Fluorescence studies on binding of amphiphilic drugs to isolated lamellar bodies: relevance to phospholipidosis.
Identifieur interne : 000562 ( PubMed/Corpus ); précédent : 000561; suivant : 000563Fluorescence studies on binding of amphiphilic drugs to isolated lamellar bodies: relevance to phospholipidosis.
Auteurs : U M Joshi ; P. Rao ; S. Kodavanti ; V G Lockard ; H M MehendaleSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 1989.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Amines.
- chemical : Anilino Naphthalenesulfonates, Diphenylhexatriene, Phospholipids.
- metabolism : Lung, Organelles.
- ultrastructure : Lung.
- Animals, In Vitro Techniques, Male, Microscopy, Electron, Rats, Rats, Inbred Strains, Spectrometry, Fluorescence.
Abstract
Lysosomal phospholipid storage disorder in lung tissue was observed during chronic treatment with amphiphilic amine drugs. The prevailing and widely accepted mechanism of phospholipidosis is that amphiphilic drugs bind to phospholipids and make the phospholipids unsuitable substrates for the action of phospholipases. We investigated hydrophobic and hydrophilic binding of fifteen drugs to the phospholipid storage organelle, lung lamellar bodies, isolated from male Sprague-Dawley rats. Hydrophobic interactions were studied using 1,6-diphenyl-1,3,5-hexatriene as a fluorescent probe and hydrophilic binding was studied using 1-anilino-8-naphthalene sulfonate as a fluorescent probe. The binding parameters were calculated using Scatchard equations. Of the fifteen drugs used, nine drugs bound to the hydrophobic moiety of lamellar bodies. The order of binding capacities was promethazine greater than chloramphenicol greater than amiodarone = desethylamiodarone greater than promazine greater than chlorpromazine greater than trimipramine greater than propranolol greater than imipramine much greater than chlorphentermine, phentermine, chloroquine, chlorimipramine, cyclizine and chlorcyclizine. Two binding affinities were calculated for all the bound drugs. Binding affinities to hydrophilic sites of lamellar bodies were calculated in terms of emission coefficients for 1-anilino-8-naphthalene sulfonate in the presence of drugs. Hydrophilic binding was in the order chlorpromazine greater than chlorimipramine greater than promazine greater than trimipramine greater than imipramine greater than chlorcyclizine greater than propranolol greater than promethazine greater than chlorphentermine greater than cyclizine greater than phentermine greater than chloroquine much greater than chloramphenicol, amiodarone and desethylamiodarone. The binding affinities of chlorinated analogs were stronger to hydrophilic sites when compared to the parent compound. Amiodarone, which is known to induce pulmonary phospholipidosis and its major non-polar metabolite, desethylamiodarone, bound strongly to lamellar bodies. These two drugs also inhibit phospholipases in vitro. The drugs with weak phospholipidosis-inducing capacity and extensive in vivo metabolism, namely, imipramine, chlorpromazine and promazine, also bound strongly to lamellar bodies with hydrophilic as well as hydrophobic interactions. On the other hand, chloroquine, which is known to induce phospholipidosis and to inhibit phospholipases, did not bind to lamellar bodies. Two major conclusions could be drawn from this study: one is that the drug interactions with isolated lamellar bodies could be studied using membrane fluorescence probes, 1,6-diphenyl-1,3,5-hexatriene and 1-anilino-8-naphthalene sulfonate; second is that the amphiphilic drugs bind to lamellar bodies, as reported for phospholipid vesicles, and the binding of drugs to lamellar bodies could be correlated with their phospholipidosis-inducing capacity only if
DOI: 10.1016/0005-2760(89)90078-7
PubMed: 2758025
Links to Exploration step
pubmed:2758025Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Fluorescence studies on binding of amphiphilic drugs to isolated lamellar bodies: relevance to phospholipidosis.</title>
<author><name sortKey="Joshi, U M" sort="Joshi, U M" uniqKey="Joshi U" first="U M" last="Joshi">U M Joshi</name>
<affiliation><nlm:affiliation>Department of Pharmacology, University of Mississippi Medical Center, Jackson 39216.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Rao, P" sort="Rao, P" uniqKey="Rao P" first="P" last="Rao">P. Rao</name>
</author>
<author><name sortKey="Kodavanti, S" sort="Kodavanti, S" uniqKey="Kodavanti S" first="S" last="Kodavanti">S. Kodavanti</name>
</author>
<author><name sortKey="Lockard, V G" sort="Lockard, V G" uniqKey="Lockard V" first="V G" last="Lockard">V G Lockard</name>
</author>
<author><name sortKey="Mehendale, H M" sort="Mehendale, H M" uniqKey="Mehendale H" first="H M" last="Mehendale">H M Mehendale</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="1989">1989</date>
<idno type="RBID">pubmed:2758025</idno>
<idno type="pmid">2758025</idno>
<idno type="doi">10.1016/0005-2760(89)90078-7</idno>
<idno type="wicri:Area/PubMed/Corpus">000562</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000562</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Fluorescence studies on binding of amphiphilic drugs to isolated lamellar bodies: relevance to phospholipidosis.</title>
<author><name sortKey="Joshi, U M" sort="Joshi, U M" uniqKey="Joshi U" first="U M" last="Joshi">U M Joshi</name>
<affiliation><nlm:affiliation>Department of Pharmacology, University of Mississippi Medical Center, Jackson 39216.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Rao, P" sort="Rao, P" uniqKey="Rao P" first="P" last="Rao">P. Rao</name>
</author>
<author><name sortKey="Kodavanti, S" sort="Kodavanti, S" uniqKey="Kodavanti S" first="S" last="Kodavanti">S. Kodavanti</name>
</author>
<author><name sortKey="Lockard, V G" sort="Lockard, V G" uniqKey="Lockard V" first="V G" last="Lockard">V G Lockard</name>
</author>
<author><name sortKey="Mehendale, H M" sort="Mehendale, H M" uniqKey="Mehendale H" first="H M" last="Mehendale">H M Mehendale</name>
</author>
</analytic>
<series><title level="j">Biochimica et biophysica acta</title>
<idno type="ISSN">0006-3002</idno>
<imprint><date when="1989" type="published">1989</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amines (metabolism)</term>
<term>Anilino Naphthalenesulfonates</term>
<term>Animals</term>
<term>Diphenylhexatriene</term>
<term>In Vitro Techniques</term>
<term>Lung (metabolism)</term>
<term>Lung (ultrastructure)</term>
<term>Male</term>
<term>Microscopy, Electron</term>
<term>Organelles (metabolism)</term>
<term>Phospholipids</term>
<term>Rats</term>
<term>Rats, Inbred Strains</term>
<term>Spectrometry, Fluorescence</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amines</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Anilino Naphthalenesulfonates</term>
<term>Diphenylhexatriene</term>
<term>Phospholipids</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Lung</term>
<term>Organelles</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Lung</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>In Vitro Techniques</term>
<term>Male</term>
<term>Microscopy, Electron</term>
<term>Rats</term>
<term>Rats, Inbred Strains</term>
<term>Spectrometry, Fluorescence</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Lysosomal phospholipid storage disorder in lung tissue was observed during chronic treatment with amphiphilic amine drugs. The prevailing and widely accepted mechanism of phospholipidosis is that amphiphilic drugs bind to phospholipids and make the phospholipids unsuitable substrates for the action of phospholipases. We investigated hydrophobic and hydrophilic binding of fifteen drugs to the phospholipid storage organelle, lung lamellar bodies, isolated from male Sprague-Dawley rats. Hydrophobic interactions were studied using 1,6-diphenyl-1,3,5-hexatriene as a fluorescent probe and hydrophilic binding was studied using 1-anilino-8-naphthalene sulfonate as a fluorescent probe. The binding parameters were calculated using Scatchard equations. Of the fifteen drugs used, nine drugs bound to the hydrophobic moiety of lamellar bodies. The order of binding capacities was promethazine greater than chloramphenicol greater than amiodarone = desethylamiodarone greater than promazine greater than chlorpromazine greater than trimipramine greater than propranolol greater than imipramine much greater than chlorphentermine, phentermine, chloroquine, chlorimipramine, cyclizine and chlorcyclizine. Two binding affinities were calculated for all the bound drugs. Binding affinities to hydrophilic sites of lamellar bodies were calculated in terms of emission coefficients for 1-anilino-8-naphthalene sulfonate in the presence of drugs. Hydrophilic binding was in the order chlorpromazine greater than chlorimipramine greater than promazine greater than trimipramine greater than imipramine greater than chlorcyclizine greater than propranolol greater than promethazine greater than chlorphentermine greater than cyclizine greater than phentermine greater than chloroquine much greater than chloramphenicol, amiodarone and desethylamiodarone. The binding affinities of chlorinated analogs were stronger to hydrophilic sites when compared to the parent compound. Amiodarone, which is known to induce pulmonary phospholipidosis and its major non-polar metabolite, desethylamiodarone, bound strongly to lamellar bodies. These two drugs also inhibit phospholipases in vitro. The drugs with weak phospholipidosis-inducing capacity and extensive in vivo metabolism, namely, imipramine, chlorpromazine and promazine, also bound strongly to lamellar bodies with hydrophilic as well as hydrophobic interactions. On the other hand, chloroquine, which is known to induce phospholipidosis and to inhibit phospholipases, did not bind to lamellar bodies. Two major conclusions could be drawn from this study: one is that the drug interactions with isolated lamellar bodies could be studied using membrane fluorescence probes, 1,6-diphenyl-1,3,5-hexatriene and 1-anilino-8-naphthalene sulfonate; second is that the amphiphilic drugs bind to lamellar bodies, as reported for phospholipid vesicles, and the binding of drugs to lamellar bodies could be correlated with their phospholipidosis-inducing capacity only if</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">2758025</PMID>
<DateCompleted><Year>1989</Year>
<Month>09</Month>
<Day>21</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>06</Month>
<Day>09</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-3002</ISSN>
<JournalIssue CitedMedium="Print"><Volume>1004</Volume>
<Issue>3</Issue>
<PubDate><Year>1989</Year>
<Month>Aug</Month>
<Day>22</Day>
</PubDate>
</JournalIssue>
<Title>Biochimica et biophysica acta</Title>
<ISOAbbreviation>Biochim. Biophys. Acta</ISOAbbreviation>
</Journal>
<ArticleTitle>Fluorescence studies on binding of amphiphilic drugs to isolated lamellar bodies: relevance to phospholipidosis.</ArticleTitle>
<Pagination><MedlinePgn>309-20</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Lysosomal phospholipid storage disorder in lung tissue was observed during chronic treatment with amphiphilic amine drugs. The prevailing and widely accepted mechanism of phospholipidosis is that amphiphilic drugs bind to phospholipids and make the phospholipids unsuitable substrates for the action of phospholipases. We investigated hydrophobic and hydrophilic binding of fifteen drugs to the phospholipid storage organelle, lung lamellar bodies, isolated from male Sprague-Dawley rats. Hydrophobic interactions were studied using 1,6-diphenyl-1,3,5-hexatriene as a fluorescent probe and hydrophilic binding was studied using 1-anilino-8-naphthalene sulfonate as a fluorescent probe. The binding parameters were calculated using Scatchard equations. Of the fifteen drugs used, nine drugs bound to the hydrophobic moiety of lamellar bodies. The order of binding capacities was promethazine greater than chloramphenicol greater than amiodarone = desethylamiodarone greater than promazine greater than chlorpromazine greater than trimipramine greater than propranolol greater than imipramine much greater than chlorphentermine, phentermine, chloroquine, chlorimipramine, cyclizine and chlorcyclizine. Two binding affinities were calculated for all the bound drugs. Binding affinities to hydrophilic sites of lamellar bodies were calculated in terms of emission coefficients for 1-anilino-8-naphthalene sulfonate in the presence of drugs. Hydrophilic binding was in the order chlorpromazine greater than chlorimipramine greater than promazine greater than trimipramine greater than imipramine greater than chlorcyclizine greater than propranolol greater than promethazine greater than chlorphentermine greater than cyclizine greater than phentermine greater than chloroquine much greater than chloramphenicol, amiodarone and desethylamiodarone. The binding affinities of chlorinated analogs were stronger to hydrophilic sites when compared to the parent compound. Amiodarone, which is known to induce pulmonary phospholipidosis and its major non-polar metabolite, desethylamiodarone, bound strongly to lamellar bodies. These two drugs also inhibit phospholipases in vitro. The drugs with weak phospholipidosis-inducing capacity and extensive in vivo metabolism, namely, imipramine, chlorpromazine and promazine, also bound strongly to lamellar bodies with hydrophilic as well as hydrophobic interactions. On the other hand, chloroquine, which is known to induce phospholipidosis and to inhibit phospholipases, did not bind to lamellar bodies. Two major conclusions could be drawn from this study: one is that the drug interactions with isolated lamellar bodies could be studied using membrane fluorescence probes, 1,6-diphenyl-1,3,5-hexatriene and 1-anilino-8-naphthalene sulfonate; second is that the amphiphilic drugs bind to lamellar bodies, as reported for phospholipid vesicles, and the binding of drugs to lamellar bodies could be correlated with their phospholipidosis-inducing capacity only if</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Joshi</LastName>
<ForeName>U M</ForeName>
<Initials>UM</Initials>
<AffiliationInfo><Affiliation>Department of Pharmacology, University of Mississippi Medical Center, Jackson 39216.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Rao</LastName>
<ForeName>P</ForeName>
<Initials>P</Initials>
</Author>
<Author ValidYN="Y"><LastName>Kodavanti</LastName>
<ForeName>S</ForeName>
<Initials>S</Initials>
</Author>
<Author ValidYN="Y"><LastName>Lockard</LastName>
<ForeName>V G</ForeName>
<Initials>VG</Initials>
</Author>
<Author ValidYN="Y"><LastName>Mehendale</LastName>
<ForeName>H M</ForeName>
<Initials>HM</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>HL-20622</GrantID>
<Acronym>HL</Acronym>
<Agency>NHLBI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
<PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType>
</PublicationTypeList>
</Article>
<MedlineJournalInfo><Country>Netherlands</Country>
<MedlineTA>Biochim Biophys Acta</MedlineTA>
<NlmUniqueID>0217513</NlmUniqueID>
<ISSNLinking>0006-3002</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000588">Amines</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000817">Anilino Naphthalenesulfonates</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010743">Phospholipids</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>1720-32-7</RegistryNumber>
<NameOfSubstance UI="D004161">Diphenylhexatriene</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000588" MajorTopicYN="N">Amines</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000817" MajorTopicYN="N">Anilino Naphthalenesulfonates</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004161" MajorTopicYN="N">Diphenylhexatriene</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D066298" MajorTopicYN="N">In Vitro Techniques</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008168" MajorTopicYN="N">Lung</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008854" MajorTopicYN="N">Microscopy, Electron</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015388" MajorTopicYN="N">Organelles</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010743" MajorTopicYN="N">Phospholipids</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011919" MajorTopicYN="N">Rats, Inbred Strains</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013050" MajorTopicYN="N">Spectrometry, Fluorescence</DescriptorName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1989</Year>
<Month>8</Month>
<Day>22</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>1989</Year>
<Month>8</Month>
<Day>22</Day>
<Hour>0</Hour>
<Minute>1</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>1989</Year>
<Month>8</Month>
<Day>22</Day>
<Hour>0</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">2758025</ArticleId>
<ArticleId IdType="pii">0005-2760(89)90078-7</ArticleId>
<ArticleId IdType="doi">10.1016/0005-2760(89)90078-7</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/ChloroquineV1/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000562 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 000562 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= ChloroquineV1 |flux= PubMed |étape= Corpus |type= RBID |clé= pubmed:2758025 |texte= Fluorescence studies on binding of amphiphilic drugs to isolated lamellar bodies: relevance to phospholipidosis. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:2758025" \ | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \ | NlmPubMed2Wicri -a ChloroquineV1
![]() | This area was generated with Dilib version V0.6.33. | ![]() |