Segregation of transferrin to a mildly acidic (pH 6.5) para-golgi compartment in the recycling pathway
To study the intracellular sorting of internalized ligands and receptors, we examined the pathways of two ligands: transferrin, which is recycled, and α 2-macroglobulin ( α 2M), which is degraded. In CHO cells the two ligands rapidly segregate into different intracellular compartments. Within 5 min...
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| Veröffentlicht in: | Cell 1984-07, Vol.37 (3), p.789-800 |
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| creator | Yamashiro, Darrell J. Tycko, Benjamin Fluss, Sharon R. Maxfield, Frederick R. |
| description | To study the intracellular sorting of internalized ligands and receptors, we examined the pathways of two ligands: transferrin, which is recycled, and
α
2-macroglobulin (
α
2M), which is degraded. In CHO cells the two ligands rapidly segregate into different intracellular compartments. Within 5 min fluorescein-labeled transferrin (F-Tf) is found in a large round juxtanuclear structure. Rhodamine-labeled
α
2M is found in a punctate pattern. Ultra-structural localization studies demonstrate that colloidal gold-
α
2M is found predominantly in endocytic vesicles, while ferritin-transferrin is found in small vesicles and tubular structures in a region adjacent to the Golgi complex. Using image intensified fluorescence microscopy and digital image analysis, we determined that the F-Tf containing structure has a pH of 6.4 ± 0.2, while endocytic vesicles containing F-
α
2M have a pH of 5.4 ± 0.1. Our study defines a mildly acidic compartment, distinct from endocytic vesicles, that is involved in the recycling of internalized components back to the cell surface. |
| doi_str_mv | 10.1016/0092-8674(84)90414-8 |
| format | Article |
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α
2-macroglobulin (
α
2M), which is degraded. In CHO cells the two ligands rapidly segregate into different intracellular compartments. Within 5 min fluorescein-labeled transferrin (F-Tf) is found in a large round juxtanuclear structure. Rhodamine-labeled
α
2M is found in a punctate pattern. Ultra-structural localization studies demonstrate that colloidal gold-
α
2M is found predominantly in endocytic vesicles, while ferritin-transferrin is found in small vesicles and tubular structures in a region adjacent to the Golgi complex. Using image intensified fluorescence microscopy and digital image analysis, we determined that the F-Tf containing structure has a pH of 6.4 ± 0.2, while endocytic vesicles containing F-
α
2M have a pH of 5.4 ± 0.1. Our study defines a mildly acidic compartment, distinct from endocytic vesicles, that is involved in the recycling of internalized components back to the cell surface.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/0092-8674(84)90414-8</identifier><identifier>PMID: 6204769</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>alpha-Macroglobulins - metabolism ; Animals ; Biological Transport ; Cell Compartmentation ; Cell Line ; Cell Membrane - metabolism ; Cricetinae ; Endocytosis ; Female ; Golgi Apparatus - metabolism ; Hydrogen-Ion Concentration ; Kinetics ; Low Density Lipoprotein Receptor-Related Protein-1 ; Membrane Proteins - metabolism ; Ovary ; Receptors, Cell Surface - metabolism ; Receptors, Immunologic - metabolism ; Receptors, Transferrin ; Transferrin - metabolism</subject><ispartof>Cell, 1984-07, Vol.37 (3), p.789-800</ispartof><rights>1984</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c423t-eee285573808a7217f36a232811787ce0bcc07412110feba51f52f1529cbb5e53</citedby><cites>FETCH-LOGICAL-c423t-eee285573808a7217f36a232811787ce0bcc07412110feba51f52f1529cbb5e53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0092867484904148$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6204769$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yamashiro, Darrell J.</creatorcontrib><creatorcontrib>Tycko, Benjamin</creatorcontrib><creatorcontrib>Fluss, Sharon R.</creatorcontrib><creatorcontrib>Maxfield, Frederick R.</creatorcontrib><title>Segregation of transferrin to a mildly acidic (pH 6.5) para-golgi compartment in the recycling pathway</title><title>Cell</title><addtitle>Cell</addtitle><description>To study the intracellular sorting of internalized ligands and receptors, we examined the pathways of two ligands: transferrin, which is recycled, and
α
2-macroglobulin (
α
2M), which is degraded. In CHO cells the two ligands rapidly segregate into different intracellular compartments. Within 5 min fluorescein-labeled transferrin (F-Tf) is found in a large round juxtanuclear structure. Rhodamine-labeled
α
2M is found in a punctate pattern. Ultra-structural localization studies demonstrate that colloidal gold-
α
2M is found predominantly in endocytic vesicles, while ferritin-transferrin is found in small vesicles and tubular structures in a region adjacent to the Golgi complex. Using image intensified fluorescence microscopy and digital image analysis, we determined that the F-Tf containing structure has a pH of 6.4 ± 0.2, while endocytic vesicles containing F-
α
2M have a pH of 5.4 ± 0.1. Our study defines a mildly acidic compartment, distinct from endocytic vesicles, that is involved in the recycling of internalized components back to the cell surface.</description><subject>alpha-Macroglobulins - metabolism</subject><subject>Animals</subject><subject>Biological Transport</subject><subject>Cell Compartmentation</subject><subject>Cell Line</subject><subject>Cell Membrane - metabolism</subject><subject>Cricetinae</subject><subject>Endocytosis</subject><subject>Female</subject><subject>Golgi Apparatus - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Low Density Lipoprotein Receptor-Related Protein-1</subject><subject>Membrane Proteins - metabolism</subject><subject>Ovary</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, Immunologic - metabolism</subject><subject>Receptors, Transferrin</subject><subject>Transferrin - metabolism</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEFr3DAQhUVoSLdJ_kELOpXNwakkS5Z8KZQlTQqBHNKchSyPHBXb2kraFP_7aLNLjj0Nw7z3ZuZD6DMl15TQ5hshLatUI_la8auWcMordYJWlLSy4lSyD2j1LvmIPqX0hxCihBBn6KxhhMumXSH3CEOEwWQfZhwcztHMyUGMfsY5YIMnP_bjgo31vbd4vb3DzbW4wlsTTTWEcfDYhql0eYI5473rGXAEu9jRz0PR5ed_ZrlAp86MCS6P9Rw9_bz5vbmr7h9uf21-3FeWszpXAMDKhbJWRBnJqHR1Y1jNFKVSSQuks5ZIThmlxEFnBHWCOSpYa7tOgKjP0ddD7jaGvztIWU8-WRhHM0PYJV2CGkkUK0J-ENoYUorg9Db6ycRFU6L3ePWend6z04rrN7xaFduXY_6um6B_Nx15lvn3wxzKky8eok7Ww2yh94VJ1n3w_1_wCrjaiJ0</recordid><startdate>198407</startdate><enddate>198407</enddate><creator>Yamashiro, Darrell J.</creator><creator>Tycko, Benjamin</creator><creator>Fluss, Sharon R.</creator><creator>Maxfield, Frederick R.</creator><general>Elsevier Inc</general><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>7X8</scope></search><sort><creationdate>198407</creationdate><title>Segregation of transferrin to a mildly acidic (pH 6.5) para-golgi compartment in the recycling pathway</title><author>Yamashiro, Darrell J. ; Tycko, Benjamin ; Fluss, Sharon R. ; Maxfield, Frederick R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c423t-eee285573808a7217f36a232811787ce0bcc07412110feba51f52f1529cbb5e53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>alpha-Macroglobulins - metabolism</topic><topic>Animals</topic><topic>Biological Transport</topic><topic>Cell Compartmentation</topic><topic>Cell Line</topic><topic>Cell Membrane - metabolism</topic><topic>Cricetinae</topic><topic>Endocytosis</topic><topic>Female</topic><topic>Golgi Apparatus - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Low Density Lipoprotein Receptor-Related Protein-1</topic><topic>Membrane Proteins - metabolism</topic><topic>Ovary</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, Immunologic - metabolism</topic><topic>Receptors, Transferrin</topic><topic>Transferrin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yamashiro, Darrell J.</creatorcontrib><creatorcontrib>Tycko, Benjamin</creatorcontrib><creatorcontrib>Fluss, Sharon R.</creatorcontrib><creatorcontrib>Maxfield, Frederick R.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yamashiro, Darrell J.</au><au>Tycko, Benjamin</au><au>Fluss, Sharon R.</au><au>Maxfield, Frederick R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Segregation of transferrin to a mildly acidic (pH 6.5) para-golgi compartment in the recycling pathway</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1984-07</date><risdate>1984</risdate><volume>37</volume><issue>3</issue><spage>789</spage><epage>800</epage><pages>789-800</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>To study the intracellular sorting of internalized ligands and receptors, we examined the pathways of two ligands: transferrin, which is recycled, and
α
2-macroglobulin (
α
2M), which is degraded. In CHO cells the two ligands rapidly segregate into different intracellular compartments. Within 5 min fluorescein-labeled transferrin (F-Tf) is found in a large round juxtanuclear structure. Rhodamine-labeled
α
2M is found in a punctate pattern. Ultra-structural localization studies demonstrate that colloidal gold-
α
2M is found predominantly in endocytic vesicles, while ferritin-transferrin is found in small vesicles and tubular structures in a region adjacent to the Golgi complex. Using image intensified fluorescence microscopy and digital image analysis, we determined that the F-Tf containing structure has a pH of 6.4 ± 0.2, while endocytic vesicles containing F-
α
2M have a pH of 5.4 ± 0.1. Our study defines a mildly acidic compartment, distinct from endocytic vesicles, that is involved in the recycling of internalized components back to the cell surface.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>6204769</pmid><doi>10.1016/0092-8674(84)90414-8</doi><tpages>12</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Cell, 1984-07, Vol.37 (3), p.789-800 |
| issn | 0092-8674 1097-4172 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | alpha-Macroglobulins - metabolism Animals Biological Transport Cell Compartmentation Cell Line Cell Membrane - metabolism Cricetinae Endocytosis Female Golgi Apparatus - metabolism Hydrogen-Ion Concentration Kinetics Low Density Lipoprotein Receptor-Related Protein-1 Membrane Proteins - metabolism Ovary Receptors, Cell Surface - metabolism Receptors, Immunologic - metabolism Receptors, Transferrin Transferrin - metabolism |
| title | Segregation of transferrin to a mildly acidic (pH 6.5) para-golgi compartment in the recycling pathway |
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