scholarly journals Oligodeoxyadenylate stimulates the protein kinase activity of anti-DNA sIgA from human milk.

2002 ◽  
Vol 49 (1) ◽  
pp. 291-294 ◽  
Author(s):  
Yuri Kit ◽  
Elena Kuligina ◽  
Dimitry Semenov ◽  
Vladimir Richter

Preparations of anti-DNA sIgA were obtained from human milk by sequential chromatography on protein A-sepharose, DEAE-fractogel and DNA-cellulose. The influence of oligonucleotides on protein kinase activity was investigated. It was discovered that incubation of anti-DNA sIgA with oligodeoxyriboadenylate d(A)12 stimulates the phosphorylation of polypeptides of sIgA in the presence of [gamma-32P]ATP. The greatest was the incorporation of P into the sIgA H-chains. We also demonstrated stimulation of the casein kinase activity of anti-DNA sIgA by d(A)12. The stimulation of the protein kinase activity of anti-DNA sIgA by oligoriboadenylate r(A)12 was not detected.

Alcohol ◽  
2014 ◽  
Vol 48 (2) ◽  
pp. 123-132 ◽  
Author(s):  
Samir Mandal ◽  
Sibabrata Mukhopadhyay ◽  
Sukdeb Bandhopadhyay ◽  
Gargi Sen ◽  
Tuli Biswas

1988 ◽  
Vol 34 (1) ◽  
pp. 26-35 ◽  
Author(s):  
David H. Lovett ◽  
Michael Martin ◽  
Stuart Bursten ◽  
Marta Szamel ◽  
Diethard Gemsa ◽  
...  

Nature ◽  
1975 ◽  
Vol 254 (5498) ◽  
pp. 347-349 ◽  
Author(s):  
STEPHEN W. SPAULDING ◽  
GERARD N. BURROW

2001 ◽  
Vol 281 (4) ◽  
pp. H1532-H1544 ◽  
Author(s):  
Siegried Pelzer ◽  
Chicuong La ◽  
Dieter J. Pelzer

We compared the effects of cytosolic free magnesium (Mg[Formula: see text]) on L-type Ca2+ current ( I Ca,L) in patch-clamped guinea pig ventricular cardiomyocytes under basal conditions, after inhibition of protein phosphorylation, and after stimulation of cAMP-mediated phosphorylation. Basal I Ca,L density displayed a bimodal dependence on the concentration of Mg[Formula: see text]([Mg2+]i; 10−6–10−2 M), which changed significantly as cell dialysis progressed due to a pronounced and long-lasting rundown of I Ca,L in low-Mg2+ dialysates. Ten minutes after patch breakthrough, I Ca,L density (at +10 mV) in Mg[Formula: see text]-depleted cells ([Mg2+]i∼1 μM) was elevated, increased to a maximum at ∼20 μM [Mg2+]i, and declined steeply at higher [Mg2+]i. Treatment with the broad-spectrum protein kinase inhibitor K252a (10 μM) reduced I Ca,L density and abolished these effects of Mg[Formula: see text] except for a negative shift of I Ca,L-voltage relations with increasing [Mg2+]i. Maximal stimulation of cAMP-mediated phosphorylation occluded the Mg[Formula: see text]-induced stimulation of I Ca,L and prevented inhibitory effects of the ion at [Mg2+]i <1 mM but not at higher concentrations. These results show that the modulation of I Ca,L by Mg[Formula: see text] requires protein kinase activity and likely originates from interactions of the ion with proteins involved in the regulation of protein phosphorylation/dephosphorylation. Stimulatory effects of Mg[Formula: see text] on I Ca,L seem to increase the cAMP-mediated phosphorylation of Ca2+ channels, whereas inhibitory effects of Mg[Formula: see text] appear to curtail and/or reverse cAMP-mediated phosphorylation.


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