ライフサイエンスコーパス: alpha-syntrophin

1 urally more aberrant than those lacking only alpha-syntrophin.

2 e and transgenic mice expressing full-length alpha-syntrophin.

3 e sarcolemma by binding to the PDZ domain of alpha-syntrophin.

4 Alpha-syntrophin, a protein containing one PDZ domain an

5 ith targeted disruption of the gene encoding alpha-syntrophin (alpha-Syn(-/-)) that lack the perivasc

6 in brain and skeletal muscle of mice lacking alpha-syntrophin (alpha-Syn(-/-)).

7 ith targeted disruption of the gene encoding alpha-syntrophin (alpha-Syn) that demonstrate diminished

8 alpha-Syntrophin (alpha-syn), a scaffold protein, links

9 r DPC proteins, including beta-dystroglycan, alpha-syntrophin and alpha-dystrobrevin in mdx muscle.

10 We conclude that both alpha-syntrophin and beta2-syntrophin play distinct role

11 of nNOS by the dystrophin-associated protein alpha-syntrophin and may have implications for the devel

12 rough a PDZ domain-mediated interaction with alpha-syntrophin and suggest an important role for the D

13 The COOH-terminal half of alpha-syntrophin binds to dystrophin and related protein

14 The Delta PDZ alpha-syntrophin displaced endogenous alpha- and beta 1-

15 trophin's rod domain and the adaptor protein alpha-syntrophin for sarcolemmal targeting.

16 Thus, alpha-syntrophin has an important role in synapse format

17 vestigated the function of the PDZ domain of alpha-syntrophin in vivo by generating transgenic mouse

18 alpha-Syntrophin is a scaffolding adapter protein expres

19 trophin were masked by compensation from the alpha-syntrophin isoform, we crossed these mice with our

20 orrect the aberrant AChR distribution of the alpha-syntrophin knock-out mice.

21 led to associate with the DGC in brains from alpha-syntrophin knockout mice.

22 Transgenic mice expressing alpha-syntrophin lacking portions of the first pleckstri

23 ng full-length alpha-syntrophin or a mutated alpha-syntrophin lacking the PDZ domain (Delta PDZ).

24 and in transgenic mice expressing a mutated alpha-syntrophin lacking the PDZ domain (DeltaPDZ), both

25 in, but no rescue was observed in muscles of alpha-syntrophin mutants that also lacked beta1-syntroph

26 artial NMJ rescue was seen in the muscles of alpha-syntrophin mutants that expressed beta1-syntrophin

27 The full-length alpha-syntrophin, not the Delta PDZ form, reestablished

28 ire PDZ domain (DeltaPDZ) were bred onto the alpha-syntrophin null background.

29 this hypothesis, we performed experiments in alpha-syntrophin null mice and in transgenic mice expres

30 y impaired in the contracting muscles of the alpha-syntrophin null mice and transgenic DeltaPDZ mice

31 We have generated alpha-syntrophin null mice by targeted gene disruption t

32 sed these mice with our previously described alpha-syntrophin null mice to produce mice lacking both

33 J architecture that were observed in mdx and alpha-syntrophin null muscles.

34 l mutants, dystrophin-deficient mdx mice and alpha-syntrophin null mutants showed reductions in the c

35 oth transgenic mouse lines were bred with an alpha-syntrophin-null mouse which lacks sarcolemmal nNOS

36 ransgenic mouse lines expressing full-length alpha-syntrophin or a mutated alpha-syntrophin lacking t

37 on of muscle sodium channels, which bind the alpha-syntrophin PDZ domain in vitro, were not altered.

38 Mice lacking the alpha-syntrophin PDZ domain or either half of the PH1 do

39 epends on the presence of a dystrophin-bound alpha-syntrophin PDZ domain.

40 to a PH domain were found to be conserved in alpha-syntrophins' PH1 domains and absent in PH2 domains

41 emonstrated that Kir4.1 can bind directly to alpha-syntrophin, requiring the presence of the last thr

42 In addition, stable overexpression of alpha-syntrophin significantly increased alpha1D-AR prot

43 Alpha-syntrophin specifically recognized the C terminus

44 ng, because mice deficient in dystrophin and alpha-syntrophin, which localizes neuronal nitric oxide

45 so seen in mice lacking the scaffold protein alpha-syntrophin, which manifest reduced astrocyte water

46 We demonstrate that alpha-Syntrophin, which resides in nuclei of myocytes, f

47 We conclude that the PH1 and PDZ domains of alpha-syntrophin work in concert to facilitate the local