Phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase
Abstract The function of the uterine smooth muscle in gestation and parturition is affected by a variety of hormones and biomolecules, some of which alter the intracellular levels of cAMP and Ca2+. Since the activity of smooth muscle MLCK has been shown to be modulated by phosphorylation, the effect...
Ausführliche Beschreibung
Autor*in: |
---|
Format: |
E-Artikel |
---|---|
Sprache: |
Englisch |
Erschienen: |
1995 |
---|
Umfang: |
11 |
---|
Reproduktion: |
Springer Online Journal Archives 1860-2002 |
---|---|
Übergeordnetes Werk: |
in: Molecular and cellular biochemistry - 1973, 149-150(1995) vom: Jan., Seite 59-69 |
Übergeordnetes Werk: |
volume:149-150 ; year:1995 ; month:01 ; pages:59-69 ; extent:11 |
Links: |
---|
Katalog-ID: |
NLEJ198036485 |
---|
LEADER | 01000caa a22002652 4500 | ||
---|---|---|---|
001 | NLEJ198036485 | ||
003 | DE-627 | ||
005 | 20210705231833.0 | ||
007 | cr uuu---uuuuu | ||
008 | 070527s1995 xx |||||o 00| ||eng c | ||
035 | |a (DE-627)NLEJ198036485 | ||
040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
041 | |a eng | ||
245 | 1 | 0 | |a Phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase |
264 | 1 | |c 1995 | |
300 | |a 11 | ||
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 function of the uterine smooth muscle in gestation and parturition is affected by a variety of hormones and biomolecules, some of which alter the intracellular levels of cAMP and Ca2+. Since the activity of smooth muscle MLCK has been shown to be modulated by phosphorylation, the effect of this modification of pregnant sheep myometrium (psm) MLCK by the catalytic subunit of cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) was studied. In contrast to other smooth muscle MLCK reported, PKA incorporates 2.0–2.2 moles phosphate into a mole of psm MLCK both in the presence and absence of Ca2+-calmodulin. Modification of serine residues inhibited the activity of the enzyme. PKC also incorporated 2.0–2.1 moles of phosphate per mole psmMLCK under both conditions but had no effect on the MLCK activity. Sequential phosphorylation by PKC and PKA incorporated 3.8–4.1 moles phosphate suggesting that the amino acid residues modified by the two kinases are different. Phosphoamino acid analysis of the MLCK revealed that PKC phosphorylated serine and threonine residues. The double reciprocal plots of the enzyme activity and calmodulin concentrations showed that the Vmax of the reaction is not altered by phosphorylation by PKA but the calmodulin concentration require for half-maximal activation is increased about 4-fold. Only 10 out of 17 monoclonal antibodies to various regions of the turkey gizzard MLCK cross-reacted with psmMLCK suggesting structural differences between these enzymes. Comparison of the deduced amino acid sequence of the cDNA encoding the C-terminal half of the psmMLCK molecule showed that while cgMLCK and psmMLCK are highly homologous, a number of nonconservative substitutions are present, particularly near the PKA phosphrylation site B (S828). | ||
533 | |f Springer Online Journal Archives 1860-2002 | ||
700 | 1 | |a Pato, Mary D. |4 oth | |
700 | 1 | |a Kerc, Ewa |4 oth | |
700 | 1 | |a Lye, Stephen J. |4 oth | |
773 | 0 | 8 | |i in |t Molecular and cellular biochemistry |d 1973 |g 149-150(1995) vom: Jan., Seite 59-69 |w (DE-627)NLEJ188989099 |w (DE-600)2003615-2 |x 1573-4919 |7 nnns |
773 | 1 | 8 | |g volume:149-150 |g year:1995 |g month:01 |g pages:59-69 |g extent:11 |
856 | 4 | 0 | |u http://dx.doi.org/10.1007/BF01076564 |
912 | |a GBV_USEFLAG_U | ||
912 | |a ZDB-1-SOJ | ||
912 | |a GBV_NL_ARTICLE | ||
951 | |a AR | ||
952 | |d 149-150 |j 1995 |c 1 |h 59-69 |g 11 |
matchkey_str |
article:15734919:1995----::hshrltoadatasqecopennsepymtimy |
---|---|
hierarchy_sort_str |
1995 |
publishDate |
1995 |
allfields |
(DE-627)NLEJ198036485 DE-627 ger DE-627 rakwb eng Phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase 1995 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract The function of the uterine smooth muscle in gestation and parturition is affected by a variety of hormones and biomolecules, some of which alter the intracellular levels of cAMP and Ca2+. Since the activity of smooth muscle MLCK has been shown to be modulated by phosphorylation, the effect of this modification of pregnant sheep myometrium (psm) MLCK by the catalytic subunit of cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) was studied. In contrast to other smooth muscle MLCK reported, PKA incorporates 2.0–2.2 moles phosphate into a mole of psm MLCK both in the presence and absence of Ca2+-calmodulin. Modification of serine residues inhibited the activity of the enzyme. PKC also incorporated 2.0–2.1 moles of phosphate per mole psmMLCK under both conditions but had no effect on the MLCK activity. Sequential phosphorylation by PKC and PKA incorporated 3.8–4.1 moles phosphate suggesting that the amino acid residues modified by the two kinases are different. Phosphoamino acid analysis of the MLCK revealed that PKC phosphorylated serine and threonine residues. The double reciprocal plots of the enzyme activity and calmodulin concentrations showed that the Vmax of the reaction is not altered by phosphorylation by PKA but the calmodulin concentration require for half-maximal activation is increased about 4-fold. Only 10 out of 17 monoclonal antibodies to various regions of the turkey gizzard MLCK cross-reacted with psmMLCK suggesting structural differences between these enzymes. Comparison of the deduced amino acid sequence of the cDNA encoding the C-terminal half of the psmMLCK molecule showed that while cgMLCK and psmMLCK are highly homologous, a number of nonconservative substitutions are present, particularly near the PKA phosphrylation site B (S828). Springer Online Journal Archives 1860-2002 Pato, Mary D. oth Kerc, Ewa oth Lye, Stephen J. oth in Molecular and cellular biochemistry 1973 149-150(1995) vom: Jan., Seite 59-69 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:149-150 year:1995 month:01 pages:59-69 extent:11 http://dx.doi.org/10.1007/BF01076564 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 149-150 1995 1 59-69 11 |
spelling |
(DE-627)NLEJ198036485 DE-627 ger DE-627 rakwb eng Phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase 1995 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract The function of the uterine smooth muscle in gestation and parturition is affected by a variety of hormones and biomolecules, some of which alter the intracellular levels of cAMP and Ca2+. Since the activity of smooth muscle MLCK has been shown to be modulated by phosphorylation, the effect of this modification of pregnant sheep myometrium (psm) MLCK by the catalytic subunit of cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) was studied. In contrast to other smooth muscle MLCK reported, PKA incorporates 2.0–2.2 moles phosphate into a mole of psm MLCK both in the presence and absence of Ca2+-calmodulin. Modification of serine residues inhibited the activity of the enzyme. PKC also incorporated 2.0–2.1 moles of phosphate per mole psmMLCK under both conditions but had no effect on the MLCK activity. Sequential phosphorylation by PKC and PKA incorporated 3.8–4.1 moles phosphate suggesting that the amino acid residues modified by the two kinases are different. Phosphoamino acid analysis of the MLCK revealed that PKC phosphorylated serine and threonine residues. The double reciprocal plots of the enzyme activity and calmodulin concentrations showed that the Vmax of the reaction is not altered by phosphorylation by PKA but the calmodulin concentration require for half-maximal activation is increased about 4-fold. Only 10 out of 17 monoclonal antibodies to various regions of the turkey gizzard MLCK cross-reacted with psmMLCK suggesting structural differences between these enzymes. Comparison of the deduced amino acid sequence of the cDNA encoding the C-terminal half of the psmMLCK molecule showed that while cgMLCK and psmMLCK are highly homologous, a number of nonconservative substitutions are present, particularly near the PKA phosphrylation site B (S828). Springer Online Journal Archives 1860-2002 Pato, Mary D. oth Kerc, Ewa oth Lye, Stephen J. oth in Molecular and cellular biochemistry 1973 149-150(1995) vom: Jan., Seite 59-69 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:149-150 year:1995 month:01 pages:59-69 extent:11 http://dx.doi.org/10.1007/BF01076564 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 149-150 1995 1 59-69 11 |
allfields_unstemmed |
(DE-627)NLEJ198036485 DE-627 ger DE-627 rakwb eng Phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase 1995 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract The function of the uterine smooth muscle in gestation and parturition is affected by a variety of hormones and biomolecules, some of which alter the intracellular levels of cAMP and Ca2+. Since the activity of smooth muscle MLCK has been shown to be modulated by phosphorylation, the effect of this modification of pregnant sheep myometrium (psm) MLCK by the catalytic subunit of cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) was studied. In contrast to other smooth muscle MLCK reported, PKA incorporates 2.0–2.2 moles phosphate into a mole of psm MLCK both in the presence and absence of Ca2+-calmodulin. Modification of serine residues inhibited the activity of the enzyme. PKC also incorporated 2.0–2.1 moles of phosphate per mole psmMLCK under both conditions but had no effect on the MLCK activity. Sequential phosphorylation by PKC and PKA incorporated 3.8–4.1 moles phosphate suggesting that the amino acid residues modified by the two kinases are different. Phosphoamino acid analysis of the MLCK revealed that PKC phosphorylated serine and threonine residues. The double reciprocal plots of the enzyme activity and calmodulin concentrations showed that the Vmax of the reaction is not altered by phosphorylation by PKA but the calmodulin concentration require for half-maximal activation is increased about 4-fold. Only 10 out of 17 monoclonal antibodies to various regions of the turkey gizzard MLCK cross-reacted with psmMLCK suggesting structural differences between these enzymes. Comparison of the deduced amino acid sequence of the cDNA encoding the C-terminal half of the psmMLCK molecule showed that while cgMLCK and psmMLCK are highly homologous, a number of nonconservative substitutions are present, particularly near the PKA phosphrylation site B (S828). Springer Online Journal Archives 1860-2002 Pato, Mary D. oth Kerc, Ewa oth Lye, Stephen J. oth in Molecular and cellular biochemistry 1973 149-150(1995) vom: Jan., Seite 59-69 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:149-150 year:1995 month:01 pages:59-69 extent:11 http://dx.doi.org/10.1007/BF01076564 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 149-150 1995 1 59-69 11 |
allfieldsGer |
(DE-627)NLEJ198036485 DE-627 ger DE-627 rakwb eng Phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase 1995 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract The function of the uterine smooth muscle in gestation and parturition is affected by a variety of hormones and biomolecules, some of which alter the intracellular levels of cAMP and Ca2+. Since the activity of smooth muscle MLCK has been shown to be modulated by phosphorylation, the effect of this modification of pregnant sheep myometrium (psm) MLCK by the catalytic subunit of cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) was studied. In contrast to other smooth muscle MLCK reported, PKA incorporates 2.0–2.2 moles phosphate into a mole of psm MLCK both in the presence and absence of Ca2+-calmodulin. Modification of serine residues inhibited the activity of the enzyme. PKC also incorporated 2.0–2.1 moles of phosphate per mole psmMLCK under both conditions but had no effect on the MLCK activity. Sequential phosphorylation by PKC and PKA incorporated 3.8–4.1 moles phosphate suggesting that the amino acid residues modified by the two kinases are different. Phosphoamino acid analysis of the MLCK revealed that PKC phosphorylated serine and threonine residues. The double reciprocal plots of the enzyme activity and calmodulin concentrations showed that the Vmax of the reaction is not altered by phosphorylation by PKA but the calmodulin concentration require for half-maximal activation is increased about 4-fold. Only 10 out of 17 monoclonal antibodies to various regions of the turkey gizzard MLCK cross-reacted with psmMLCK suggesting structural differences between these enzymes. Comparison of the deduced amino acid sequence of the cDNA encoding the C-terminal half of the psmMLCK molecule showed that while cgMLCK and psmMLCK are highly homologous, a number of nonconservative substitutions are present, particularly near the PKA phosphrylation site B (S828). Springer Online Journal Archives 1860-2002 Pato, Mary D. oth Kerc, Ewa oth Lye, Stephen J. oth in Molecular and cellular biochemistry 1973 149-150(1995) vom: Jan., Seite 59-69 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:149-150 year:1995 month:01 pages:59-69 extent:11 http://dx.doi.org/10.1007/BF01076564 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 149-150 1995 1 59-69 11 |
allfieldsSound |
(DE-627)NLEJ198036485 DE-627 ger DE-627 rakwb eng Phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase 1995 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract The function of the uterine smooth muscle in gestation and parturition is affected by a variety of hormones and biomolecules, some of which alter the intracellular levels of cAMP and Ca2+. Since the activity of smooth muscle MLCK has been shown to be modulated by phosphorylation, the effect of this modification of pregnant sheep myometrium (psm) MLCK by the catalytic subunit of cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) was studied. In contrast to other smooth muscle MLCK reported, PKA incorporates 2.0–2.2 moles phosphate into a mole of psm MLCK both in the presence and absence of Ca2+-calmodulin. Modification of serine residues inhibited the activity of the enzyme. PKC also incorporated 2.0–2.1 moles of phosphate per mole psmMLCK under both conditions but had no effect on the MLCK activity. Sequential phosphorylation by PKC and PKA incorporated 3.8–4.1 moles phosphate suggesting that the amino acid residues modified by the two kinases are different. Phosphoamino acid analysis of the MLCK revealed that PKC phosphorylated serine and threonine residues. The double reciprocal plots of the enzyme activity and calmodulin concentrations showed that the Vmax of the reaction is not altered by phosphorylation by PKA but the calmodulin concentration require for half-maximal activation is increased about 4-fold. Only 10 out of 17 monoclonal antibodies to various regions of the turkey gizzard MLCK cross-reacted with psmMLCK suggesting structural differences between these enzymes. Comparison of the deduced amino acid sequence of the cDNA encoding the C-terminal half of the psmMLCK molecule showed that while cgMLCK and psmMLCK are highly homologous, a number of nonconservative substitutions are present, particularly near the PKA phosphrylation site B (S828). Springer Online Journal Archives 1860-2002 Pato, Mary D. oth Kerc, Ewa oth Lye, Stephen J. oth in Molecular and cellular biochemistry 1973 149-150(1995) vom: Jan., Seite 59-69 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:149-150 year:1995 month:01 pages:59-69 extent:11 http://dx.doi.org/10.1007/BF01076564 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 149-150 1995 1 59-69 11 |
language |
English |
source |
in Molecular and cellular biochemistry 149-150(1995) vom: Jan., Seite 59-69 volume:149-150 year:1995 month:01 pages:59-69 extent:11 |
sourceStr |
in Molecular and cellular biochemistry 149-150(1995) vom: Jan., Seite 59-69 volume:149-150 year:1995 month:01 pages:59-69 extent:11 |
format_phy_str_mv |
Article |
institution |
findex.gbv.de |
isfreeaccess_bool |
false |
container_title |
Molecular and cellular biochemistry |
authorswithroles_txt_mv |
Pato, Mary D. @@oth@@ Kerc, Ewa @@oth@@ Lye, Stephen J. @@oth@@ |
publishDateDaySort_date |
1995-01-01T00:00:00Z |
hierarchy_top_id |
NLEJ188989099 |
id |
NLEJ198036485 |
language_de |
englisch |
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">NLEJ198036485</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210705231833.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070527s1995 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ198036485</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="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1995</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">11</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 function of the uterine smooth muscle in gestation and parturition is affected by a variety of hormones and biomolecules, some of which alter the intracellular levels of cAMP and Ca2+. Since the activity of smooth muscle MLCK has been shown to be modulated by phosphorylation, the effect of this modification of pregnant sheep myometrium (psm) MLCK by the catalytic subunit of cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) was studied. In contrast to other smooth muscle MLCK reported, PKA incorporates 2.0–2.2 moles phosphate into a mole of psm MLCK both in the presence and absence of Ca2+-calmodulin. Modification of serine residues inhibited the activity of the enzyme. PKC also incorporated 2.0–2.1 moles of phosphate per mole psmMLCK under both conditions but had no effect on the MLCK activity. Sequential phosphorylation by PKC and PKA incorporated 3.8–4.1 moles phosphate suggesting that the amino acid residues modified by the two kinases are different. Phosphoamino acid analysis of the MLCK revealed that PKC phosphorylated serine and threonine residues. The double reciprocal plots of the enzyme activity and calmodulin concentrations showed that the Vmax of the reaction is not altered by phosphorylation by PKA but the calmodulin concentration require for half-maximal activation is increased about 4-fold. Only 10 out of 17 monoclonal antibodies to various regions of the turkey gizzard MLCK cross-reacted with psmMLCK suggesting structural differences between these enzymes. Comparison of the deduced amino acid sequence of the cDNA encoding the C-terminal half of the psmMLCK molecule showed that while cgMLCK and psmMLCK are highly homologous, a number of nonconservative substitutions are present, particularly near the PKA phosphrylation site B (S828).</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Springer Online Journal Archives 1860-2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Pato, Mary D.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kerc, Ewa</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lye, Stephen J.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Molecular and cellular biochemistry</subfield><subfield code="d">1973</subfield><subfield code="g">149-150(1995) vom: Jan., Seite 59-69</subfield><subfield code="w">(DE-627)NLEJ188989099</subfield><subfield code="w">(DE-600)2003615-2</subfield><subfield code="x">1573-4919</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:149-150</subfield><subfield code="g">year:1995</subfield><subfield code="g">month:01</subfield><subfield code="g">pages:59-69</subfield><subfield code="g">extent:11</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1007/BF01076564</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-SOJ</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">149-150</subfield><subfield code="j">1995</subfield><subfield code="c">1</subfield><subfield code="h">59-69</subfield><subfield code="g">11</subfield></datafield></record></collection>
|
series2 |
Springer Online Journal Archives 1860-2002 |
ppnlink_with_tag_str_mv |
@@773@@(DE-627)NLEJ188989099 |
format |
electronic Article |
delete_txt_mv |
keep |
collection |
NL |
remote_str |
true |
illustrated |
Not Illustrated |
issn |
1573-4919 |
topic_title |
Phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase |
format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
format_main_str_mv |
Text Zeitschrift/Artikel |
carriertype_str_mv |
zu |
author2_variant |
m d p md mdp e k ek s j l sj sjl |
hierarchy_parent_title |
Molecular and cellular biochemistry |
hierarchy_parent_id |
NLEJ188989099 |
hierarchy_top_title |
Molecular and cellular biochemistry |
isfreeaccess_txt |
false |
familylinks_str_mv |
(DE-627)NLEJ188989099 (DE-600)2003615-2 |
title |
Phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase |
spellingShingle |
Phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase |
ctrlnum |
(DE-627)NLEJ198036485 |
title_full |
Phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase |
journal |
Molecular and cellular biochemistry |
journalStr |
Molecular and cellular biochemistry |
lang_code |
eng |
isOA_bool |
false |
recordtype |
marc |
publishDateSort |
1995 |
contenttype_str_mv |
zzz |
container_start_page |
59 |
container_volume |
149-150 |
physical |
11 |
format_se |
Elektronische Aufsätze |
title_sort |
phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase |
title_auth |
Phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase |
abstract |
Abstract The function of the uterine smooth muscle in gestation and parturition is affected by a variety of hormones and biomolecules, some of which alter the intracellular levels of cAMP and Ca2+. Since the activity of smooth muscle MLCK has been shown to be modulated by phosphorylation, the effect of this modification of pregnant sheep myometrium (psm) MLCK by the catalytic subunit of cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) was studied. In contrast to other smooth muscle MLCK reported, PKA incorporates 2.0–2.2 moles phosphate into a mole of psm MLCK both in the presence and absence of Ca2+-calmodulin. Modification of serine residues inhibited the activity of the enzyme. PKC also incorporated 2.0–2.1 moles of phosphate per mole psmMLCK under both conditions but had no effect on the MLCK activity. Sequential phosphorylation by PKC and PKA incorporated 3.8–4.1 moles phosphate suggesting that the amino acid residues modified by the two kinases are different. Phosphoamino acid analysis of the MLCK revealed that PKC phosphorylated serine and threonine residues. The double reciprocal plots of the enzyme activity and calmodulin concentrations showed that the Vmax of the reaction is not altered by phosphorylation by PKA but the calmodulin concentration require for half-maximal activation is increased about 4-fold. Only 10 out of 17 monoclonal antibodies to various regions of the turkey gizzard MLCK cross-reacted with psmMLCK suggesting structural differences between these enzymes. Comparison of the deduced amino acid sequence of the cDNA encoding the C-terminal half of the psmMLCK molecule showed that while cgMLCK and psmMLCK are highly homologous, a number of nonconservative substitutions are present, particularly near the PKA phosphrylation site B (S828). |
abstractGer |
Abstract The function of the uterine smooth muscle in gestation and parturition is affected by a variety of hormones and biomolecules, some of which alter the intracellular levels of cAMP and Ca2+. Since the activity of smooth muscle MLCK has been shown to be modulated by phosphorylation, the effect of this modification of pregnant sheep myometrium (psm) MLCK by the catalytic subunit of cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) was studied. In contrast to other smooth muscle MLCK reported, PKA incorporates 2.0–2.2 moles phosphate into a mole of psm MLCK both in the presence and absence of Ca2+-calmodulin. Modification of serine residues inhibited the activity of the enzyme. PKC also incorporated 2.0–2.1 moles of phosphate per mole psmMLCK under both conditions but had no effect on the MLCK activity. Sequential phosphorylation by PKC and PKA incorporated 3.8–4.1 moles phosphate suggesting that the amino acid residues modified by the two kinases are different. Phosphoamino acid analysis of the MLCK revealed that PKC phosphorylated serine and threonine residues. The double reciprocal plots of the enzyme activity and calmodulin concentrations showed that the Vmax of the reaction is not altered by phosphorylation by PKA but the calmodulin concentration require for half-maximal activation is increased about 4-fold. Only 10 out of 17 monoclonal antibodies to various regions of the turkey gizzard MLCK cross-reacted with psmMLCK suggesting structural differences between these enzymes. Comparison of the deduced amino acid sequence of the cDNA encoding the C-terminal half of the psmMLCK molecule showed that while cgMLCK and psmMLCK are highly homologous, a number of nonconservative substitutions are present, particularly near the PKA phosphrylation site B (S828). |
abstract_unstemmed |
Abstract The function of the uterine smooth muscle in gestation and parturition is affected by a variety of hormones and biomolecules, some of which alter the intracellular levels of cAMP and Ca2+. Since the activity of smooth muscle MLCK has been shown to be modulated by phosphorylation, the effect of this modification of pregnant sheep myometrium (psm) MLCK by the catalytic subunit of cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) was studied. In contrast to other smooth muscle MLCK reported, PKA incorporates 2.0–2.2 moles phosphate into a mole of psm MLCK both in the presence and absence of Ca2+-calmodulin. Modification of serine residues inhibited the activity of the enzyme. PKC also incorporated 2.0–2.1 moles of phosphate per mole psmMLCK under both conditions but had no effect on the MLCK activity. Sequential phosphorylation by PKC and PKA incorporated 3.8–4.1 moles phosphate suggesting that the amino acid residues modified by the two kinases are different. Phosphoamino acid analysis of the MLCK revealed that PKC phosphorylated serine and threonine residues. The double reciprocal plots of the enzyme activity and calmodulin concentrations showed that the Vmax of the reaction is not altered by phosphorylation by PKA but the calmodulin concentration require for half-maximal activation is increased about 4-fold. Only 10 out of 17 monoclonal antibodies to various regions of the turkey gizzard MLCK cross-reacted with psmMLCK suggesting structural differences between these enzymes. Comparison of the deduced amino acid sequence of the cDNA encoding the C-terminal half of the psmMLCK molecule showed that while cgMLCK and psmMLCK are highly homologous, a number of nonconservative substitutions are present, particularly near the PKA phosphrylation site B (S828). |
collection_details |
GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE |
title_short |
Phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase |
url |
http://dx.doi.org/10.1007/BF01076564 |
remote_bool |
true |
author2 |
Pato, Mary D. Kerc, Ewa Lye, Stephen J. |
author2Str |
Pato, Mary D. Kerc, Ewa Lye, Stephen J. |
ppnlink |
NLEJ188989099 |
mediatype_str_mv |
z |
isOA_txt |
false |
hochschulschrift_bool |
false |
author2_role |
oth oth oth |
up_date |
2024-07-06T10:22:04.744Z |
_version_ |
1803824738855813120 |
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">NLEJ198036485</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210705231833.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070527s1995 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ198036485</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="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1995</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">11</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 function of the uterine smooth muscle in gestation and parturition is affected by a variety of hormones and biomolecules, some of which alter the intracellular levels of cAMP and Ca2+. Since the activity of smooth muscle MLCK has been shown to be modulated by phosphorylation, the effect of this modification of pregnant sheep myometrium (psm) MLCK by the catalytic subunit of cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) was studied. In contrast to other smooth muscle MLCK reported, PKA incorporates 2.0–2.2 moles phosphate into a mole of psm MLCK both in the presence and absence of Ca2+-calmodulin. Modification of serine residues inhibited the activity of the enzyme. PKC also incorporated 2.0–2.1 moles of phosphate per mole psmMLCK under both conditions but had no effect on the MLCK activity. Sequential phosphorylation by PKC and PKA incorporated 3.8–4.1 moles phosphate suggesting that the amino acid residues modified by the two kinases are different. Phosphoamino acid analysis of the MLCK revealed that PKC phosphorylated serine and threonine residues. The double reciprocal plots of the enzyme activity and calmodulin concentrations showed that the Vmax of the reaction is not altered by phosphorylation by PKA but the calmodulin concentration require for half-maximal activation is increased about 4-fold. Only 10 out of 17 monoclonal antibodies to various regions of the turkey gizzard MLCK cross-reacted with psmMLCK suggesting structural differences between these enzymes. Comparison of the deduced amino acid sequence of the cDNA encoding the C-terminal half of the psmMLCK molecule showed that while cgMLCK and psmMLCK are highly homologous, a number of nonconservative substitutions are present, particularly near the PKA phosphrylation site B (S828).</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Springer Online Journal Archives 1860-2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Pato, Mary D.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kerc, Ewa</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lye, Stephen J.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Molecular and cellular biochemistry</subfield><subfield code="d">1973</subfield><subfield code="g">149-150(1995) vom: Jan., Seite 59-69</subfield><subfield code="w">(DE-627)NLEJ188989099</subfield><subfield code="w">(DE-600)2003615-2</subfield><subfield code="x">1573-4919</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:149-150</subfield><subfield code="g">year:1995</subfield><subfield code="g">month:01</subfield><subfield code="g">pages:59-69</subfield><subfield code="g">extent:11</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1007/BF01076564</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-SOJ</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">149-150</subfield><subfield code="j">1995</subfield><subfield code="c">1</subfield><subfield code="h">59-69</subfield><subfield code="g">11</subfield></datafield></record></collection>
|
score |
7.3994884 |