| 1. |
- Arnell, Kai, et al.
(författare)
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Hydrocephalus
- 2008
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Ingår i: Pediatric surgery. - Berlin : Springer Verlag. - 9783540695592 ; , s. 418-426
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Bokkapitel (populärvet., debatt m.m.)
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| 2. |
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| 3. |
- Koomoa, Dana-Lynn T., et al.
(författare)
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Expression profile of PRAF2 in the human brain and enrichment in synaptic vesicles
- 2008
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Ingår i: Neuroscience Letters. - : Elsevier BV. - 0304-3940 .- 1872-7972. ; 436:2, s. 171-176
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Tidskriftsartikel (refereegranskat)abstract
- PRA1 domain family, member 2 (PRAF2) is a novel 19-kDa protein with a prenylated Rab acceptor 1 (PRA1) motif and four transmembrane domains. Our previous studies revealed that PRAF2 is highly expressed in the brain and serves as a candidate prognostic marker in neuroblastoma (NB). PRAF2 is related to proteins PRAF1 (PRA1, prenylin, Yip3) and PRAF3 (GTRAP3-18, JWA, Arl6-IP5), both of which are enriched in the brain and implicated in cellular transport and endo/exocytic vesicle trafficking. However, the function for PRAF2 remains unknown. In this study, we analyzed the distribution and localization of PRAF2 in the mature human brain using two new antibodies specific for the protein. Analysis by immunohistochemistry revealed that in the human cerebellum, the PRAF2 protein was strongly expressed in Purkinje cells and, more moderately, in cells of the molecular and the granular layers. In the cerebral cortex, hippocampus, and lateral ventricles, PRAF2 protein was detected in neuronal cells, but not in non-neuronal cells. Intriguingly, immunoblot analysis revealed that PRAF2 is enriched in synaptic vesicles (SVs) prepared from rat brains. The expression of PRAF2 in specific regions of the brain including SVs suggest an important physiological function for this novel protein, possibly by participating in multiple aspects of SV maturation, transport, and signal transmission.
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| 5. |
- Wester, Elisabet S, et al.
(författare)
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Erythroid urea transporter deficiency due to novel JK(null) alleles
- 2008
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Ingår i: Transfusion. - : Wiley. - 1537-2995 .- 0041-1132. ; 48:2, s. 365-372
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Tidskriftsartikel (refereegranskat)abstract
- BACKGROUND: The Kidd blood group antigens Jk(a) and Jk(b) are encoded by the red blood cell (RBC) urea transporter gene. Homozygosity for silent JK alleles results in the rare Jk(a-b-) phenotype. To date, seven JK(null) alleles have been identified, and of these, two are more frequent in the Polynesians and Finns. This study reports the identification of other JK(null) alleles in Jk(a-b-) individuals of different ethnic or geographic origins. STUDY DESIGN AND METHODS: Nine Jk(a-b-) samples and a sample from a Jk(a-b+) mother of a Jk(a+b-) baby were investigated. Polymerase chain reaction amplification and sequence analysis of the JK gene was performed. Western blotting and urea lysis were used to confirm Jk(a-b-) RBCs. RESULTS: Four novel alleles were identified: two different nonsense mutations, 202C > T (Gln68Stop) and 723delA (Ile262Stop) were identified on otherwise consensus JK*1 and JK*2 alleles, respectively. A missense mutation, 956C > T (Thr319Met), was identified in a JK*1 allele from an African-American and a JK*2 allele in two people of subcontinental Indian descent. Immunoblotting and urea lysis confirmed absence of JK glycoprotein in RBC membranes from a sample carrying the 956C > T mutation. Other previously described JK(null) mutations were found in samples of origins other than in which they were first identified. CONCLUSION: The molecular bases of the Jk(a-b-) phenotype are diverse and this is the first report of JK(null) alleles in individuals of African and subcontinental Indian descent. Although rare, these alleles should be taken into consideration when planning genotyping strategies for blood donors and patients.
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