Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells

<p<Abstract</p< <p<CD36, an 88 kDa membrane glycoprotein, is found in several cell types and it has been characterized to have two hydrophobic domains at their N- and C-termini which are essential for protein folding and targeting. In this study, we first tagged the green fluoresce...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Crandall Ian [verfasserIn] Zhang Jianshe [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2007

Übergeordnetes Werk:	In: Lipids in Health and Disease - BMC, 2003, 6(2007), 1, p 24
Übergeordnetes Werk:	volume:6 ; year:2007 ; number:1, p 24

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1186/1476-511X-6-24

Katalog-ID:	DOAJ005384907

Internformat


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allfields	10.1186/1476-511X-6-24 doi (DE-627)DOAJ005384907 (DE-599)DOAJ8bd5e3aa37e040679390e37f996c9ced DE-627 ger DE-627 rakwb eng RC620-627 Crandall Ian verfasserin aut Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <p<Abstract</p< <p<CD36, an 88 kDa membrane glycoprotein, is found in several cell types and it has been characterized to have two hydrophobic domains at their N- and C-termini which are essential for protein folding and targeting. In this study, we first tagged the green fluorescent protein (GFP) to both the N- and C-termini of huCD36 and investigated their cellular expression and influences on lipoprotein and plasmodium falciparium parasitized erythrocytes (pRBC) binding. Our work revealed that huCD36 proteins are expressed normally irrespective of the GFP tag presence at either the N- or C-termini. However, the two recombinant proteins showed discrepancy in uptake and surface-binding of OxLDL but they did not affect pRBC binding. These results suggested that the interaction between oxLDL and CD36 could be blocked using recombinant proteins and this may be useful in potential control of the trafficking of modified lipoproteins into monocytes leading to atherogenesis.</p< Nutritional diseases. Deficiency diseases Zhang Jianshe verfasserin aut In Lipids in Health and Disease BMC, 2003 6(2007), 1, p 24 (DE-627)355987694 (DE-600)2091381-3 1476511X nnns volume:6 year:2007 number:1, p 24 https://doi.org/10.1186/1476-511X-6-24 kostenfrei https://doaj.org/article/8bd5e3aa37e040679390e37f996c9ced kostenfrei http://www.lipidworld.com/content/6/1/24 kostenfrei https://doaj.org/toc/1476-511X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2007 1, p 24
spelling	10.1186/1476-511X-6-24 doi (DE-627)DOAJ005384907 (DE-599)DOAJ8bd5e3aa37e040679390e37f996c9ced DE-627 ger DE-627 rakwb eng RC620-627 Crandall Ian verfasserin aut Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <p<Abstract</p< <p<CD36, an 88 kDa membrane glycoprotein, is found in several cell types and it has been characterized to have two hydrophobic domains at their N- and C-termini which are essential for protein folding and targeting. In this study, we first tagged the green fluorescent protein (GFP) to both the N- and C-termini of huCD36 and investigated their cellular expression and influences on lipoprotein and plasmodium falciparium parasitized erythrocytes (pRBC) binding. Our work revealed that huCD36 proteins are expressed normally irrespective of the GFP tag presence at either the N- or C-termini. However, the two recombinant proteins showed discrepancy in uptake and surface-binding of OxLDL but they did not affect pRBC binding. These results suggested that the interaction between oxLDL and CD36 could be blocked using recombinant proteins and this may be useful in potential control of the trafficking of modified lipoproteins into monocytes leading to atherogenesis.</p< Nutritional diseases. Deficiency diseases Zhang Jianshe verfasserin aut In Lipids in Health and Disease BMC, 2003 6(2007), 1, p 24 (DE-627)355987694 (DE-600)2091381-3 1476511X nnns volume:6 year:2007 number:1, p 24 https://doi.org/10.1186/1476-511X-6-24 kostenfrei https://doaj.org/article/8bd5e3aa37e040679390e37f996c9ced kostenfrei http://www.lipidworld.com/content/6/1/24 kostenfrei https://doaj.org/toc/1476-511X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2007 1, p 24
allfields_unstemmed	10.1186/1476-511X-6-24 doi (DE-627)DOAJ005384907 (DE-599)DOAJ8bd5e3aa37e040679390e37f996c9ced DE-627 ger DE-627 rakwb eng RC620-627 Crandall Ian verfasserin aut Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <p<Abstract</p< <p<CD36, an 88 kDa membrane glycoprotein, is found in several cell types and it has been characterized to have two hydrophobic domains at their N- and C-termini which are essential for protein folding and targeting. In this study, we first tagged the green fluorescent protein (GFP) to both the N- and C-termini of huCD36 and investigated their cellular expression and influences on lipoprotein and plasmodium falciparium parasitized erythrocytes (pRBC) binding. Our work revealed that huCD36 proteins are expressed normally irrespective of the GFP tag presence at either the N- or C-termini. However, the two recombinant proteins showed discrepancy in uptake and surface-binding of OxLDL but they did not affect pRBC binding. These results suggested that the interaction between oxLDL and CD36 could be blocked using recombinant proteins and this may be useful in potential control of the trafficking of modified lipoproteins into monocytes leading to atherogenesis.</p< Nutritional diseases. Deficiency diseases Zhang Jianshe verfasserin aut In Lipids in Health and Disease BMC, 2003 6(2007), 1, p 24 (DE-627)355987694 (DE-600)2091381-3 1476511X nnns volume:6 year:2007 number:1, p 24 https://doi.org/10.1186/1476-511X-6-24 kostenfrei https://doaj.org/article/8bd5e3aa37e040679390e37f996c9ced kostenfrei http://www.lipidworld.com/content/6/1/24 kostenfrei https://doaj.org/toc/1476-511X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2007 1, p 24
allfieldsGer	10.1186/1476-511X-6-24 doi (DE-627)DOAJ005384907 (DE-599)DOAJ8bd5e3aa37e040679390e37f996c9ced DE-627 ger DE-627 rakwb eng RC620-627 Crandall Ian verfasserin aut Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <p<Abstract</p< <p<CD36, an 88 kDa membrane glycoprotein, is found in several cell types and it has been characterized to have two hydrophobic domains at their N- and C-termini which are essential for protein folding and targeting. In this study, we first tagged the green fluorescent protein (GFP) to both the N- and C-termini of huCD36 and investigated their cellular expression and influences on lipoprotein and plasmodium falciparium parasitized erythrocytes (pRBC) binding. Our work revealed that huCD36 proteins are expressed normally irrespective of the GFP tag presence at either the N- or C-termini. However, the two recombinant proteins showed discrepancy in uptake and surface-binding of OxLDL but they did not affect pRBC binding. These results suggested that the interaction between oxLDL and CD36 could be blocked using recombinant proteins and this may be useful in potential control of the trafficking of modified lipoproteins into monocytes leading to atherogenesis.</p< Nutritional diseases. Deficiency diseases Zhang Jianshe verfasserin aut In Lipids in Health and Disease BMC, 2003 6(2007), 1, p 24 (DE-627)355987694 (DE-600)2091381-3 1476511X nnns volume:6 year:2007 number:1, p 24 https://doi.org/10.1186/1476-511X-6-24 kostenfrei https://doaj.org/article/8bd5e3aa37e040679390e37f996c9ced kostenfrei http://www.lipidworld.com/content/6/1/24 kostenfrei https://doaj.org/toc/1476-511X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2007 1, p 24
allfieldsSound	10.1186/1476-511X-6-24 doi (DE-627)DOAJ005384907 (DE-599)DOAJ8bd5e3aa37e040679390e37f996c9ced DE-627 ger DE-627 rakwb eng RC620-627 Crandall Ian verfasserin aut Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <p<Abstract</p< <p<CD36, an 88 kDa membrane glycoprotein, is found in several cell types and it has been characterized to have two hydrophobic domains at their N- and C-termini which are essential for protein folding and targeting. In this study, we first tagged the green fluorescent protein (GFP) to both the N- and C-termini of huCD36 and investigated their cellular expression and influences on lipoprotein and plasmodium falciparium parasitized erythrocytes (pRBC) binding. Our work revealed that huCD36 proteins are expressed normally irrespective of the GFP tag presence at either the N- or C-termini. However, the two recombinant proteins showed discrepancy in uptake and surface-binding of OxLDL but they did not affect pRBC binding. These results suggested that the interaction between oxLDL and CD36 could be blocked using recombinant proteins and this may be useful in potential control of the trafficking of modified lipoproteins into monocytes leading to atherogenesis.</p< Nutritional diseases. Deficiency diseases Zhang Jianshe verfasserin aut In Lipids in Health and Disease BMC, 2003 6(2007), 1, p 24 (DE-627)355987694 (DE-600)2091381-3 1476511X nnns volume:6 year:2007 number:1, p 24 https://doi.org/10.1186/1476-511X-6-24 kostenfrei https://doaj.org/article/8bd5e3aa37e040679390e37f996c9ced kostenfrei http://www.lipidworld.com/content/6/1/24 kostenfrei https://doaj.org/toc/1476-511X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2007 1, p 24
language	English
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callnumber-first	R - Medicine
author	Crandall Ian
spellingShingle	Crandall Ian misc RC620-627 misc Nutritional diseases. Deficiency diseases Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells
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topic_title	RC620-627 Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells
topic	misc RC620-627 misc Nutritional diseases. Deficiency diseases
topic_unstemmed	misc RC620-627 misc Nutritional diseases. Deficiency diseases
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title	Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells
ctrlnum	(DE-627)DOAJ005384907 (DE-599)DOAJ8bd5e3aa37e040679390e37f996c9ced
title_full	Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells
author_sort	Crandall Ian
journal	Lipids in Health and Disease
journalStr	Lipids in Health and Disease
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author_browse	Crandall Ian Zhang Jianshe
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title_sort	expression of both n- and c-terminal gfp tagged hucd36 and their discrepancy in oxldl and prbc binding on cho cells
callnumber	RC620-627
title_auth	Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells
abstract	<p<Abstract</p< <p<CD36, an 88 kDa membrane glycoprotein, is found in several cell types and it has been characterized to have two hydrophobic domains at their N- and C-termini which are essential for protein folding and targeting. In this study, we first tagged the green fluorescent protein (GFP) to both the N- and C-termini of huCD36 and investigated their cellular expression and influences on lipoprotein and plasmodium falciparium parasitized erythrocytes (pRBC) binding. Our work revealed that huCD36 proteins are expressed normally irrespective of the GFP tag presence at either the N- or C-termini. However, the two recombinant proteins showed discrepancy in uptake and surface-binding of OxLDL but they did not affect pRBC binding. These results suggested that the interaction between oxLDL and CD36 could be blocked using recombinant proteins and this may be useful in potential control of the trafficking of modified lipoproteins into monocytes leading to atherogenesis.</p<
abstractGer	<p<Abstract</p< <p<CD36, an 88 kDa membrane glycoprotein, is found in several cell types and it has been characterized to have two hydrophobic domains at their N- and C-termini which are essential for protein folding and targeting. In this study, we first tagged the green fluorescent protein (GFP) to both the N- and C-termini of huCD36 and investigated their cellular expression and influences on lipoprotein and plasmodium falciparium parasitized erythrocytes (pRBC) binding. Our work revealed that huCD36 proteins are expressed normally irrespective of the GFP tag presence at either the N- or C-termini. However, the two recombinant proteins showed discrepancy in uptake and surface-binding of OxLDL but they did not affect pRBC binding. These results suggested that the interaction between oxLDL and CD36 could be blocked using recombinant proteins and this may be useful in potential control of the trafficking of modified lipoproteins into monocytes leading to atherogenesis.</p<
abstract_unstemmed	<p<Abstract</p< <p<CD36, an 88 kDa membrane glycoprotein, is found in several cell types and it has been characterized to have two hydrophobic domains at their N- and C-termini which are essential for protein folding and targeting. In this study, we first tagged the green fluorescent protein (GFP) to both the N- and C-termini of huCD36 and investigated their cellular expression and influences on lipoprotein and plasmodium falciparium parasitized erythrocytes (pRBC) binding. Our work revealed that huCD36 proteins are expressed normally irrespective of the GFP tag presence at either the N- or C-termini. However, the two recombinant proteins showed discrepancy in uptake and surface-binding of OxLDL but they did not affect pRBC binding. These results suggested that the interaction between oxLDL and CD36 could be blocked using recombinant proteins and this may be useful in potential control of the trafficking of modified lipoproteins into monocytes leading to atherogenesis.</p<
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container_issue	1, p 24
title_short	Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells
url	https://doi.org/10.1186/1476-511X-6-24 https://doaj.org/article/8bd5e3aa37e040679390e37f996c9ced http://www.lipidworld.com/content/6/1/24 https://doaj.org/toc/1476-511X
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up_date	2024-07-03T14:42:03.270Z
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Expression of both N- and C-terminal GFP tagged huCD36 and their discrepancy in OxLDL and pRBC binding on CHO cells

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