Inhibitory effect of NH4Cl on secretion of collagen in human gingival fibroblasts
Identifieur interne : 000695 ( Istex/Corpus ); précédent : 000694; suivant : 000696Inhibitory effect of NH4Cl on secretion of collagen in human gingival fibroblasts
Auteurs : Kristen HelgelandSource :
- European Journal of Oral Sciences [ 0909-8836 ] ; 1984-10.
English descriptors
- Teeft :
- Amino, Amino acid pool, Amino acids, Ammonia, Ascorbic acid, Biochim biophys, Biol chem, Cell cultures, Cell layer, Cell type, Cellular fraction, Cellular pool, Chloroquine, Collagen, Collagen metabolism, Collagen secretion, Collagen synthesis, Control cultures, Control values, Cultured fibroblasts, Different lysosomotropic agents, Embryonic chick tendon cells, Extracellular collagen, Fibroblast, Fibronectin, General protein synthesis, Gingival, Human gingival fibroblasts, Inhibitory effect, Intracellular degradation, Methylamine, Nh4ci, Nh4ci treatment, Noncollagen, Noncollagen protein, Other proteins, Parallel cultures, Precursor pool, Prominent effect, Protein synthesis, Radiolabeled protein, Secretion.
Abstract
Abstract – The general protein synthesis in human gingival fibroblasts as measured by 14C‐proline incorporation was only moderately inhibited by 10 mM NH4Cl during incubation for 36 h. The proportion secreted as noncollagen protein and recovered from the cellular fraction as collagen was not significantly affected, whereas a pronounced inhibitory effect on the secretion of collagen was evident after 24 h. This effect was dose dependent, with a significant inhibition of collagen secretion even at 2 mM ammonia. The applied concentrations of NH4Cl had no significant effect on the hydroxylation of prolyl residues in collagen. Ammonia had no inhibitory effect on the secretion of fibronectin, another major secretory protein from fibroblasts. When comparing different lysosomotropic agents; NH4Cl, chloroquine and methylamine, the most prominent effect was consistently found to be an inhibition of the secretion of collagen.
Url:
DOI: 10.1111/j.1600-0722.1984.tb00911.x
Links to Exploration step
ISTEX:160100910C7F32CDDAB0369946BEABAF77C73932Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Inhibitory effect of NH4Cl on secretion of collagen in human gingival fibroblasts</title><author><name sortKey="Helgeland, Kristen" sort="Helgeland, Kristen" uniqKey="Helgeland K" first="Kristen" last="Helgeland">Kristen Helgeland</name><affiliation><mods:affiliation>Department of Microbiology, Dental Faculty, University of Oslo, Blindern, Oslo, Norway</mods:affiliation></affiliation><affiliation><mods:affiliation>Correspondence address: Department of Microbiology, Dental Faculty, University of Oslo, P.O.B. 1052, Blindern, Oslo 3, Norway.</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:160100910C7F32CDDAB0369946BEABAF77C73932</idno><date when="1984" year="1984">1984</date><idno type="doi">10.1111/j.1600-0722.1984.tb00911.x</idno><idno type="url">https://api.istex.fr/ark:/67375/WNG-BK37GLL1-3/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000695</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000695</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main">Inhibitory effect of NH4Cl on secretion of collagen in human gingival fibroblasts</title><author><name sortKey="Helgeland, Kristen" sort="Helgeland, Kristen" uniqKey="Helgeland K" first="Kristen" last="Helgeland">Kristen Helgeland</name><affiliation><mods:affiliation>Department of Microbiology, Dental Faculty, University of Oslo, Blindern, Oslo, Norway</mods:affiliation></affiliation><affiliation><mods:affiliation>Correspondence address: Department of Microbiology, Dental Faculty, University of Oslo, P.O.B. 1052, Blindern, Oslo 3, Norway.</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">European Journal of Oral Sciences</title><title level="j" type="alt">EUROPEAN JOURNAL OF ORAL SCIENCES</title><idno type="ISSN">0909-8836</idno><idno type="eISSN">1600-0722</idno><imprint><biblScope unit="vol">92</biblScope><biblScope unit="issue">5</biblScope><biblScope unit="page" from="419">419</biblScope><biblScope unit="page" to="425">425</biblScope><biblScope unit="page-count">7</biblScope><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="1984-10">1984-10</date></imprint><idno type="ISSN">0909-8836</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0909-8836</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Amino</term><term>Amino acid pool</term><term>Amino acids</term><term>Ammonia</term><term>Ascorbic acid</term><term>Biochim biophys</term><term>Biol chem</term><term>Cell cultures</term><term>Cell layer</term><term>Cell type</term><term>Cellular fraction</term><term>Cellular pool</term><term>Chloroquine</term><term>Collagen</term><term>Collagen metabolism</term><term>Collagen secretion</term><term>Collagen synthesis</term><term>Control cultures</term><term>Control values</term><term>Cultured fibroblasts</term><term>Different lysosomotropic agents</term><term>Embryonic chick tendon cells</term><term>Extracellular collagen</term><term>Fibroblast</term><term>Fibronectin</term><term>General protein synthesis</term><term>Gingival</term><term>Human gingival fibroblasts</term><term>Inhibitory effect</term><term>Intracellular degradation</term><term>Methylamine</term><term>Nh4ci</term><term>Nh4ci treatment</term><term>Noncollagen</term><term>Noncollagen protein</term><term>Other proteins</term><term>Parallel cultures</term><term>Precursor pool</term><term>Prominent effect</term><term>Protein synthesis</term><term>Radiolabeled protein</term><term>Secretion</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract – The general protein synthesis in human gingival fibroblasts as measured by 14C‐proline incorporation was only moderately inhibited by 10 mM NH4Cl during incubation for 36 h. The proportion secreted as noncollagen protein and recovered from the cellular fraction as collagen was not significantly affected, whereas a pronounced inhibitory effect on the secretion of collagen was evident after 24 h. This effect was dose dependent, with a significant inhibition of collagen secretion even at 2 mM ammonia. The applied concentrations of NH4Cl had no significant effect on the hydroxylation of prolyl residues in collagen. Ammonia had no inhibitory effect on the secretion of fibronectin, another major secretory protein from fibroblasts. When comparing different lysosomotropic agents; NH4Cl, chloroquine and methylamine, the most prominent effect was consistently found to be an inhibition of the secretion of collagen.</div></front></TEI><istex><corpusName>wiley</corpusName><keywords><teeft><json:string>nh4ci</json:string><json:string>fibroblast</json:string><json:string>ammonia</json:string><json:string>gingival</json:string><json:string>collagen</json:string><json:string>noncollagen</json:string><json:string>chloroquine</json:string><json:string>methylamine</json:string><json:string>fibronectin</json:string><json:string>human gingival fibroblasts</json:string><json:string>collagen secretion</json:string><json:string>noncollagen protein</json:string><json:string>collagen synthesis</json:string><json:string>inhibitory effect</json:string><json:string>general protein synthesis</json:string><json:string>secretion</json:string><json:string>amino</json:string><json:string>amino acids</json:string><json:string>cellular fraction</json:string><json:string>collagen metabolism</json:string><json:string>biol chem</json:string><json:string>radiolabeled protein</json:string><json:string>amino acid pool</json:string><json:string>ascorbic acid</json:string><json:string>cellular pool</json:string><json:string>cell layer</json:string><json:string>control values</json:string><json:string>precursor pool</json:string><json:string>prominent effect</json:string><json:string>control cultures</json:string><json:string>nh4ci treatment</json:string><json:string>intracellular degradation</json:string><json:string>cell cultures</json:string><json:string>parallel cultures</json:string><json:string>embryonic chick tendon cells</json:string><json:string>cell type</json:string><json:string>extracellular collagen</json:string><json:string>other proteins</json:string><json:string>cultured fibroblasts</json:string><json:string>biochim biophys</json:string><json:string>different lysosomotropic agents</json:string><json:string>protein synthesis</json:string></teeft></keywords><author><json:item><name>KRISTEN HELGELAND</name><affiliations><json:string>Department of Microbiology, Dental Faculty, University of Oslo, Blindern, Oslo, Norway</json:string><json:string>Correspondence address: Department of Microbiology, Dental Faculty, University of Oslo, P.O.B. 1052, Blindern, Oslo 3, Norway.</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>ammonia</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>collagen secretion</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>gingival fibroblasts</value></json:item></subject><articleId><json:string>EOS419</json:string></articleId><arkIstex>ark:/67375/WNG-BK37GLL1-3</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>Abstract – The general protein synthesis in human gingival fibroblasts as measured by 14C‐proline incorporation was only moderately inhibited by 10 mM NH4Cl during incubation for 36 h. 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The proportion secreted as noncollagen protein and recovered from the cellular fraction as collagen was not significantly affected, whereas a pronounced inhibitory effect on the secretion of collagen was evident after 24 h. This effect was dose dependent, with a significant inhibition of collagen secretion even at 2 mM ammonia. The applied concentrations of NH<sub>4</sub>Cl had no significant effect on the hydroxylation of prolyl residues in collagen. Ammonia had no inhibitory effect on the secretion of fibronectin, another major secretory protein from fibroblasts. When comparing different lysosomotropic agents; NH<sub>4</sub>Cl, chloroquine and methylamine, the most prominent effect was consistently found to be an inhibition of the secretion of collagen.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Inhibitory effect of NH4Cl on secretion of collagen in human gingival fibroblasts</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Inhibitory effect of NH4Cl on secretion of collagen in human gingival fibroblasts</title></titleInfo><name type="personal"><namePart type="given">KRISTEN</namePart><namePart type="family">HELGELAND</namePart><affiliation>Department of Microbiology, Dental Faculty, University of Oslo, Blindern, Oslo, Norway</affiliation><affiliation>Correspondence address: Department of Microbiology, Dental Faculty, University of Oslo, P.O.B. 1052, Blindern, Oslo 3, Norway.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><place><placeTerm type="text">Oxford, UK</placeTerm></place><dateIssued encoding="w3cdtf">1984-10</dateIssued><edition>Accepted for publication 14 January 1984</edition><copyrightDate encoding="w3cdtf">1984</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="references">28</extent><extent unit="linksCrossRef">2</extent></physicalDescription><abstract lang="en">Abstract – The general protein synthesis in human gingival fibroblasts as measured by 14C‐proline incorporation was only moderately inhibited by 10 mM NH4Cl during incubation for 36 h. The proportion secreted as noncollagen protein and recovered from the cellular fraction as collagen was not significantly affected, whereas a pronounced inhibitory effect on the secretion of collagen was evident after 24 h. This effect was dose dependent, with a significant inhibition of collagen secretion even at 2 mM ammonia. The applied concentrations of NH4Cl had no significant effect on the hydroxylation of prolyl residues in collagen. Ammonia had no inhibitory effect on the secretion of fibronectin, another major secretory protein from fibroblasts. When comparing different lysosomotropic agents; NH4Cl, chloroquine and methylamine, the most prominent effect was consistently found to be an inhibition of the secretion of collagen.</abstract><subject lang="en"><genre>keywords</genre><topic>ammonia</topic><topic>collagen secretion</topic><topic>gingival fibroblasts</topic></subject><relatedItem type="host"><titleInfo><title>European Journal of Oral Sciences</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><identifier type="ISSN">0909-8836</identifier><identifier type="eISSN">1600-0722</identifier><identifier type="DOI">10.1111/(ISSN)1600-0722</identifier><identifier type="PublisherID">EOS</identifier><part><date>1984</date><detail type="volume"><caption>vol.</caption><number>92</number></detail><detail type="issue"><caption>no.</caption><number>5</number></detail><extent unit="pages"><start>419</start><end>425</end><total>7</total></extent></part></relatedItem><relatedItem type="references" displayLabel="cit1"><titleInfo><title>Studies on the ammonia production and the ureolytic activity of dental plaque material</title></titleInfo><name type="personal"><namePart type="given">G.</namePart><namePart type="family">Frostell</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Frostell, G. Studies on the ammonia production and the ureolytic activity of dental plaque material. Acta Odontol Scand 1960; 18: 29–65.</note><part><date>1960</date><detail type="volume"><caption>vol.</caption><number>18</number></detail><extent unit="pages"><start>29</start><end>65</end></extent></part><relatedItem type="host"><titleInfo><title>Acta Odontol Scand</title></titleInfo><part><date>1960</date><detail type="volume"><caption>vol.</caption><number>18</number></detail><extent unit="pages"><start>29</start><end>65</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit2"><titleInfo><title>Ammonia and urea content of human incisor tooth plaque</title></titleInfo><name type="personal"><namePart type="given">DL</namePart><namePart type="family">Singer</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">I.</namePart><namePart type="family">Kleinberg</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Singer, DL, Kleinberg, I. 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