The effects of lead upon collagen synthesis and proline hydroxylation in the Swiss mouse 3T6 fibroblast
The effects of lead upon collagen synthesis and proline hydroxylation were examined in the Swiss mouse 3T6 fibroblast. The results indicate that lead reduces proline hydroxylation in stationary phase cultures of 3T6 cells, resulting in increased cellular retention of unhydroxylated procollagen. Inhi...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1977-02, Vol.179 (1), p.15-23 |
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| container_title | Archives of biochemistry and biophysics |
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| creator | Vistica, David T. Ahrens, Franklin A. Ellison, Warren R. |
| description | The effects of lead upon collagen synthesis and proline hydroxylation were examined in the Swiss mouse 3T6 fibroblast. The results indicate that lead reduces proline hydroxylation in stationary phase cultures of 3T6 cells, resulting in increased cellular retention of unhydroxylated procollagen. Inhibition of proline hydroxylation by lead was prevented by increasing the extracellular
Fe
2+
Pb
2+
molar ratio. Interference by lead in the hydroxylation of proline in logarithmic phase cultures of 3T6 cells resulted in increases in the 0.5
n HClO
4 soluble/insoluble hydroxyproline ratio. This was attributed to an increase in the rate of breakdown of lead-induced unhydroxylated procollagen. Kinetic analysis of the lead-iron interaction with proline hydroxylase suggests that the mechanism is competitive. |
| doi_str_mv | 10.1016/0003-9861(77)90081-9 |
| format | Article |
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Fe
2+
Pb
2+
molar ratio. Interference by lead in the hydroxylation of proline in logarithmic phase cultures of 3T6 cells resulted in increases in the 0.5
n HClO
4 soluble/insoluble hydroxyproline ratio. This was attributed to an increase in the rate of breakdown of lead-induced unhydroxylated procollagen. Kinetic analysis of the lead-iron interaction with proline hydroxylase suggests that the mechanism is competitive.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(77)90081-9</identifier><identifier>PMID: 190947</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Cell Line ; Collagen - biosynthesis ; Fibroblasts - drug effects ; Fibroblasts - metabolism ; Kinetics ; Lead - pharmacology ; Mice ; Procollagen-Proline Dioxygenase - metabolism</subject><ispartof>Archives of biochemistry and biophysics, 1977-02, Vol.179 (1), p.15-23</ispartof><rights>1977</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c356t-93b4ea9a11f62972abead13a1c563e56dac1cb75f0eb8c0f3d4ec616f6f41c8e3</citedby><cites>FETCH-LOGICAL-c356t-93b4ea9a11f62972abead13a1c563e56dac1cb75f0eb8c0f3d4ec616f6f41c8e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0003-9861(77)90081-9$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/190947$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vistica, David T.</creatorcontrib><creatorcontrib>Ahrens, Franklin A.</creatorcontrib><creatorcontrib>Ellison, Warren R.</creatorcontrib><title>The effects of lead upon collagen synthesis and proline hydroxylation in the Swiss mouse 3T6 fibroblast</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The effects of lead upon collagen synthesis and proline hydroxylation were examined in the Swiss mouse 3T6 fibroblast. The results indicate that lead reduces proline hydroxylation in stationary phase cultures of 3T6 cells, resulting in increased cellular retention of unhydroxylated procollagen. Inhibition of proline hydroxylation by lead was prevented by increasing the extracellular
Fe
2+
Pb
2+
molar ratio. Interference by lead in the hydroxylation of proline in logarithmic phase cultures of 3T6 cells resulted in increases in the 0.5
n HClO
4 soluble/insoluble hydroxyproline ratio. This was attributed to an increase in the rate of breakdown of lead-induced unhydroxylated procollagen. Kinetic analysis of the lead-iron interaction with proline hydroxylase suggests that the mechanism is competitive.</description><subject>Animals</subject><subject>Cell Line</subject><subject>Collagen - biosynthesis</subject><subject>Fibroblasts - drug effects</subject><subject>Fibroblasts - metabolism</subject><subject>Kinetics</subject><subject>Lead - pharmacology</subject><subject>Mice</subject><subject>Procollagen-Proline Dioxygenase - metabolism</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1977</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtOwzAQRS3Eqzz-gIVXCBYBT5048QYJVbykSiwoa8txxtQojYudAP17XIpgx2oWc-bqziHkBNgFMBCXjDGeyUrAWVmeS8YqyOQWGQGTImO8yrfJ6BfZJwcxvjIGkIvxHtkFyWRejsjLbI4UrUXTR-otbVE3dFj6jhrftvoFOxpXXT_H6CLVXUOXwbeuQzpfNcF_rlrduwS7jiaGPn24GOnCDxEpnwlqXR183erYH5Edq9uIxz_zkDzf3swm99n08e5hcj3NDC9En0le56ilBrBiLMuxrlMf4BpMITgWotEGTF0WlmFdGWZ5k6MRIKywOZgK-SE53eSmnm8Dxl4tXDSYXukw1VIVr4QockhgvgFN8DEGtGoZ3EKHlQKm1nrV2p1au1Nlqb71KpnOTn7yh3qBzd_Rt8-0vtqsMf347jCoaBx2BhsXkmLVePd__hc4FIsq</recordid><startdate>197702</startdate><enddate>197702</enddate><creator>Vistica, David T.</creator><creator>Ahrens, Franklin A.</creator><creator>Ellison, Warren 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>197702</creationdate><title>The effects of lead upon collagen synthesis and proline hydroxylation in the Swiss mouse 3T6 fibroblast</title><author>Vistica, David T. ; Ahrens, Franklin A. ; Ellison, Warren R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-93b4ea9a11f62972abead13a1c563e56dac1cb75f0eb8c0f3d4ec616f6f41c8e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1977</creationdate><topic>Animals</topic><topic>Cell Line</topic><topic>Collagen - biosynthesis</topic><topic>Fibroblasts - drug effects</topic><topic>Fibroblasts - metabolism</topic><topic>Kinetics</topic><topic>Lead - pharmacology</topic><topic>Mice</topic><topic>Procollagen-Proline Dioxygenase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vistica, David T.</creatorcontrib><creatorcontrib>Ahrens, Franklin A.</creatorcontrib><creatorcontrib>Ellison, Warren 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>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vistica, David T.</au><au>Ahrens, Franklin A.</au><au>Ellison, Warren R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The effects of lead upon collagen synthesis and proline hydroxylation in the Swiss mouse 3T6 fibroblast</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1977-02</date><risdate>1977</risdate><volume>179</volume><issue>1</issue><spage>15</spage><epage>23</epage><pages>15-23</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>The effects of lead upon collagen synthesis and proline hydroxylation were examined in the Swiss mouse 3T6 fibroblast. The results indicate that lead reduces proline hydroxylation in stationary phase cultures of 3T6 cells, resulting in increased cellular retention of unhydroxylated procollagen. Inhibition of proline hydroxylation by lead was prevented by increasing the extracellular
Fe
2+
Pb
2+
molar ratio. Interference by lead in the hydroxylation of proline in logarithmic phase cultures of 3T6 cells resulted in increases in the 0.5
n HClO
4 soluble/insoluble hydroxyproline ratio. This was attributed to an increase in the rate of breakdown of lead-induced unhydroxylated procollagen. Kinetic analysis of the lead-iron interaction with proline hydroxylase suggests that the mechanism is competitive.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>190947</pmid><doi>10.1016/0003-9861(77)90081-9</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 1977-02, Vol.179 (1), p.15-23 |
| issn | 0003-9861 1096-0384 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Cell Line Collagen - biosynthesis Fibroblasts - drug effects Fibroblasts - metabolism Kinetics Lead - pharmacology Mice Procollagen-Proline Dioxygenase - metabolism |
| title | The effects of lead upon collagen synthesis and proline hydroxylation in the Swiss mouse 3T6 fibroblast |
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