ライフサイエンスコーパス: CaM KII

1 sitized to repeated cocaine was blocked by a CaM-KII inhibitor.

2 or UV light-induced apoptosis also lacked a CaM-KII response.

3 by either TNF or UV light, did not activate CaM-KII in response to these stimuli.

4 rom HEK-293 cells co-expressing an activated CaM-KII.

5 Coexpression in HEK-293 cells of activated CaM-KII with GluR1 did not affect the glutamate affinity

6 CaM-KIIN interacted only with activated CaM-KII (i.e., in the presence of Ca2+/CaM or after auto

7 as that of GluR1 coexpressed with activated CaM-KII in HEK-293 cells.

8 Colocalization of CaM-KIIN with activated CaM-KII was demonstrated in COS-7 cells transfected with

9 tates of two synaptic substrates for PKA and CaM KII, rabphilin and synapsin, are regulated different

10 ylation of syntaxin and SNAP-25 with PKC and CaM KII did not affect interactions with the synprint si

11 the synprint site indicate that the PKC- and CaM KII-mediated inhibition of binding involves multiple

12 ts arises from the induction of calcium- and CaM-KII-dependent mechanisms.

13 The Ser831 site is specific to GluR1, and CaM-KII did not phosphorylate or potentiate current in c

14 sibility of synergistic interactions between CaM-KII and protein kinase C in regulating synaptic plas

15 mutated at S831, the site phosphorylated by CaM-KII during long-term potentiation.

16 lepropionic acid-type glutamate receptors by CaM-KII, but not by protein kinase C, was blocked upon c

17 the mechanism of AMPA receptor regulation by CaM-KII and further strengthens the idea how calcium-dep

18 lar mechanism of AMPA receptor regulation by CaM-KII is examined here by a novel approach, silence an

19 ork provides evidence that ischemia disturbs CaM-KII distribution and activity in PSDf and this may l

20 ng specific peptide substrate and endogenous CaM-KII substrates.

21 ly regulated and indicate a primary role for CaM-KII in shaping and regulating interneuronal communic

22 yme, calmodulin-dependent protein kinase II (CaM KII).

23 calmodulin-dependent protein kinase type II (CaM KII) phosphorylated a recombinant his-tagged synprin

24 cium/calmodulin-dependent protein kinase II (CaM-KII) also prevented the augmented increase in dopami

25 Ca2+/CaM-dependent protein kinase II (CaM-KII) can phosphorylate and potentiate responses of a

26 for calmodulin-dependent protein kinase II (CaM-KII) in signal transduction leading to apoptosis.

27 Ca2+/Calmodulin-dependent protein kinase II (CaM-KII) in the fraction enriched in postsynaptic densit

28 (2+)/calmodulin-dependent protein kinase II (CaM-KII) is believed to be one of the major contributors

29 Ca2+/calmodulin-dependent protein kinase II (CaM-KII) regulates numerous physiological functions, inc

30 res activation of Ca2+/calmodulin-kinase II (CaM-KII), which phosphorylates Ser-831 in the GluR1 subu

31 and calmodulin-dependent protein kinase II (CaM-KII): (i) it correlated with the activation and auto

32 The observed changes in CaM-KII content did not represent general protein redist

33 modulin-dependent protein kinases II and IV (CaM-KII and CaM-KIV).

34 proteins that may interact with and modulate CaM-KII function, a yeast two-hybrid screen was performe

35 1-478), or only the autoregulatory domain of CaM KII (residues 281-315) was exchanged for residues 78

36 tes that the entire autoregulatory domain of CaM KII can replace that of smMLCK in its ability to pro

37 utoregulatory and oligomerization domains of CaM KII (residues 281-478) were substituted for residues

38 inhibitors of CaM-KII blocked activation of CaM-KII and prevented DNA fragmentation and death.

39 Activation of CaM-KII during apoptosis and inhibition of DNA fragmenta

40 Sustained activation of CaM-KII localized at the postsynaptic density results in

41 idly stimulated Ca2+-independent activity of CaM-KII in the monocytic leukemia, U937.

42 th the activation and autophosphorylation of CaM-KII, (ii) it was blocked by the CaM-KII inhibitor KN

43 c protein that bound the catalytic domain of CaM-KII alpha and beta and potently inhibited kinase act

44 ntiated by injection of an activated form of CaM-KII.

45 ide), was highly selective for inhibition of CaM-KII with little effect on CaM-KI, CaM-KIV, CaM-KK, p

46 a potent and specific cellular inhibitor of CaM-KII that may have an important role in the physiolog

47 , a potent and specific peptide inhibitor of CaM-KII, whereas the responses were potentiated by injec

48 Both inhibitors of CaM-KII and the protease inhibitors blocked activation o

49 Two mechanistically different inhibitors of CaM-KII blocked activation of CaM-KII and prevented DNA

50 The redistribution of CaM-KII coincided with gradual (up to 80%) reduction of

51 e occlusion and was followed by reduction of CaM-KII to 50% of control content one week after the ins

52 ough enhanced dendritic protein synthesis of CaM-KII and regulation of nuclear gene transcription by

53 h proteolytic activity functions upstream of CaM-KII.

54 osphorylation of the synprint site by PKC or CaM KII may serve as a biochemical switch for interactio

55 PKC or CaM KII phosphorylation of the synprint peptide also inh

56 rylation of the synprint peptide with PKC or CaM KII, but not PKA or PKG, strongly inhibited binding

57 lar Ca2+ release), a CaM-binding peptide, or CaM-KII/PKC pseudosubstrate peptides.

58 These results indicate that CaM-KII can mediate plasticity at glutamatergic synapses

59 ation of CaM-KII, (ii) it was blocked by the CaM-KII inhibitor KN-62, and (iii) its phosphorus-32 pep

60 In this study we have identified this CaM-KII regulatory site using deletion and site-specific

61 d inhibition of DNA fragmentation by the two CaM-KII inhibitors were reproduced in several other line

62 Likewise, when CaM-KII was infused into cells expressing GluR1, the Ser

63 ve identified a molecular mechanism by which CaM-KII potentiates AMPA-Rs.

64 egulatory domain of smMLCK was replaced with CaM KII residues 301-315, MK(CK301-315), were inactive i

65 ance states for GluR1, and coexpression with CaM-KII or a mutation of Ser-831 to Asp increased the co