ライフサイエンスコーパス: merosin

1 mice with complete or partial deficiency of merosin.

2 observed previously with purified placental merosin.

3 than on other substrata such as laminin and merosin.

4 ystroglycan binding to laminin-1, but not to merosin.

5 m unstable myotubes, express laminin but not merosin.

6 adients of retinal basal lamina proteins and merosin.

7 0 cpm/well) was similar to that measured for merosin (7440 +/- 970 cpm/well).

8 5I- alpha-dystroglycan to native laminin and merosin (a mixture of laminin-2 and -4) was also compare

9 On gradients of merosin, a significant alteration in the axonal growth d

10 o not express either protein, but laminin or merosin added to the culture medium induced their fusion

11 tion of the merosin-deficient cells with the merosin alpha 2 chain cDNA.

12 in vitro through cell transfection with the merosin alpha2 chain restored the normal localization of

13 their clonal variants to study the roles of merosin and laminin in myogenesis.

14 Finally, merosin appears to promote myotube stability by preventi

15 Po and merosin are required for normal myelination in the nervo

16 SAP binds to human laminin and merosin as well as mouse and rat laminins.

17 uscle alpha-dystroglycan, both laminin-1 and merosin binding to 120-kDa brain alpha-dystroglycan were

18 muscle alpha-dystroglycan, both laminin and merosin binding to purified brain alpha-dystroglycan was

19 inhibited 125I-alpha-dystroglycan binding to merosin by only 17 +/- 5.2%.

20 genes for the adhesion molecules Po, L1, and merosin cause severe abnormalities in nervous system dev

21 Exogenous merosin converted these myotubes to a stable phenotype,

22 d in congenital muscular dystrophy caused by merosin deficiency and provide in vitro models to furthe

23 Correction of merosin deficiency in vitro through cell transfection wi

24 cted most efficiently by transfection of the merosin-deficient cells with the merosin alpha 2 chain c

25 biopsy specimens from DMD, Ullrich CMD, and merosin-deficient CMD patients, all of which present hig

26 mbrane protein laminin-2/merosin suffer from merosin-deficient congenital muscular dystrophy (MCMD).

27 Merosin-deficient congenital muscular dystrophy type 1A

28 Merosin-deficient congenital muscular dystrophy type 1A

29 Merosin-deficient congenital muscular dystrophy type 1A

30 Merosin-deficient congenital muscular dystrophy type 1A

31 oblasts from patients with Bethlem myopathy, merosin-deficient congenital muscular dystrophy, LGMD2A,

32 g activity of residual laminins expressed in merosin-deficient dy/dy skeletal muscle was inhibited dr

33 tion of alpha7beta1 isoforms in myofibers of merosin-deficient human patients and mice, but not in dy

34 , limb-girdle muscular dystrophy, congenital merosin-deficient muscular dystrophy, and Duchenne muscu

35 molecule Bcl-2 also promoted the survival of merosin-deficient myotubes, but did not restore a normal

36 The clinical features in the 10 merosin-deficient patients were homogeneous, with severe

37 In the 'merosin-deficient' subgroup, which represents about half

38 r merosin in skeletal muscle; (b) indicate a merosin dependence for the accurate expression and membr

39 to mouse EHS laminin or to human laminin-2 (merosin), eliminating the alpha1, alpha2, beta1, and gam

40 The alpha2 chain of laminin-2 (merosin), encoded by a gene on chromosome 6q22, is defic

41 fuse efficiently to multinucleated myotubes, merosin expression is upregulated as a function of diffe

42 eviously that skeletal muscle fibers require merosin for survival and function.

43 alpha2-chain of laminin-2 (previously called merosin) has been shown by immunohistochemical and genet

44 Merosin immunocytochemistry was normal, and no abnormali

45 The human vessels expressed GLUT-1 and merosin, immunodiagnostic markers for infantile hemangio

46 ever, the precise nature of the functions of merosin in muscle remain unknown.

47 dies identify novel biological functions for merosin in myoblast fusion and muscle cell survival; fur

48 e a molecular basis for the critical role of merosin in myofiber survival; and (d) add new insights t

49 e restores the synthesis and localization of merosin in skeletal muscle, and greatly improves muscle

50 ta1D integrins as the de facto receptors for merosin in skeletal muscle; (b) indicate a merosin depen

51 ts to compensate fully for the deficiency of merosin in some forms of muscular dystrophy.

52 These results indicate that the absence of merosin in tissues other than the muscle, such as nervou

53 etal muscle showing that the alpha2 chain of merosin is reduced markedly and that the laminin alpha1

54 Merosin (laminin-2 and -4; alpha 2-beta 1/beta 2-gamma 1

55 istribution of agrin with that of laminin-1, merosin (laminin-2), neurofilament, and neural cell adhe

56 ha2 chain of the basement membrane component merosin (laminin-2/4) cause various forms of muscular dy

57 s specific for laminin-1; neither laminin-2 (merosin) nor laminin-11 (a synapse-specific isoform) are

58 e sarcoglycan complex and the alpha 2-chain (merosin) of laminin-2 in the extracellular matrix.

59 ults were confirmed by iodinated laminin and merosin overlay of electrophoretically separated and blo

60 rominent feature in a group of patients with merosin-positive congenital muscular dystrophy, where it

61 ion, analysis of the laminin alpha2 chain of merosin showed that this protein was expressed as a doub

62 psy samples for the assessment of laminin-2 (merosin) status in congenital muscular dystrophy.

63 1.2-coated magnetic beads and plated onto a merosin substrate.

64 onic or adult mice were placed on laminin or merosin substrates and the outgrowth of optic fibers was

65 ted retinal neurite extension on mixed agrin/merosin substrates.

66 t of the basement membrane protein laminin-2/merosin suffer from merosin-deficient congenital muscula

67 y heparin, whereas the binding of commercial merosin to skeletal muscle alpha-dystroglycan was only m

68 dle muscular dystrophy in whom an absence of merosin was noted on immunoblotting.

69 trate gradients of basal lamina proteins and merosin were similar but not identical, indicating that

70 alpha2 subunit of the protein laminin-2 (or merosin), which is unable to form a stable link between