A novel iron uptake mechanism mediated by GPI‐anchored human p97
The established process for iron uptake into mammalian cells involves transferrin and its receptor. Here, the role of the glycosyl‐phosphatidylinositol (GPI)‐linked transferrin homologue, melanotransferrin or p97, was studied using CHO cell lines defective in the transferrin receptor (TR) and transf...
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| Veröffentlicht in: | The EMBO journal 1995-09, Vol.14 (17), p.4178-4186 |
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| creator | Kennard, M. L. Richardson, D. R. Gabathuler, R. Ponka, P. Jefferies, W. A. |
| description | The established process for iron uptake into mammalian cells involves transferrin and its receptor. Here, the role of the glycosyl‐phosphatidylinositol (GPI)‐linked transferrin homologue, melanotransferrin or p97, was studied using CHO cell lines defective in the transferrin receptor (TR) and transfected with human TR and/or human p97. The presence of p97 doubled the iron uptake, which could be explained by the binding of one atom of iron to one molecule of p97. The internalization of iron was shown to be temperature sensitive and saturated at a media iron concentration of 2.5 micrograms/ml with a Vmax of 0.1 pmol Fe/10(6) cell/min and a Km of 2.58 microM for p97. Treatment of the cells with either phosphatidylinositol‐phospholipase C or monoclonal antibodies against p97 resulted in over a 50% reduction and a 47% increase in the iron uptake respectively. These data identify p97 as a unique cell surface GPI‐anchored, iron binding protein involved in the transferrin‐independent uptake of iron in mammals. |
| doi_str_mv | 10.1002/j.1460-2075.1995.tb00091.x |
| format | Article |
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L. ; Richardson, D. R. ; Gabathuler, R. ; Ponka, P. ; Jefferies, W. A.</creator><creatorcontrib>Kennard, M. L. ; Richardson, D. R. ; Gabathuler, R. ; Ponka, P. ; Jefferies, W. A.</creatorcontrib><description>The established process for iron uptake into mammalian cells involves transferrin and its receptor. Here, the role of the glycosyl‐phosphatidylinositol (GPI)‐linked transferrin homologue, melanotransferrin or p97, was studied using CHO cell lines defective in the transferrin receptor (TR) and transfected with human TR and/or human p97. The presence of p97 doubled the iron uptake, which could be explained by the binding of one atom of iron to one molecule of p97. The internalization of iron was shown to be temperature sensitive and saturated at a media iron concentration of 2.5 micrograms/ml with a Vmax of 0.1 pmol Fe/10(6) cell/min and a Km of 2.58 microM for p97. Treatment of the cells with either phosphatidylinositol‐phospholipase C or monoclonal antibodies against p97 resulted in over a 50% reduction and a 47% increase in the iron uptake respectively. 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The internalization of iron was shown to be temperature sensitive and saturated at a media iron concentration of 2.5 micrograms/ml with a Vmax of 0.1 pmol Fe/10(6) cell/min and a Km of 2.58 microM for p97. Treatment of the cells with either phosphatidylinositol‐phospholipase C or monoclonal antibodies against p97 resulted in over a 50% reduction and a 47% increase in the iron uptake respectively. These data identify p97 as a unique cell surface GPI‐anchored, iron binding protein involved in the transferrin‐independent uptake of iron in mammals.</description><subject>Animals</subject><subject>Antigens, Neoplasm</subject><subject>Antigens, Surface - metabolism</subject><subject>Biological Transport</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>Gene Expression</subject><subject>Glycosylphosphatidylinositols - metabolism</subject><subject>Humans</subject><subject>Iron - metabolism</subject><subject>Kinetics</subject><subject>Mammals</subject><subject>Melanoma-Specific Antigens</subject><subject>Neoplasm Proteins - biosynthesis</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Phosphatidylinositol Diacylglycerol-Lyase</subject><subject>Phosphoric Diester Hydrolases - metabolism</subject><subject>Phosphoric Diester Hydrolases - pharmacology</subject><subject>Pronase - pharmacology</subject><subject>Receptors, Transferrin - biosynthesis</subject><subject>Receptors, Transferrin - metabolism</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - metabolism</subject><subject>Transfection</subject><subject>Transferrin - biosynthesis</subject><subject>Transferrin - metabolism</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkUtOwzAURS0EKuWzBKSIAbMEO_UnRmLQVlBARTCAseU4LzQlnxIn0M5YAmtkJbi0qmCEGPnZ996nax2EjgkOCMbh6TQglGM_xIIFREoWNDHGWJJgvoW6G2kbdXHIiU9JJHfRnrVTZ2KRIB3UEYxxN3fRoO-V1SvkXlZXpdfOGv0MXgFmosvMFm5KMt1A4sULb3R__fn-oUszqWr3MmkLXXozKQ7QTqpzC4frcx89Xl48DK_88d3oetgf-4a5bj4AGJrqBGIZao6JJEkkQbhrAjSmMjWUGkI4NZJzobVIeyAiSENgqeE47O2j89XeWRu7XgbKpta5mtVZoeuFqnSmfitlNlFP1avqScowdvmTdb6uXlqwjSoyayDPdQlVa5UQTFDJ2J9GwiNJIhI549nKaOrK2hrSTRmC1ZKUmqolDrXEoZak1JqUmrvw0c_vbKJrNE7vr_S3LIfFPzari9vBzffc-wKCy6Yc</recordid><startdate>199509</startdate><enddate>199509</enddate><creator>Kennard, M. 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A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5091-eeec4fadeb92a60191d89e7eb9de4b49fc44c1164c9667aa7f3e78ef2e5fc6023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Animals</topic><topic>Antigens, Neoplasm</topic><topic>Antigens, Surface - metabolism</topic><topic>Biological Transport</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>Gene Expression</topic><topic>Glycosylphosphatidylinositols - metabolism</topic><topic>Humans</topic><topic>Iron - metabolism</topic><topic>Kinetics</topic><topic>Mammals</topic><topic>Melanoma-Specific Antigens</topic><topic>Neoplasm Proteins - biosynthesis</topic><topic>Neoplasm Proteins - metabolism</topic><topic>Phosphatidylinositol Diacylglycerol-Lyase</topic><topic>Phosphoric Diester Hydrolases - metabolism</topic><topic>Phosphoric Diester Hydrolases - pharmacology</topic><topic>Pronase - pharmacology</topic><topic>Receptors, Transferrin - biosynthesis</topic><topic>Receptors, Transferrin - metabolism</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - metabolism</topic><topic>Transfection</topic><topic>Transferrin - biosynthesis</topic><topic>Transferrin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kennard, M. L.</creatorcontrib><creatorcontrib>Richardson, D. R.</creatorcontrib><creatorcontrib>Gabathuler, R.</creatorcontrib><creatorcontrib>Ponka, P.</creatorcontrib><creatorcontrib>Jefferies, W. A.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kennard, M. L.</au><au>Richardson, D. R.</au><au>Gabathuler, R.</au><au>Ponka, P.</au><au>Jefferies, W. A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel iron uptake mechanism mediated by GPI‐anchored human p97</atitle><jtitle>The EMBO journal</jtitle><addtitle>EMBO J</addtitle><date>1995-09</date><risdate>1995</risdate><volume>14</volume><issue>17</issue><spage>4178</spage><epage>4186</epage><pages>4178-4186</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><abstract>The established process for iron uptake into mammalian cells involves transferrin and its receptor. Here, the role of the glycosyl‐phosphatidylinositol (GPI)‐linked transferrin homologue, melanotransferrin or p97, was studied using CHO cell lines defective in the transferrin receptor (TR) and transfected with human TR and/or human p97. The presence of p97 doubled the iron uptake, which could be explained by the binding of one atom of iron to one molecule of p97. The internalization of iron was shown to be temperature sensitive and saturated at a media iron concentration of 2.5 micrograms/ml with a Vmax of 0.1 pmol Fe/10(6) cell/min and a Km of 2.58 microM for p97. Treatment of the cells with either phosphatidylinositol‐phospholipase C or monoclonal antibodies against p97 resulted in over a 50% reduction and a 47% increase in the iron uptake respectively. These data identify p97 as a unique cell surface GPI‐anchored, iron binding protein involved in the transferrin‐independent uptake of iron in mammals.</abstract><cop>England</cop><pmid>7556058</pmid><doi>10.1002/j.1460-2075.1995.tb00091.x</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Antigens, Neoplasm Antigens, Surface - metabolism Biological Transport CHO Cells Cricetinae Gene Expression Glycosylphosphatidylinositols - metabolism Humans Iron - metabolism Kinetics Mammals Melanoma-Specific Antigens Neoplasm Proteins - biosynthesis Neoplasm Proteins - metabolism Phosphatidylinositol Diacylglycerol-Lyase Phosphoric Diester Hydrolases - metabolism Phosphoric Diester Hydrolases - pharmacology Pronase - pharmacology Receptors, Transferrin - biosynthesis Receptors, Transferrin - metabolism Recombinant Proteins - biosynthesis Recombinant Proteins - metabolism Transfection Transferrin - biosynthesis Transferrin - metabolism |
| title | A novel iron uptake mechanism mediated by GPI‐anchored human p97 |
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