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001-es BibID:	BIBFORM074060
Első szerző:	Bátori Róbert Károly (biológus, biotechnológus)
Cím:	Differential mechanisms of adenosine- and ATpγS-induced microvascular endothelial barrier strengthening / Róbert Bátori, Sanjiv Kumar, Zsuzsanna Bordán, Mary Cherian-Shaw, Anita Kovács-Kása, Justin A. MacDonald, David J. R. Fulton, Ferenc Erdődi, Alexander D. Verin
Dátum:	2019
ISSN:	0021-9541
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban Endothelial barrier
Megjelenés:	Journal of Cellular Physiology. - 234 : 5 (2019), p. 5863-5879. -
További szerzők:	Kumar, Sanjiv Bordán Zsuzsanna Cherian-Shaw, Mary Kovács-Kása Anita (1983-) MacDonald, Justin A. Fulton, David Erdődi Ferenc (1953-) (biokémikus) Verin, Alexander
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM028725
Első szerző:	Murányi Andrea (biokémikus)
Cím:	Phosphorylation of the myosin phosphatase target subunit by integrin-linked kinase / Andrea Murányi, Justin A. MacDonald, Jing Ti Deng, David P. Wilson, Timothy A. J. Haystead, Michael P. Walsh, Ferenc Erdődi, Enikő Kiss, Yue Wu, David J. Hartshorne
Dátum:	2002
ISSN:	0264-6021
Megjegyzések:	A mechanism proposed for regulation of myosin phosphatase (MP) activity is phosphorylation of the myosin phosphatase target subunit (MYPT1). Integrin-linked kinase (ILK) is associated with the contractile machinery and can phosphorylate myosin at the myosin light-chain kinase sites. The possibility that ILK may also phosphorylate and regulate MP was investigated. ILK was associated with the MP holoenzyme, shown by Western blots and in-gel kinase assays. MYPT1 was phosphorylated by ILK and phosphorylation sites in the N- and C-terminal fragments of MYPT1 were detected. From sequence analyses, three sites were identified: a primary site at Thr(709), and two other sites at Thr(695) and Thr(495). One of the sites for cAMP-dependent protein kinase (PKA) was Ser(694). Assays with the catalytic subunit of type 1 phosphatase indicated that only the C-terminal fragment of MYPT1 phosphorylated by zipper-interacting protein kinase, and ILK inhibited activity. The phosphorylated N-terminal fragment activated phosphatase activity and phosphorylation by PKA was without effect. Using full-length MYPT1 constructs phosphorylated by various kinases it was shown that Rho kinase gave marked inhibition; ILK produced an intermediate level of inhibition, which was considerably reduced for the Thr(695)-->Ala mutant; and PKA had no effect. In summary, phosphorylation of the various sites indicated that Thr(695) was the major inhibitory site, Thr(709) had only a slight inhibitory effect and Ser(694) had no effect. The findings that ILK phosphorylated both MYPT1 and myosin and the association of ILK with MP suggest that ILK may influence cytoskeletal structure or function.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban külföldön készült közlemény
Megjelenés:	Biochemical Journal. - 366 (2002), p. 211-216. -
További szerzők:	MacDonald, Justin A. Deng, Jing Ti Wilson, David P. Haystead, Timothy A. J. Walsh, Michael P. Kiss Enikő Wu, Yue Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus)
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001-es BibID:	BIBFORM028720
Első szerző:	Wooldridge, Anne A.
Cím:	Smooth muscle phosphatase is regulated in vivo by exclusion of phosphorylation of threonine 696 of MYPT1 by phosphorylation of Serine 695 in response to cyclic nucleotides / Anne A. Wooldridge, Justin A. MacDonald, Ferenc Erdodi, Chaoyu Ma, Meredith A. Borman, David J. Hartshorne, Timothy A. J. Haystead
Dátum:	2004
ISSN:	0021-9258
Megjegyzések:	Regulation of smooth muscle myosin phosphatase (SMPP-1M) is thought to be a primary mechanism for explaining Ca(2+) sensitization/desensitization in smooth muscle. Ca(2+) sensitization induced by activation of G protein-coupled receptors acting through RhoA involves phosphorylation of Thr-696 (of the human isoform) of the myosin targeting subunit (MYPT1) of SMPP-1M inhibiting activity. In contrast, agonists that elevate intracellular cGMP and cAMP promote Ca(2+) desensitization in smooth muscle through apparent activation of SMPP-1M. We show that cGMP-dependent protein kinase (PKG)/cAMP-dependent protein kinase (PKA) efficiently phosphorylates MYPT1 in vitro at Ser-692, Ser-695, and Ser-852 (numbering for human isoform). Although phosphorylation of MYPT1 by PKA/PKG has no direct effect on SMPP-1M activity, a primary site of phosphorylation is Ser-695, which is immediately adjacent to the inactivating Thr-696. In vitro, phosphorylation of Ser-695 by PKA/PKG appeared to prevent phosphorylation of Thr-696 by MYPT1K. In ileum smooth muscle, Ser-695 showed a 3-fold increase in phosphorylation in response to 8-bromo-cGMP. Addition of constitutively active recombinant MYPT1K to permeabilized smooth muscles caused phosphorylation of Thr-696 and Ca(2+) sensitization; however, this phosphorylation was blocked by preincubation with 8-bromo-cGMP. These findings suggest a mechanism of Ca(2+) desensitization in smooth muscle that involves mutual exclusion of phosphorylation, whereby phosphorylation of Ser-695 prevents phosphorylation of Thr-696 and therefore inhibition of SMPP-1M.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban külföldön készült közlemény
Megjelenés:	Journal of Biological Chemistry. - 279 : 33 (2004), p. 34496-34504. -
További szerzők:	MacDonald, Justin A. Ma, Chaoyu Borman, Meredith A. Hartshorne, David J. Haystead, Timothy A. J. Erdődi Ferenc (1953-) (biokémikus)
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