Regulation of Sialyltransferase Activities by Phosphorylation and Dephosphorylation
Abstract: The composition of tissue gangliosides is thought to result mainly from the active regulation and selective expression of specific enzymes responsible for their metabolism. In the last few years, we have purified several rat brain sialyltransferases to homogeneity; the availability of thes...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Gu, Xinbin [verfasserIn] Preuß, Ute [verfasserIn] Gu, Tianjue [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|
| Erschienen: |
Oxford, UK: Blackwell Science Ltd ; 1995 |
|---|
| Schlagwörter: |
|---|
| Umfang: |
Online-Ressource |
|---|
| Reproduktion: |
2002 ; Blackwell Publishing Journal Backfiles 1879-2005 |
|---|---|
| Übergeordnetes Werk: |
In: Journal of neurochemistry - Oxford : Wiley-Blackwell, 1956, 64(1995), 5, Seite 0 |
| Übergeordnetes Werk: |
volume:64 ; year:1995 ; number:5 ; pages:0 |
| Links: |
|---|
| DOI / URN: |
10.1046/j.1471-4159.1995.64052295.x |
|---|
| Katalog-ID: |
NLEJ240236165 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLEJ240236165 | ||
| 003 | DE-627 | ||
| 005 | 20210707104835.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 120426s1995 xx |||||o 00| ||und c | ||
| 024 | 7 | |a 10.1046/j.1471-4159.1995.64052295.x |2 doi | |
| 035 | |a (DE-627)NLEJ240236165 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 100 | 1 | |a Gu, Xinbin |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Regulation of Sialyltransferase Activities by Phosphorylation and Dephosphorylation |
| 264 | 1 | |a Oxford, UK |b Blackwell Science Ltd |c 1995 | |
| 300 | |a Online-Ressource | ||
| 336 | |a nicht spezifiziert |b zzz |2 rdacontent | ||
| 337 | |a nicht spezifiziert |b z |2 rdamedia | ||
| 338 | |a nicht spezifiziert |b zu |2 rdacarrier | ||
| 520 | |a Abstract: The composition of tissue gangliosides is thought to result mainly from the active regulation and selective expression of specific enzymes responsible for their metabolism. In the last few years, we have purified several rat brain sialyltransferases to homogeneity; the availability of these highly purified enzymes enabled us to investigate their regulation and expression at the molecular level. Thus, we studied the regulation of sialyltransferase activities, in particular, CMP-NeuAc:GM1 and CMP-NeuAc:LacCer sialyltransferases by a phosphorylation/dephosphorylation mechanism. Protein kinase C was added to a standard enzyme assay mixture containing [γ-32P]ATP, and the activity of the enzyme was measured after various incubation times. We found that treatment of several sialyltransferases by protein kinase C decreased their activities in a time-dependent manner. Analyses of 32P-labeled amino acids revealed that the major phosphorylation site of CMP-NeuAc:GM1 α2→3 sialyltransferase (ST-IV) was serine and that for CMP-NeuAc:LacCer α2→3 sialyltransferase (ST-I) was primarily threonine. Partial recovery of the enzyme activity could be achieved by treatment of the phosphorylated sialyltransferases with rat brain protein phosphatase. We conclude that the activities of sialyltransferases can be modulated by protein kinase C and protein phosphatase and this may represent a potential regulatory mechanism for ganglioside biosynthesis. | ||
| 533 | |d 2002 |f Blackwell Publishing Journal Backfiles 1879-2005 |7 |2002|||||||||| | ||
| 650 | 4 | |a Sialyltransferases | |
| 700 | 1 | |a Preuß, Ute |e verfasserin |4 aut | |
| 700 | 1 | |a Gu, Tianjue |e verfasserin |4 aut | |
| 700 | 1 | |a Yu, Robert K. |4 oth | |
| 773 | 0 | 8 | |i In |t Journal of neurochemistry |d Oxford : Wiley-Blackwell, 1956 |g 64(1995), 5, Seite 0 |h Online-Ressource |w (DE-627)NLEJ243927584 |w (DE-600)2020528-4 |x 1471-4159 |7 nnns |
| 773 | 1 | 8 | |g volume:64 |g year:1995 |g number:5 |g pages:0 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1046/j.1471-4159.1995.64052295.x |q text/html |x Verlag |z Deutschlandweit zugänglich |3 Volltext |
| 912 | |a GBV_USEFLAG_U | ||
| 912 | |a ZDB-1-DJB | ||
| 912 | |a GBV_NL_ARTICLE | ||
| 951 | |a AR | ||
| 952 | |d 64 |j 1995 |e 5 |h 0 | ||
| author_variant |
x g xg u p up t g tg |
|---|---|
| matchkey_str |
article:14714159:1995----::euainfillrnfrsatvtebpopoyain |
| hierarchy_sort_str |
1995 |
| publishDate |
1995 |
| allfields |
10.1046/j.1471-4159.1995.64052295.x doi (DE-627)NLEJ240236165 DE-627 ger DE-627 rakwb Gu, Xinbin verfasserin aut Regulation of Sialyltransferase Activities by Phosphorylation and Dephosphorylation Oxford, UK Blackwell Science Ltd 1995 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The composition of tissue gangliosides is thought to result mainly from the active regulation and selective expression of specific enzymes responsible for their metabolism. In the last few years, we have purified several rat brain sialyltransferases to homogeneity; the availability of these highly purified enzymes enabled us to investigate their regulation and expression at the molecular level. Thus, we studied the regulation of sialyltransferase activities, in particular, CMP-NeuAc:GM1 and CMP-NeuAc:LacCer sialyltransferases by a phosphorylation/dephosphorylation mechanism. Protein kinase C was added to a standard enzyme assay mixture containing [γ-32P]ATP, and the activity of the enzyme was measured after various incubation times. We found that treatment of several sialyltransferases by protein kinase C decreased their activities in a time-dependent manner. Analyses of 32P-labeled amino acids revealed that the major phosphorylation site of CMP-NeuAc:GM1 α2→3 sialyltransferase (ST-IV) was serine and that for CMP-NeuAc:LacCer α2→3 sialyltransferase (ST-I) was primarily threonine. Partial recovery of the enzyme activity could be achieved by treatment of the phosphorylated sialyltransferases with rat brain protein phosphatase. We conclude that the activities of sialyltransferases can be modulated by protein kinase C and protein phosphatase and this may represent a potential regulatory mechanism for ganglioside biosynthesis. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Sialyltransferases Preuß, Ute verfasserin aut Gu, Tianjue verfasserin aut Yu, Robert K. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 64(1995), 5, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:64 year:1995 number:5 pages:0 http://dx.doi.org/10.1046/j.1471-4159.1995.64052295.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 64 1995 5 0 |
| spelling |
10.1046/j.1471-4159.1995.64052295.x doi (DE-627)NLEJ240236165 DE-627 ger DE-627 rakwb Gu, Xinbin verfasserin aut Regulation of Sialyltransferase Activities by Phosphorylation and Dephosphorylation Oxford, UK Blackwell Science Ltd 1995 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The composition of tissue gangliosides is thought to result mainly from the active regulation and selective expression of specific enzymes responsible for their metabolism. In the last few years, we have purified several rat brain sialyltransferases to homogeneity; the availability of these highly purified enzymes enabled us to investigate their regulation and expression at the molecular level. Thus, we studied the regulation of sialyltransferase activities, in particular, CMP-NeuAc:GM1 and CMP-NeuAc:LacCer sialyltransferases by a phosphorylation/dephosphorylation mechanism. Protein kinase C was added to a standard enzyme assay mixture containing [γ-32P]ATP, and the activity of the enzyme was measured after various incubation times. We found that treatment of several sialyltransferases by protein kinase C decreased their activities in a time-dependent manner. Analyses of 32P-labeled amino acids revealed that the major phosphorylation site of CMP-NeuAc:GM1 α2→3 sialyltransferase (ST-IV) was serine and that for CMP-NeuAc:LacCer α2→3 sialyltransferase (ST-I) was primarily threonine. Partial recovery of the enzyme activity could be achieved by treatment of the phosphorylated sialyltransferases with rat brain protein phosphatase. We conclude that the activities of sialyltransferases can be modulated by protein kinase C and protein phosphatase and this may represent a potential regulatory mechanism for ganglioside biosynthesis. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Sialyltransferases Preuß, Ute verfasserin aut Gu, Tianjue verfasserin aut Yu, Robert K. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 64(1995), 5, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:64 year:1995 number:5 pages:0 http://dx.doi.org/10.1046/j.1471-4159.1995.64052295.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 64 1995 5 0 |
| allfields_unstemmed |
10.1046/j.1471-4159.1995.64052295.x doi (DE-627)NLEJ240236165 DE-627 ger DE-627 rakwb Gu, Xinbin verfasserin aut Regulation of Sialyltransferase Activities by Phosphorylation and Dephosphorylation Oxford, UK Blackwell Science Ltd 1995 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The composition of tissue gangliosides is thought to result mainly from the active regulation and selective expression of specific enzymes responsible for their metabolism. In the last few years, we have purified several rat brain sialyltransferases to homogeneity; the availability of these highly purified enzymes enabled us to investigate their regulation and expression at the molecular level. Thus, we studied the regulation of sialyltransferase activities, in particular, CMP-NeuAc:GM1 and CMP-NeuAc:LacCer sialyltransferases by a phosphorylation/dephosphorylation mechanism. Protein kinase C was added to a standard enzyme assay mixture containing [γ-32P]ATP, and the activity of the enzyme was measured after various incubation times. We found that treatment of several sialyltransferases by protein kinase C decreased their activities in a time-dependent manner. Analyses of 32P-labeled amino acids revealed that the major phosphorylation site of CMP-NeuAc:GM1 α2→3 sialyltransferase (ST-IV) was serine and that for CMP-NeuAc:LacCer α2→3 sialyltransferase (ST-I) was primarily threonine. Partial recovery of the enzyme activity could be achieved by treatment of the phosphorylated sialyltransferases with rat brain protein phosphatase. We conclude that the activities of sialyltransferases can be modulated by protein kinase C and protein phosphatase and this may represent a potential regulatory mechanism for ganglioside biosynthesis. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Sialyltransferases Preuß, Ute verfasserin aut Gu, Tianjue verfasserin aut Yu, Robert K. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 64(1995), 5, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:64 year:1995 number:5 pages:0 http://dx.doi.org/10.1046/j.1471-4159.1995.64052295.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 64 1995 5 0 |
| allfieldsGer |
10.1046/j.1471-4159.1995.64052295.x doi (DE-627)NLEJ240236165 DE-627 ger DE-627 rakwb Gu, Xinbin verfasserin aut Regulation of Sialyltransferase Activities by Phosphorylation and Dephosphorylation Oxford, UK Blackwell Science Ltd 1995 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The composition of tissue gangliosides is thought to result mainly from the active regulation and selective expression of specific enzymes responsible for their metabolism. In the last few years, we have purified several rat brain sialyltransferases to homogeneity; the availability of these highly purified enzymes enabled us to investigate their regulation and expression at the molecular level. Thus, we studied the regulation of sialyltransferase activities, in particular, CMP-NeuAc:GM1 and CMP-NeuAc:LacCer sialyltransferases by a phosphorylation/dephosphorylation mechanism. Protein kinase C was added to a standard enzyme assay mixture containing [γ-32P]ATP, and the activity of the enzyme was measured after various incubation times. We found that treatment of several sialyltransferases by protein kinase C decreased their activities in a time-dependent manner. Analyses of 32P-labeled amino acids revealed that the major phosphorylation site of CMP-NeuAc:GM1 α2→3 sialyltransferase (ST-IV) was serine and that for CMP-NeuAc:LacCer α2→3 sialyltransferase (ST-I) was primarily threonine. Partial recovery of the enzyme activity could be achieved by treatment of the phosphorylated sialyltransferases with rat brain protein phosphatase. We conclude that the activities of sialyltransferases can be modulated by protein kinase C and protein phosphatase and this may represent a potential regulatory mechanism for ganglioside biosynthesis. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Sialyltransferases Preuß, Ute verfasserin aut Gu, Tianjue verfasserin aut Yu, Robert K. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 64(1995), 5, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:64 year:1995 number:5 pages:0 http://dx.doi.org/10.1046/j.1471-4159.1995.64052295.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 64 1995 5 0 |
| allfieldsSound |
10.1046/j.1471-4159.1995.64052295.x doi (DE-627)NLEJ240236165 DE-627 ger DE-627 rakwb Gu, Xinbin verfasserin aut Regulation of Sialyltransferase Activities by Phosphorylation and Dephosphorylation Oxford, UK Blackwell Science Ltd 1995 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The composition of tissue gangliosides is thought to result mainly from the active regulation and selective expression of specific enzymes responsible for their metabolism. In the last few years, we have purified several rat brain sialyltransferases to homogeneity; the availability of these highly purified enzymes enabled us to investigate their regulation and expression at the molecular level. Thus, we studied the regulation of sialyltransferase activities, in particular, CMP-NeuAc:GM1 and CMP-NeuAc:LacCer sialyltransferases by a phosphorylation/dephosphorylation mechanism. Protein kinase C was added to a standard enzyme assay mixture containing [γ-32P]ATP, and the activity of the enzyme was measured after various incubation times. We found that treatment of several sialyltransferases by protein kinase C decreased their activities in a time-dependent manner. Analyses of 32P-labeled amino acids revealed that the major phosphorylation site of CMP-NeuAc:GM1 α2→3 sialyltransferase (ST-IV) was serine and that for CMP-NeuAc:LacCer α2→3 sialyltransferase (ST-I) was primarily threonine. Partial recovery of the enzyme activity could be achieved by treatment of the phosphorylated sialyltransferases with rat brain protein phosphatase. We conclude that the activities of sialyltransferases can be modulated by protein kinase C and protein phosphatase and this may represent a potential regulatory mechanism for ganglioside biosynthesis. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Sialyltransferases Preuß, Ute verfasserin aut Gu, Tianjue verfasserin aut Yu, Robert K. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 64(1995), 5, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:64 year:1995 number:5 pages:0 http://dx.doi.org/10.1046/j.1471-4159.1995.64052295.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 64 1995 5 0 |
| source |
In Journal of neurochemistry 64(1995), 5, Seite 0 volume:64 year:1995 number:5 pages:0 |
| sourceStr |
In Journal of neurochemistry 64(1995), 5, Seite 0 volume:64 year:1995 number:5 pages:0 |
| format_phy_str_mv |
Article |
| institution |
findex.gbv.de |
| topic_facet |
Sialyltransferases |
| isfreeaccess_bool |
false |
| container_title |
Journal of neurochemistry |
| authorswithroles_txt_mv |
Gu, Xinbin @@aut@@ Preuß, Ute @@aut@@ Gu, Tianjue @@aut@@ Yu, Robert K. @@oth@@ |
| publishDateDaySort_date |
1995-01-01T00:00:00Z |
| hierarchy_top_id |
NLEJ243927584 |
| id |
NLEJ240236165 |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ240236165</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707104835.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120426s1995 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1046/j.1471-4159.1995.64052295.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ240236165</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Gu, Xinbin</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Regulation of Sialyltransferase Activities by Phosphorylation and Dephosphorylation</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Science Ltd</subfield><subfield code="c">1995</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract: The composition of tissue gangliosides is thought to result mainly from the active regulation and selective expression of specific enzymes responsible for their metabolism. In the last few years, we have purified several rat brain sialyltransferases to homogeneity; the availability of these highly purified enzymes enabled us to investigate their regulation and expression at the molecular level. Thus, we studied the regulation of sialyltransferase activities, in particular, CMP-NeuAc:GM1 and CMP-NeuAc:LacCer sialyltransferases by a phosphorylation/dephosphorylation mechanism. Protein kinase C was added to a standard enzyme assay mixture containing [γ-32P]ATP, and the activity of the enzyme was measured after various incubation times. We found that treatment of several sialyltransferases by protein kinase C decreased their activities in a time-dependent manner. Analyses of 32P-labeled amino acids revealed that the major phosphorylation site of CMP-NeuAc:GM1 α2→3 sialyltransferase (ST-IV) was serine and that for CMP-NeuAc:LacCer α2→3 sialyltransferase (ST-I) was primarily threonine. Partial recovery of the enzyme activity could be achieved by treatment of the phosphorylated sialyltransferases with rat brain protein phosphatase. We conclude that the activities of sialyltransferases can be modulated by protein kinase C and protein phosphatase and this may represent a potential regulatory mechanism for ganglioside biosynthesis.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2002</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2002||||||||||</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Sialyltransferases</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Preuß, Ute</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gu, Tianjue</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Yu, Robert K.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Journal of neurochemistry</subfield><subfield code="d">Oxford : Wiley-Blackwell, 1956</subfield><subfield code="g">64(1995), 5, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243927584</subfield><subfield code="w">(DE-600)2020528-4</subfield><subfield code="x">1471-4159</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:64</subfield><subfield code="g">year:1995</subfield><subfield code="g">number:5</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1046/j.1471-4159.1995.64052295.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">64</subfield><subfield code="j">1995</subfield><subfield code="e">5</subfield><subfield code="h">0</subfield></datafield></record></collection>
|
| series2 |
Blackwell Publishing Journal Backfiles 1879-2005 |
| author |
Gu, Xinbin |
| spellingShingle |
Gu, Xinbin misc Sialyltransferases Regulation of Sialyltransferase Activities by Phosphorylation and Dephosphorylation |
| authorStr |
Gu, Xinbin |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)NLEJ243927584 |
| format |
electronic Article |
| delete_txt_mv |
keep |
| author_role |
aut aut aut |
| collection |
NL |
| publishPlace |
Oxford, UK |
| remote_str |
true |
| illustrated |
Not Illustrated |
| issn |
1471-4159 |
| topic_title |
Regulation of Sialyltransferase Activities by Phosphorylation and Dephosphorylation Sialyltransferases |
| publisher |
Blackwell Science Ltd |
| publisherStr |
Blackwell Science Ltd |
| topic |
misc Sialyltransferases |
| topic_unstemmed |
misc Sialyltransferases |
| topic_browse |
misc Sialyltransferases |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
zu |
| author2_variant |
r k y rk rky |
| hierarchy_parent_title |
Journal of neurochemistry |
| hierarchy_parent_id |
NLEJ243927584 |
| hierarchy_top_title |
Journal of neurochemistry |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)NLEJ243927584 (DE-600)2020528-4 |
| title |
Regulation of Sialyltransferase Activities by Phosphorylation and Dephosphorylation |
| ctrlnum |
(DE-627)NLEJ240236165 |
| title_full |
Regulation of Sialyltransferase Activities by Phosphorylation and Dephosphorylation |
| author_sort |
Gu, Xinbin |
| journal |
Journal of neurochemistry |
| journalStr |
Journal of neurochemistry |
| isOA_bool |
false |
| recordtype |
marc |
| publishDateSort |
1995 |
| contenttype_str_mv |
zzz |
| container_start_page |
0 |
| author_browse |
Gu, Xinbin Preuß, Ute Gu, Tianjue |
| container_volume |
64 |
| physical |
Online-Ressource |
| format_se |
Elektronische Aufsätze |
| author-letter |
Gu, Xinbin |
| doi_str_mv |
10.1046/j.1471-4159.1995.64052295.x |
| author2-role |
verfasserin |
| title_sort |
regulation of sialyltransferase activities by phosphorylation and dephosphorylation |
| title_auth |
Regulation of Sialyltransferase Activities by Phosphorylation and Dephosphorylation |
| abstract |
Abstract: The composition of tissue gangliosides is thought to result mainly from the active regulation and selective expression of specific enzymes responsible for their metabolism. In the last few years, we have purified several rat brain sialyltransferases to homogeneity; the availability of these highly purified enzymes enabled us to investigate their regulation and expression at the molecular level. Thus, we studied the regulation of sialyltransferase activities, in particular, CMP-NeuAc:GM1 and CMP-NeuAc:LacCer sialyltransferases by a phosphorylation/dephosphorylation mechanism. Protein kinase C was added to a standard enzyme assay mixture containing [γ-32P]ATP, and the activity of the enzyme was measured after various incubation times. We found that treatment of several sialyltransferases by protein kinase C decreased their activities in a time-dependent manner. Analyses of 32P-labeled amino acids revealed that the major phosphorylation site of CMP-NeuAc:GM1 α2→3 sialyltransferase (ST-IV) was serine and that for CMP-NeuAc:LacCer α2→3 sialyltransferase (ST-I) was primarily threonine. Partial recovery of the enzyme activity could be achieved by treatment of the phosphorylated sialyltransferases with rat brain protein phosphatase. We conclude that the activities of sialyltransferases can be modulated by protein kinase C and protein phosphatase and this may represent a potential regulatory mechanism for ganglioside biosynthesis. |
| abstractGer |
Abstract: The composition of tissue gangliosides is thought to result mainly from the active regulation and selective expression of specific enzymes responsible for their metabolism. In the last few years, we have purified several rat brain sialyltransferases to homogeneity; the availability of these highly purified enzymes enabled us to investigate their regulation and expression at the molecular level. Thus, we studied the regulation of sialyltransferase activities, in particular, CMP-NeuAc:GM1 and CMP-NeuAc:LacCer sialyltransferases by a phosphorylation/dephosphorylation mechanism. Protein kinase C was added to a standard enzyme assay mixture containing [γ-32P]ATP, and the activity of the enzyme was measured after various incubation times. We found that treatment of several sialyltransferases by protein kinase C decreased their activities in a time-dependent manner. Analyses of 32P-labeled amino acids revealed that the major phosphorylation site of CMP-NeuAc:GM1 α2→3 sialyltransferase (ST-IV) was serine and that for CMP-NeuAc:LacCer α2→3 sialyltransferase (ST-I) was primarily threonine. Partial recovery of the enzyme activity could be achieved by treatment of the phosphorylated sialyltransferases with rat brain protein phosphatase. We conclude that the activities of sialyltransferases can be modulated by protein kinase C and protein phosphatase and this may represent a potential regulatory mechanism for ganglioside biosynthesis. |
| abstract_unstemmed |
Abstract: The composition of tissue gangliosides is thought to result mainly from the active regulation and selective expression of specific enzymes responsible for their metabolism. In the last few years, we have purified several rat brain sialyltransferases to homogeneity; the availability of these highly purified enzymes enabled us to investigate their regulation and expression at the molecular level. Thus, we studied the regulation of sialyltransferase activities, in particular, CMP-NeuAc:GM1 and CMP-NeuAc:LacCer sialyltransferases by a phosphorylation/dephosphorylation mechanism. Protein kinase C was added to a standard enzyme assay mixture containing [γ-32P]ATP, and the activity of the enzyme was measured after various incubation times. We found that treatment of several sialyltransferases by protein kinase C decreased their activities in a time-dependent manner. Analyses of 32P-labeled amino acids revealed that the major phosphorylation site of CMP-NeuAc:GM1 α2→3 sialyltransferase (ST-IV) was serine and that for CMP-NeuAc:LacCer α2→3 sialyltransferase (ST-I) was primarily threonine. Partial recovery of the enzyme activity could be achieved by treatment of the phosphorylated sialyltransferases with rat brain protein phosphatase. We conclude that the activities of sialyltransferases can be modulated by protein kinase C and protein phosphatase and this may represent a potential regulatory mechanism for ganglioside biosynthesis. |
| collection_details |
GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE |
| container_issue |
5 |
| title_short |
Regulation of Sialyltransferase Activities by Phosphorylation and Dephosphorylation |
| url |
http://dx.doi.org/10.1046/j.1471-4159.1995.64052295.x |
| remote_bool |
true |
| author2 |
Preuß, Ute Gu, Tianjue Yu, Robert K. |
| author2Str |
Preuß, Ute Gu, Tianjue Yu, Robert K. |
| ppnlink |
NLEJ243927584 |
| mediatype_str_mv |
z |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| author2_role |
oth |
| doi_str |
10.1046/j.1471-4159.1995.64052295.x |
| up_date |
2024-07-06T09:25:25.980Z |
| _version_ |
1803821174994501632 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ240236165</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707104835.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120426s1995 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1046/j.1471-4159.1995.64052295.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ240236165</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Gu, Xinbin</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Regulation of Sialyltransferase Activities by Phosphorylation and Dephosphorylation</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Science Ltd</subfield><subfield code="c">1995</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract: The composition of tissue gangliosides is thought to result mainly from the active regulation and selective expression of specific enzymes responsible for their metabolism. In the last few years, we have purified several rat brain sialyltransferases to homogeneity; the availability of these highly purified enzymes enabled us to investigate their regulation and expression at the molecular level. Thus, we studied the regulation of sialyltransferase activities, in particular, CMP-NeuAc:GM1 and CMP-NeuAc:LacCer sialyltransferases by a phosphorylation/dephosphorylation mechanism. Protein kinase C was added to a standard enzyme assay mixture containing [γ-32P]ATP, and the activity of the enzyme was measured after various incubation times. We found that treatment of several sialyltransferases by protein kinase C decreased their activities in a time-dependent manner. Analyses of 32P-labeled amino acids revealed that the major phosphorylation site of CMP-NeuAc:GM1 α2→3 sialyltransferase (ST-IV) was serine and that for CMP-NeuAc:LacCer α2→3 sialyltransferase (ST-I) was primarily threonine. Partial recovery of the enzyme activity could be achieved by treatment of the phosphorylated sialyltransferases with rat brain protein phosphatase. We conclude that the activities of sialyltransferases can be modulated by protein kinase C and protein phosphatase and this may represent a potential regulatory mechanism for ganglioside biosynthesis.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2002</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2002||||||||||</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Sialyltransferases</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Preuß, Ute</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gu, Tianjue</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Yu, Robert K.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Journal of neurochemistry</subfield><subfield code="d">Oxford : Wiley-Blackwell, 1956</subfield><subfield code="g">64(1995), 5, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243927584</subfield><subfield code="w">(DE-600)2020528-4</subfield><subfield code="x">1471-4159</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:64</subfield><subfield code="g">year:1995</subfield><subfield code="g">number:5</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1046/j.1471-4159.1995.64052295.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">64</subfield><subfield code="j">1995</subfield><subfield code="e">5</subfield><subfield code="h">0</subfield></datafield></record></collection>
|
| score |
7.399295 |