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001-es BibID:	BIBFORM029385
Első szerző:	Bárány Katalin
Cím:	Phosphorylation and dephosphorylation of distinct sites of the 20,000-Dalton myosin light chain in smooth muscle / Kate Bárány, Mary D. Pato, Anikó Rokolya, Ferenc Erdődi, Joseph Di Salvo, Michael Bárány
Dátum:	1989
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban külföldön készült közlemény
Megjelenés:	Advances in Protein Phosphatases. - 5 (1989), p. 517-534. -
További szerzők:	Pato, Mary D. Rokolya Anikó Salvo, Joseph Di Bárány Mihály Erdődi Ferenc (1953-) (biokémikus)
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM029045
Első szerző:	Erdődi Ferenc (biokémikus)
Cím:	Effect of okadaic acid on phosphorylation-dephosphorylation of myosin light chain in aortic smooth muscle homogenate / Ferenc Erdődi, Anikó Rokolya, Joseph Di Salvo, Michael Bárány, Kate Bárány
Dátum:	1988
ISSN:	0006-291X
Megjegyzések:	Myosin light chain phosphorylation in aortic smooth muscle homogenate reached a maximal level of 0.75 mol phosphate/mol light chain, and then declined. Addition of okadaic acid led to a sustained phosphorylation level of 1.7 mol/mol. In the absence of okadaic acid, phosphorylation was predominantly due to myosin light chain kinase, whereas in the presence of okadaic acid both myosin light chain kinase and protein kinase C were involved in phosphorylation. Okadaic acid inhibited dephosphorylation of the distinct sites in LC phosphorylated by either myosin light chain kinase or protein kinase C, suggesting that it exerts its effect through inhibition of myosin light chain phosphatases present in aortic homogenate.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban külföldön készült közlemény
Megjelenés:	Biochemical and Biophysical Research Communications. - 153 : 1 (1988), p. 156-161. -
További szerzők:	Rokolya Anikó Salvo, Joseph Di Bárány Mihály Bárány Katalin
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM029044
Első szerző:	Erdődi Ferenc (biokémikus)
Cím:	Phosphorylation of the 20,000-Da myosin light chain isoforms of arterial smooth muscle by myosin light chain kinase and protein kinase C / Ferenc Erdődi, Anikó Rokolya, Michael Bárány, Kate Bárány
Dátum:	1988
ISSN:	0003-9861
Megjegyzések:	Phosphorylation of myosin light chain (LC) isoforms in arterial actomyosin can be induced by endogenous kinases upon addition of Mg2+ and ATP. The extent of phosphorylation in the presence of 2 mM ethylene glycol bis(beta-aminoethyl ether)N,N'-tetraacetic acid (EGTA), 0.2 mM Ca2+, or 0.2 mM Ca2+ plus calmodulin is 1.6, 2.1, and 2.3 mol phosphate/mol LC, respectively. Two-dimensional gel electrophoresis of actomyosin shows that the LC isoforms may be mono-, di-, and triphosphorylated. Tryptic phosphopeptide mapping of LC indicates that the radioactive phosphate is distributed to six peptides referred to as A through F. Phosphoamino acid analyses and the phosphopeptide maps of isolated LC, phosphorylated by either purified myosin light chain kinase or protein kinase C, reveal that myosin light chain kinase phosphorylates a serine residue in peptides A and B, and threonine plus serine residues in peptides C and D. Peptides E and F are phosphorylated by protein kinase C in serine and threonine residues, respectively. In actomyosin, with EGTA, phosphorylation of peptides E and F proceeds while phosphorylation of peptides A, B, C, and D is inhibited. Ca2+ and calmodulin enhance the phosphorylation of peptides A, B, C, and D, while phosphorylation of peptides E and F is decreased. In isolated LC, myosin light chain kinase preferentially phosphorylates the peptides A and B over C and D. Phosphorylation of peptides E and F in LC by protein kinase C promotes additional phosphorylation of peptides C and D by myosin light chain kinase, whereas phosphorylation of peptides A and B is diminished. The present data suggest that the phosphorylation of distinct sites in arterial myosin light chain by myosin light chain kinase and protein kinase C is interrelated.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban külföldön készült közlemény
Megjelenés:	Archives of Biochemistry And Biophysics. - 266 : 2 (1988), p. 583-591. -
További szerzők:	Rokolya Anikó Bárány Mihály Bárány Katalin
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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001-es BibID:	BIBFORM029042
Első szerző:	Erdődi Ferenc (biokémikus)
Cím:	Dephosphorylation of distinct sites in myosin light chain by two types of phosphatase in aortic smooth muscle / Ferenc Erdődi, Anikó Rokolya, Michael Bárány, Kate Bárány
Dátum:	1989
ISSN:	0167-4889
Megjegyzések:	Two types of myosin light chain phosphatase from aortic smooth muscle extract were separated by chromatography on heparin-agarose. The phosphatase which appeared in the flow-through fractions had low activity on actomyosin, its apparent molecular mass was 260 kDa and upon ethanol treatment it generated a catalytic subunit with an apparent molecular mass of 36-39 kDa as determined by gel filtration. This phosphatase preferentially dephosphorylated the alpha-subunit of phosphorylase kinase and its phosphorylase phosphatase activity was not inhibited by heparin, inhibitor-1 or inhibitor-2. The phosphatase retained by heparin-agarose had high activity on actomyosin, its apparent molecular mass was 150 kDa and upon ethanol treatment it generated a catalytic subunit with an apparent molecular mass of 39-42 kDa. It preferentially dephosphorylated the beta-subunit of phosphorylase kinase and its phosphorylase phosphatase activity was not inhibited by heparin, inhibitor-1 or inhibitor-2. Myosin light chain was phosphorylated by myosin light chain kinase in peptides AB (Ser-P) and CD (Thr-P), and/or by protein kinase C in peptides E (Ser-P) and F (Thr-P) as determined by one-dimensional phosphopeptide mapping. The catalytic subunit of heparin-agarose flow-through phosphatase preferentially dephosphorylated peptide F over peptides AB, CD and E in both isolated light chain and actomyosin. The catalytic subunit of heparin-agarose bound phosphatase could effectively dephosphorylate all sites in isolated light chain, whereas it was less effective on dephosphorylation of peptide E in actomyosin.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban külföldön készült közlemény Myosin light chain Multiple phosphorylation Myosin light chain phosphatase Aortic smooth muscle
Megjelenés:	Biochimica et Biophysica Acta (BBA). Molecular Cell Research. - 1011 : 1 (1989), p. 67-74. -
További szerzők:	Rokolya Anikó Bárány Mihály Bárány Katalin
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI Szerző által megadott URL
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