anti-Gap Junction Protein, gamma 2, 47kDa (GJC2) Antikörper

Mouse (Murine) Gap Junction Protein, gamma 2, 47kDa (GJC2) Interaktionspartner

1. This study found the much more severe disruption of the blood-spinal cord barrier in the Cx47KO, than in EAE mice.

2. Main findings are that i) Cx47 is involved in the reversal of acute increases in serum triglycerides, ii) serum lipid levels of mice on chow but not high-cholesterol diet are affected by Cx47 and iii) Cx47-deficiency tends to increase plaque size but decreases macrophage content of diet-induced atherosclerotic plaques. Results show that Cx47-deficient mice do not display an overt lymphatic phenotype.

3. Data show that segregation of Foxc2 and NFATc1 transcription factor is closely associated with the highly polarized expression of connexins Cx37, Cx43, and Cx47.

4. This study showed that Connexin47 alterations after neural precursor cells transplantation in experimental autoimmune encephalomyelitis.

5. This study demonistrated that Cx30/Cx47 double-deficient mice has the functional role of both connexins for interastrocytic, interoligodendrocytic, and panglial coupling, and show that both connexins are required for maintenance of myelin.

6. PMLD1 (Pelizaeus-Merzbacher-like disease 1) is caused by the loss of Cx47 channel function that results in impaired panglial coupling in white matter tissue.

7. oligodendrocyte-astrocyte gap junction coupling in Cx32 or Cx47 knockout mice. In the neocortex, oligodendrocytes appeared to be directly and exclusively coupled to astrocytes; Cx47, but not Cx32, was required for O:A coupling.

8. oligodendrocytes in white matter form a functional syncytium predominantly among each other dependent on Cx47 and Cx32 expression, while astrocytic connexins expression can promote the size of this network

9. Cx47-deficient mice revealed a vacuolation of nerve fibers at the site of the optic nerve where axons are first contacted by oligodendrocytes and myelination starts; Cx32/Cx47-double-deficient mice developed action tremor and died ca 51 d after birth

10. Mice lacking either Cx47 or Cx32 are viable but mice lacking both connexins die by postnatal week 6 from CNS myelin sheath abnormalities, vacuolation, enlarged periaxonal collars, oligodendrocyte cell death, and axonal loss

11. All oligodendrocytes appear to express Cx47, which is largely restricted to their perikarya

12. These results demonstrate MUPP1 at O/A gap junctions and Cx47-dependent targeting of connexins to the plasma membranes of oligodendrocyte somata.

Human Gap Junction Protein, gamma 2, 47kDa (GJC2) Interaktionspartner

1. Connexin 43-connexin 47 channels are important for astrocyte/ oligodendrocyte cross-talk in myelination and demyelination. (Review)

2. Different mutations in the Cx47 lead to discrepant activation of unfolded protein response (UPR) pathway, which encouraged apoptotic cell death at different levels. Inappropriate activation of UPR may play important roles in the pathophysiology of Pelizaeus-Merzbacher-Like Disease.

3. GJC2 promoter region mutation screening should be included in the evaluation of patients with unexplained hypomyelinating leukodystrophies.

4. we provide evidence that a mutation in GJA1 leads not only to ODD as already described in the literature, but can also lead to lymphoedema as an associated feature.

5. a novel homozygous mutation in GJC2 was identified in a 21-year-old female patient with Pelizaeus-Merzbacher-like disease

6. This study identified novel chromosomal rearrangements proximal and distal to, and exclusive of the PLP1 gene, showed equal frequencies of PLP1 and GJA12/GJC2 mutations

7. Most of the Pelizaeus-Merzbacher-like disease (PMLD)-linked Cx47 mutants disrupt Cx47/Cx47 and Cx47/Cx43 GJ function in the glial network, which may play a role in leading to PMLD symptoms

8. the extremely severe clinical Pelizaeus-Merzbacher-like disease form likely correlates with the predicted impairment of gap junction channel assembly resulting from the detrimental effect of the new p.Glu260Lys mutant allele on Cx47 protein

9. founder mutation c.-167A>G localized in the GJC2 protein promoter region in patients with Pelizaeus Merzbacher disease and Pelizaeus Merzbacher like disease

10. Cx47 mutations were identified in individuals having secondary lymphedema following breast cancer treatment; these novel mutations are dysfunctional and provide evidence that altered gap junction function leads to lymphedema

11. We report the identification of the GJC2 promoter mutation (c.-167A>G) in nine patients from three unrelated Pakistani families with Pelizaeus-Merzbacher-like disease. Linkage analysis was consistent with a likely founder effect of this mutation

12. Mutations within the GJC2 gene are associated with primary lymphoedema.

13. The identification of GJC2 mutations as a cause of primary lymphedema

14. GJA12 gene mutations reported from two Chinese Pelizaeus-Merzbacher-like disease patients

15. She carried no GJA12 mutations. These facts suggested that this disease is a novel, autosomal recessive hypomyelinating leukodystrophy.

16. Patients from one family carrying a homozygous frameshift mutation in GJA12 presenting with nystagmus and brain demyelinating disease.

17. GJA12 mutations are the initiaial genetic test in patients with consanguineous parents with Pelizaeus-Merzbacher-like disease.

18. study shows the Cx47 mutants associated with Pelizaeus-Merzbacher-like disease likely disrupt the gap junction coupling between astrocytes and oligodendrocytes

19. The clinical phenotype of patients with a GJA12 mutation was evaluated and is overall comparable to the clinical features seen in mild forms of PLP1-related disorder but with better cognition and earlier signs of axonal degeneration.

20. GJA12 alterations are a rare cause of Pelizaeus-Merzbacher-like disease even after extending the screening for copy number variation and for mutations in the non-coding region of GJA12.

Cow (Bovine) Gap Junction Protein, gamma 2, 47kDa (GJC2) Interaktionspartner

1. AQP-0 and connexins can be segregated in the membrane by protein-lipid interactions as modified by AQP-0 homo-oligomerization