Tritrichomonas foetus:Iron Acquisition from Lactoferrin and Transferrin
Tachezy, J., Kulda, J., Bahnı́ková, I., Suchan, P., Rázga, J., and Schrével, J. 1996.Tritrichomonas foetus:Iron acquisition from lactoferrin and transferrin.Experimental Parasitology83,216–228. Acquisition of iron from lactoferrin and transferrin by a parasitic protozoonTritrichomonas foetushas been...
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description | Tachezy, J., Kulda, J., Bahnı́ková, I., Suchan, P., Rázga, J., and Schrével, J. 1996.Tritrichomonas foetus:Iron acquisition from lactoferrin and transferrin.Experimental Parasitology83,216–228. Acquisition of iron from lactoferrin and transferrin by a parasitic protozoonTritrichomonas foetushas been studiedin vitro.Specific, time-dependent, and saturable binding of iodinated ligands to the outer membrane ofT. foetusat 4°C was demonstrated for125I-labeled lactoferrin only. About 1.7 × 105binding sites of a single class withKd≅ 3.6 μMwas estimated by means of Scatchard analysis. Internalization of the bound lactoferrin was observed at 37°C. The cell-associated radioactivity after 30 min incubation of the parasite with125I-lactoferrin at 37°C was about 3.5-fold higher than the amount bound at 4°C. The majority of internalized125I-lactoferrin was released within 15 min of cell reincubation at 37°C in the presence of a 100-fold excess of nonlabeled lactoferrin. Released lactoferrin displayed unchanged mobility on autoradiography. In contrast to lactoferrin, binding of125I-transferrin was nonspecific and did not display saturable kinetics. The growth ofT. foetusin iron-restricted media was stimulated by both lactoferrin and transferrin. The ability of the cells to remove and accumulate iron from both proteins was therefore examined using59Fe-saturated lactoferrin and transferrin. It was found that trichomonads acquired a comparable amount of iron from both lactoferrin and transferrin during 60 min incubation at 37°C (495 and 577 pmole Fe/mg of protein, respectively). The pH of the assay medium (PBS) decreased from pH 7.4 to 5.6 after incubation with trichomonads. At this pH, marked release of iron from transferrin (up to 47%) but not from lactoferrin (4%) was determined in cell-free media. These results indicate thatT. foetusis able to utilize both lactoferrin and transferrin to cover its iron requirements. However, mechanisms of iron acquisition from these host proteins appear to be different. Specific binding and internalization of lactoferrin suggests the possible involvement of receptor-mediated endocytosis in the acquisition of lactoferrin-bound iron, while retrieval of iron from transferrin may depend on the extracellular release of iron from this ligand. |
doi_str_mv | 10.1006/expr.1996.0068 |
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Acquisition of iron from lactoferrin and transferrin by a parasitic protozoonTritrichomonas foetushas been studiedin vitro.Specific, time-dependent, and saturable binding of iodinated ligands to the outer membrane ofT. foetusat 4°C was demonstrated for125I-labeled lactoferrin only. About 1.7 × 105binding sites of a single class withKd≅ 3.6 μMwas estimated by means of Scatchard analysis. Internalization of the bound lactoferrin was observed at 37°C. The cell-associated radioactivity after 30 min incubation of the parasite with125I-lactoferrin at 37°C was about 3.5-fold higher than the amount bound at 4°C. The majority of internalized125I-lactoferrin was released within 15 min of cell reincubation at 37°C in the presence of a 100-fold excess of nonlabeled lactoferrin. Released lactoferrin displayed unchanged mobility on autoradiography. In contrast to lactoferrin, binding of125I-transferrin was nonspecific and did not display saturable kinetics. The growth ofT. foetusin iron-restricted media was stimulated by both lactoferrin and transferrin. The ability of the cells to remove and accumulate iron from both proteins was therefore examined using59Fe-saturated lactoferrin and transferrin. It was found that trichomonads acquired a comparable amount of iron from both lactoferrin and transferrin during 60 min incubation at 37°C (495 and 577 pmole Fe/mg of protein, respectively). The pH of the assay medium (PBS) decreased from pH 7.4 to 5.6 after incubation with trichomonads. At this pH, marked release of iron from transferrin (up to 47%) but not from lactoferrin (4%) was determined in cell-free media. These results indicate thatT. foetusis able to utilize both lactoferrin and transferrin to cover its iron requirements. However, mechanisms of iron acquisition from these host proteins appear to be different. Specific binding and internalization of lactoferrin suggests the possible involvement of receptor-mediated endocytosis in the acquisition of lactoferrin-bound iron, while retrieval of iron from transferrin may depend on the extracellular release of iron from this ligand.</description><identifier>ISSN: 0014-4894</identifier><identifier>EISSN: 1090-2449</identifier><identifier>DOI: 10.1006/expr.1996.0068</identifier><identifier>PMID: 8682190</identifier><identifier>CODEN: EXPAAA</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>2,2'-Dipyridyl - pharmacology ; ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; Animals ; BIOAVAILABILITY ; Biochemistry. Physiology. Immunology. Molecular biology ; BIODISPONIBILIDAD ; BIODISPONIBILITE ; Biological and medical sciences ; Cattle ; CRECIMIENTO ; CROISSANCE ; EDTA, ethylendiaminetetracetic acid ; endocytosis ; ENZYMIC ACTIVITY ; EXPERIMENTACION IN VITRO ; EXPERIMENTATION IN VITRO ; FER ; Ferric Compounds - pharmacology ; Fundamental and applied biological sciences. Psychology ; GROWTH ; HIERRO ; Hydrogen-Ion Concentration ; HYDROGENASE ; hydrogenase (EC 1.18.3.1) ; Hydrogenase - metabolism ; IN VITRO EXPERIMENTATION ; IRON ; Iron - metabolism ; Iron Chelating Agents - pharmacology ; Ketone Oxidoreductases - metabolism ; LACTOFERRIN ; Lactoferrin - metabolism ; lactoferrin and transferrin-dependent iron uptake ; lactoferrin-specific receptors ; LACTOFERRINAS ; LACTOFERRINE ; Ligands ; Male ; Mice ; MODE OF ACTION ; Nitrilotriacetic Acid - analogs & derivatives ; Nitrilotriacetic Acid - pharmacology ; OXIDOREDUCTASES ; OXIDORREDUCTASAS ; OXYDOREDUCTASE ; PBS, phosphate-buffered saline ; PFOR, pyruvate:ferredoxin oxidoreductase (EC 1.2.7.1) ; Protozoa ; Pyruvate Synthase ; Receptors, Cell Surface - metabolism ; Receptors, Transferrin - metabolism ; SDS–PAGE, sodium dodecyl sulfate–polyacrylamide gel electrophoresis ; Temperature ; Transferrin - metabolism ; TRANSFERRINAS ; TRANSFERRINE ; TRANSFERRINS ; TRITRICHOMONAS FOETUS ; Tritrichomonas foetus - drug effects ; Tritrichomonas foetus - growth & development ; Tritrichomonas foetus - metabolism ; TYM, trypticase–yeast extract–maltose ; UPTAKE</subject><ispartof>Experimental parasitology, 1996-07, Vol.83 (2), p.216-228</ispartof><rights>1996 Academic Press</rights><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c447t-1c41a639500dc6af679d3b99a1c2f02cb1ae2c04da871dbc0862c21074d56e373</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014489496900685$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3195989$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8682190$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tachezy, Jan</creatorcontrib><creatorcontrib>Kulda, Jaroslav</creatorcontrib><creatorcontrib>Bahnı́ková, Ivana</creatorcontrib><creatorcontrib>Suchan, Pavel</creatorcontrib><creatorcontrib>Rázga, Jakub</creatorcontrib><creatorcontrib>Schrével, Joseph</creatorcontrib><title>Tritrichomonas foetus:Iron Acquisition from Lactoferrin and Transferrin</title><title>Experimental parasitology</title><addtitle>Exp Parasitol</addtitle><description>Tachezy, J., Kulda, J., Bahnı́ková, I., Suchan, P., Rázga, J., and Schrével, J. 1996.Tritrichomonas foetus:Iron acquisition from lactoferrin and transferrin.Experimental Parasitology83,216–228. Acquisition of iron from lactoferrin and transferrin by a parasitic protozoonTritrichomonas foetushas been studiedin vitro.Specific, time-dependent, and saturable binding of iodinated ligands to the outer membrane ofT. foetusat 4°C was demonstrated for125I-labeled lactoferrin only. About 1.7 × 105binding sites of a single class withKd≅ 3.6 μMwas estimated by means of Scatchard analysis. Internalization of the bound lactoferrin was observed at 37°C. The cell-associated radioactivity after 30 min incubation of the parasite with125I-lactoferrin at 37°C was about 3.5-fold higher than the amount bound at 4°C. The majority of internalized125I-lactoferrin was released within 15 min of cell reincubation at 37°C in the presence of a 100-fold excess of nonlabeled lactoferrin. Released lactoferrin displayed unchanged mobility on autoradiography. In contrast to lactoferrin, binding of125I-transferrin was nonspecific and did not display saturable kinetics. The growth ofT. foetusin iron-restricted media was stimulated by both lactoferrin and transferrin. The ability of the cells to remove and accumulate iron from both proteins was therefore examined using59Fe-saturated lactoferrin and transferrin. It was found that trichomonads acquired a comparable amount of iron from both lactoferrin and transferrin during 60 min incubation at 37°C (495 and 577 pmole Fe/mg of protein, respectively). The pH of the assay medium (PBS) decreased from pH 7.4 to 5.6 after incubation with trichomonads. At this pH, marked release of iron from transferrin (up to 47%) but not from lactoferrin (4%) was determined in cell-free media. These results indicate thatT. foetusis able to utilize both lactoferrin and transferrin to cover its iron requirements. However, mechanisms of iron acquisition from these host proteins appear to be different. Specific binding and internalization of lactoferrin suggests the possible involvement of receptor-mediated endocytosis in the acquisition of lactoferrin-bound iron, while retrieval of iron from transferrin may depend on the extracellular release of iron from this ligand.</description><subject>2,2'-Dipyridyl - pharmacology</subject><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>Animals</subject><subject>BIOAVAILABILITY</subject><subject>Biochemistry. Physiology. Immunology. Molecular biology</subject><subject>BIODISPONIBILIDAD</subject><subject>BIODISPONIBILITE</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>CRECIMIENTO</subject><subject>CROISSANCE</subject><subject>EDTA, ethylendiaminetetracetic acid</subject><subject>endocytosis</subject><subject>ENZYMIC ACTIVITY</subject><subject>EXPERIMENTACION IN VITRO</subject><subject>EXPERIMENTATION IN VITRO</subject><subject>FER</subject><subject>Ferric Compounds - pharmacology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GROWTH</subject><subject>HIERRO</subject><subject>Hydrogen-Ion Concentration</subject><subject>HYDROGENASE</subject><subject>hydrogenase (EC 1.18.3.1)</subject><subject>Hydrogenase - metabolism</subject><subject>IN VITRO EXPERIMENTATION</subject><subject>IRON</subject><subject>Iron - metabolism</subject><subject>Iron Chelating Agents - pharmacology</subject><subject>Ketone Oxidoreductases - metabolism</subject><subject>LACTOFERRIN</subject><subject>Lactoferrin - metabolism</subject><subject>lactoferrin and transferrin-dependent iron uptake</subject><subject>lactoferrin-specific receptors</subject><subject>LACTOFERRINAS</subject><subject>LACTOFERRINE</subject><subject>Ligands</subject><subject>Male</subject><subject>Mice</subject><subject>MODE OF ACTION</subject><subject>Nitrilotriacetic Acid - analogs & derivatives</subject><subject>Nitrilotriacetic Acid - pharmacology</subject><subject>OXIDOREDUCTASES</subject><subject>OXIDORREDUCTASAS</subject><subject>OXYDOREDUCTASE</subject><subject>PBS, phosphate-buffered saline</subject><subject>PFOR, pyruvate:ferredoxin oxidoreductase (EC 1.2.7.1)</subject><subject>Protozoa</subject><subject>Pyruvate Synthase</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, Transferrin - metabolism</subject><subject>SDS–PAGE, sodium dodecyl sulfate–polyacrylamide gel electrophoresis</subject><subject>Temperature</subject><subject>Transferrin - metabolism</subject><subject>TRANSFERRINAS</subject><subject>TRANSFERRINE</subject><subject>TRANSFERRINS</subject><subject>TRITRICHOMONAS FOETUS</subject><subject>Tritrichomonas foetus - drug effects</subject><subject>Tritrichomonas foetus - growth & development</subject><subject>Tritrichomonas foetus - metabolism</subject><subject>TYM, trypticase–yeast extract–maltose</subject><subject>UPTAKE</subject><issn>0014-4894</issn><issn>1090-2449</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1v1DAQhq0KVLYfVw5ISDmg3rLMOF7H5lZVUCqtxIHt2fKOnWK0ibd2UsG_x1FWvXHyjN7HY8_D2HuENQLIz_7PMa1Ra7kunTpjKwQNNRdCv2ErABS1UFq8Yxc5_wYAhVycs3MlFUcNK3a_S2FMgX7FPg42V13045S_PKQ4VLf0PIUcxlDqLsW-2loaY-dTCkNlB1ftkh3y0l-xt509ZH99Oi_Z47evu7vv9fbH_cPd7bYmIdqxRhJoZaM3AI6k7WSrXbPX2iLxDjjt0XpOIJxVLbo9gZKcOEIr3Eb6pm0u2c0y95ji8-TzaPqQyR8OdvBxygalaOUGeQHXC0gp5px8Z44p9Db9NQhmNmdmc2Y2Z2Zz5cLH0-Rp33v3ip9UlfzTKbeZ7KEru1PIr1iDeqOVLtiHBetsNPYpFeTxp24BUcxvqCX0RdFL8MlkCn4g70LyNBoXw_--9w_uCZKT</recordid><startdate>19960701</startdate><enddate>19960701</enddate><creator>Tachezy, Jan</creator><creator>Kulda, Jaroslav</creator><creator>Bahnı́ková, Ivana</creator><creator>Suchan, Pavel</creator><creator>Rázga, Jakub</creator><creator>Schrével, Joseph</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>FBQ</scope><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>M7N</scope></search><sort><creationdate>19960701</creationdate><title>Tritrichomonas foetus:Iron Acquisition from Lactoferrin and Transferrin</title><author>Tachezy, Jan ; Kulda, Jaroslav ; Bahnı́ková, Ivana ; Suchan, Pavel ; Rázga, Jakub ; Schrével, Joseph</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c447t-1c41a639500dc6af679d3b99a1c2f02cb1ae2c04da871dbc0862c21074d56e373</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>2,2'-Dipyridyl - pharmacology</topic><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>Animals</topic><topic>BIOAVAILABILITY</topic><topic>Biochemistry. Physiology. Immunology. Molecular biology</topic><topic>BIODISPONIBILIDAD</topic><topic>BIODISPONIBILITE</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>CRECIMIENTO</topic><topic>CROISSANCE</topic><topic>EDTA, ethylendiaminetetracetic acid</topic><topic>endocytosis</topic><topic>ENZYMIC ACTIVITY</topic><topic>EXPERIMENTACION IN VITRO</topic><topic>EXPERIMENTATION IN VITRO</topic><topic>FER</topic><topic>Ferric Compounds - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GROWTH</topic><topic>HIERRO</topic><topic>Hydrogen-Ion Concentration</topic><topic>HYDROGENASE</topic><topic>hydrogenase (EC 1.18.3.1)</topic><topic>Hydrogenase - metabolism</topic><topic>IN VITRO EXPERIMENTATION</topic><topic>IRON</topic><topic>Iron - metabolism</topic><topic>Iron Chelating Agents - pharmacology</topic><topic>Ketone Oxidoreductases - metabolism</topic><topic>LACTOFERRIN</topic><topic>Lactoferrin - metabolism</topic><topic>lactoferrin and transferrin-dependent iron uptake</topic><topic>lactoferrin-specific receptors</topic><topic>LACTOFERRINAS</topic><topic>LACTOFERRINE</topic><topic>Ligands</topic><topic>Male</topic><topic>Mice</topic><topic>MODE OF ACTION</topic><topic>Nitrilotriacetic Acid - analogs & derivatives</topic><topic>Nitrilotriacetic Acid - pharmacology</topic><topic>OXIDOREDUCTASES</topic><topic>OXIDORREDUCTASAS</topic><topic>OXYDOREDUCTASE</topic><topic>PBS, phosphate-buffered saline</topic><topic>PFOR, pyruvate:ferredoxin oxidoreductase (EC 1.2.7.1)</topic><topic>Protozoa</topic><topic>Pyruvate Synthase</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, Transferrin - metabolism</topic><topic>SDS–PAGE, sodium dodecyl sulfate–polyacrylamide gel electrophoresis</topic><topic>Temperature</topic><topic>Transferrin - metabolism</topic><topic>TRANSFERRINAS</topic><topic>TRANSFERRINE</topic><topic>TRANSFERRINS</topic><topic>TRITRICHOMONAS FOETUS</topic><topic>Tritrichomonas foetus - drug effects</topic><topic>Tritrichomonas foetus - growth & development</topic><topic>Tritrichomonas foetus - metabolism</topic><topic>TYM, trypticase–yeast extract–maltose</topic><topic>UPTAKE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tachezy, Jan</creatorcontrib><creatorcontrib>Kulda, Jaroslav</creatorcontrib><creatorcontrib>Bahnı́ková, Ivana</creatorcontrib><creatorcontrib>Suchan, Pavel</creatorcontrib><creatorcontrib>Rázga, Jakub</creatorcontrib><creatorcontrib>Schrével, Joseph</creatorcontrib><collection>AGRIS</collection><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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>Experimental parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tachezy, Jan</au><au>Kulda, Jaroslav</au><au>Bahnı́ková, Ivana</au><au>Suchan, Pavel</au><au>Rázga, Jakub</au><au>Schrével, Joseph</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tritrichomonas foetus:Iron Acquisition from Lactoferrin and Transferrin</atitle><jtitle>Experimental parasitology</jtitle><addtitle>Exp Parasitol</addtitle><date>1996-07-01</date><risdate>1996</risdate><volume>83</volume><issue>2</issue><spage>216</spage><epage>228</epage><pages>216-228</pages><issn>0014-4894</issn><eissn>1090-2449</eissn><coden>EXPAAA</coden><abstract>Tachezy, J., Kulda, J., Bahnı́ková, I., Suchan, P., Rázga, J., and Schrével, J. 1996.Tritrichomonas foetus:Iron acquisition from lactoferrin and transferrin.Experimental Parasitology83,216–228. Acquisition of iron from lactoferrin and transferrin by a parasitic protozoonTritrichomonas foetushas been studiedin vitro.Specific, time-dependent, and saturable binding of iodinated ligands to the outer membrane ofT. foetusat 4°C was demonstrated for125I-labeled lactoferrin only. About 1.7 × 105binding sites of a single class withKd≅ 3.6 μMwas estimated by means of Scatchard analysis. Internalization of the bound lactoferrin was observed at 37°C. The cell-associated radioactivity after 30 min incubation of the parasite with125I-lactoferrin at 37°C was about 3.5-fold higher than the amount bound at 4°C. The majority of internalized125I-lactoferrin was released within 15 min of cell reincubation at 37°C in the presence of a 100-fold excess of nonlabeled lactoferrin. Released lactoferrin displayed unchanged mobility on autoradiography. In contrast to lactoferrin, binding of125I-transferrin was nonspecific and did not display saturable kinetics. The growth ofT. foetusin iron-restricted media was stimulated by both lactoferrin and transferrin. The ability of the cells to remove and accumulate iron from both proteins was therefore examined using59Fe-saturated lactoferrin and transferrin. It was found that trichomonads acquired a comparable amount of iron from both lactoferrin and transferrin during 60 min incubation at 37°C (495 and 577 pmole Fe/mg of protein, respectively). The pH of the assay medium (PBS) decreased from pH 7.4 to 5.6 after incubation with trichomonads. At this pH, marked release of iron from transferrin (up to 47%) but not from lactoferrin (4%) was determined in cell-free media. These results indicate thatT. foetusis able to utilize both lactoferrin and transferrin to cover its iron requirements. However, mechanisms of iron acquisition from these host proteins appear to be different. Specific binding and internalization of lactoferrin suggests the possible involvement of receptor-mediated endocytosis in the acquisition of lactoferrin-bound iron, while retrieval of iron from transferrin may depend on the extracellular release of iron from this ligand.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>8682190</pmid><doi>10.1006/expr.1996.0068</doi><tpages>13</tpages></addata></record> |
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subjects | 2,2'-Dipyridyl - pharmacology ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Animals BIOAVAILABILITY Biochemistry. Physiology. Immunology. Molecular biology BIODISPONIBILIDAD BIODISPONIBILITE Biological and medical sciences Cattle CRECIMIENTO CROISSANCE EDTA, ethylendiaminetetracetic acid endocytosis ENZYMIC ACTIVITY EXPERIMENTACION IN VITRO EXPERIMENTATION IN VITRO FER Ferric Compounds - pharmacology Fundamental and applied biological sciences. Psychology GROWTH HIERRO Hydrogen-Ion Concentration HYDROGENASE hydrogenase (EC 1.18.3.1) Hydrogenase - metabolism IN VITRO EXPERIMENTATION IRON Iron - metabolism Iron Chelating Agents - pharmacology Ketone Oxidoreductases - metabolism LACTOFERRIN Lactoferrin - metabolism lactoferrin and transferrin-dependent iron uptake lactoferrin-specific receptors LACTOFERRINAS LACTOFERRINE Ligands Male Mice MODE OF ACTION Nitrilotriacetic Acid - analogs & derivatives Nitrilotriacetic Acid - pharmacology OXIDOREDUCTASES OXIDORREDUCTASAS OXYDOREDUCTASE PBS, phosphate-buffered saline PFOR, pyruvate:ferredoxin oxidoreductase (EC 1.2.7.1) Protozoa Pyruvate Synthase Receptors, Cell Surface - metabolism Receptors, Transferrin - metabolism SDS–PAGE, sodium dodecyl sulfate–polyacrylamide gel electrophoresis Temperature Transferrin - metabolism TRANSFERRINAS TRANSFERRINE TRANSFERRINS TRITRICHOMONAS FOETUS Tritrichomonas foetus - drug effects Tritrichomonas foetus - growth & development Tritrichomonas foetus - metabolism TYM, trypticase–yeast extract–maltose UPTAKE |
title | Tritrichomonas foetus:Iron Acquisition from Lactoferrin and Transferrin |
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