to the sucessful systemic delivery of biopharmaceuticals via the oral route, whereas in health in the lungs these powerful proteases are virtually absent from the extracellular fluids. Despite this, the absorption of some (but not all) natural peptides and proteins from the lungs may be poor, and one has to acknowledge that information on the activity and spatial distribution of proteolytic enzymes in the human lung is scarce. Here, we investigated expression patterns of a series of proteolytic enzymes in several human respiratory cell types on mRNA level in an attempt to better understand the fate of inhaled biopharmaceuticals.
The mRNA expression of proteolytic enzymes (i.e., carboxypeptidases: CPA1, CPA2, CPB, CPM; gamma-glutamyltransferases: GGT1, GGT2; angiotensin-converting enzymes: ACE, ACE2; aminopeptidases: APA, APB, APN, APP1, APP2, APP3; endopeptidases: 24.11 (neprilysin), 24.15 (thimet oligopeptidase), 24.18 (meprin A); enteropeptidase; trypsin 1, trypsin 2; neutrophilic elastase; dipeptidyl peptidase 4; gamma-glutamylhydrolase) was investigated by semiquantitative RT-PCR in human bronchial (hBEpC, Calu-3, 16HBE14o-) and alveolar (A549) epithelial cells, respectively. Gastrointestinal Caco-2 cells were used as comparison.
Obvious differences were observed in proteinases' expression pattern between the investigated cell types. Although considered to be of bronchial epithelial phenotype, neither Calu-3 nor 16HBE14o- cells matched the mRNA expression pattern of hBEpC in primary culture. Of all investigated cell lines, Caco-2 expresses the highest number of proteases and peptidases.
Although mRNA expression does not necessarily signify enzyme functionality, our results provide the first comprehensive analysis of peptidase and protease expression and distribution in human lung epithelial cells and are the basis for further investigations.</abstract><cop>New Rochelle, NY</cop><pub>Mary Ann Liebert</pub><pmid>21410325</pmid><doi>10.1089/jamp.2010.0842</doi><tpages>13</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1941-2711 |
| ispartof | Journal of aerosol medicine, 2011-04, Vol.24 (2), p.89-101 |
| issn | 1941-2711 1941-2703 1941-2703 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_861208378 |
| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Aerosols Alveoli Aminopeptidase Aspartic proteinases Biological and medical sciences Caco-2 Cells Carboxypeptidase Cell culture Cells, Cultured Digestive enzymes Drug delivery Elastase endopeptidase Enteropeptidase Epithelial cells Epithelial Cells - enzymology gamma -Glutamyltransferase Gene expression Gene Expression Profiling - methods Gene Expression Regulation, Enzymologic General pharmacology Genetic aspects Health technology assessment Humans Intestinal Mucosa - enzymology Leukocytes (neutrophilic) Lung Medical sciences Meprin A Neprilysin Pancreas peptidase Peptide Hydrolases - genetics Pharmaceutical technology. Pharmaceutical industry Pharmaceuticals Pharmacology. Drug treatments Physiological aspects Polymerase chain reaction Practice Proteinase Proteolysis Proteolytic enzymes Registered nurses Respiration Respiratory Mucosa - enzymology Reverse Transcriptase Polymerase Chain Reaction Reverse transcription RNA, Messenger - metabolism Spatial distribution Thimet oligopeptidase Trypsin |
| title | Reverse Transcription Polymerase Chain Reaction (RT-PCR) Analysis of Proteolytic Enzymes in Cultures of Human Respiratory Epithelial Cells |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-08T21%3A43%3A27IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Reverse%20Transcription%20Polymerase%20Chain%20Reaction%20(RT-PCR)%20Analysis%20of%20Proteolytic%20Enzymes%20in%20Cultures%20of%20Human%20Respiratory%20Epithelial%20Cells&rft.jtitle=Journal%20of%20aerosol%20medicine&rft.au=BAGINSKI,%20Leonie&rft.date=2011-04-01&rft.volume=24&rft.issue=2&rft.spage=89&rft.epage=101&rft.pages=89-101&rft.issn=1941-2711&rft.eissn=1941-2703&rft_id=info:doi/10.1089/jamp.2010.0842&rft_dat=%3Cgale_proqu%3EA254827096%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=860717941&rft_id=info:pmid/21410325&rft_galeid=A254827096&rfr_iscdi=true |