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A Novel N14Y Mutation in Connexin26 in Keratitis-Ichthyosis-Deafness Syndrome: Analyses of Altered Gap Junctional Communication and Molecular Structure of N Terminus of Mutated Connexin26

Arita, Ken ; Akiyama, Masashi ; Aizawa, Tomoyasu ; Umetsu, Yoshitaka ; Segawa, Ikuo ; Goto, Maki ; Sawamura, Daisuke ; Demura, Makoto ; Kawano, Keiichi ; Shimizu, Hiroshi

The American journal of pathology, 2006-08, Vol.169 (2), p.416-423 [Periódico revisado por pares]

Bethesda, MD: ASIP

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Título:
A Novel N14Y Mutation in Connexin26 in Keratitis-Ichthyosis-Deafness Syndrome: Analyses of Altered Gap Junctional Communication and Molecular Structure of N Terminus of Mutated Connexin26
Autor: Arita, Ken ; Akiyama, Masashi ; Aizawa, Tomoyasu ; Umetsu, Yoshitaka ; Segawa, Ikuo ; Goto, Maki ; Sawamura, Daisuke ; Demura, Makoto ; Kawano, Keiichi ; Shimizu, Hiroshi
Assuntos: 3T3 Cells ; Amino Acids - chemistry ; Animals ; Base Sequence ; Biological and medical sciences ; Cells, Cultured ; Child, Preschool ; Circular Dichroism ; Complex syndromes ; Connexin 26 ; Connexins - chemistry ; Connexins - genetics ; Deafness - genetics ; DNA Mutational Analysis ; Female ; Gap Junctions - pathology ; Gap Junctions - ultrastructure ; Humans ; Ichthyosis - genetics ; Investigative techniques, diagnostic techniques (general aspects) ; Keratinocytes - cytology ; Keratinocytes - pathology ; Keratitis - genetics ; Medical genetics ; Medical sciences ; Mice ; Molecular Sequence Data ; Mutant Proteins - chemistry ; Mutant Proteins - genetics ; Mutation - genetics ; Nuclear Magnetic Resonance, Biomolecular ; Pathology. Cytology. Biochemistry. Spectrometry. Miscellaneous investigative techniques ; Regular ; Skin - cytology ; Skin - pathology ; Skin - ultrastructure ; Syndrome
É parte de: The American journal of pathology, 2006-08, Vol.169 (2), p.416-423
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Descrição: Connexins (Cxs) are transmembranous proteins that connect adjacent cells via channels known as gap junctions. The N-terminal 21 amino acids of Cx26 are located at the cytoplasmic side of the channel pore and are thought to be essential for the regulation of channel selectivity. We have found a novel mutation, N14Y, in the N-terminal domain of Cx26 in a case of keratitis-ichthyosis-deafness syndrome. Reduced gap junctional intercellular communication was observed in the patient's keratinocytes by the dye transfer assay using scrape-loading methods. The effect of this mutation on molecular structure was investigated using synthetic N-terminal peptides from both wild-type and mutated Cx26. Two-dimensional (1)H nuclear magnetic resonance and circular dichroism measurements demonstrated that the secondary structures of these two model peptides are similar to each other. However, several novel nuclear Overhauser effect signals appeared in the N14Y mutant, and the secondary structure of the mutant peptide was more susceptible to induction of 2,2,2-trifluoroethanol than wild type. Thus, it is likely that the N14Y mutation induces a change in local structural flexibility of the N-terminal domain, which is important for exerting the activity of the channel function, resulting in impaired gap junctional intercellular communication.
Editor: Bethesda, MD: ASIP
Idioma: Inglês

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A Novel N14Y Mutation in Connexin26 in Keratitis-Ichthyosis-Deafness Syndrome: Analyses of Altered Gap Junctional Communication and Molecular Structure of N Terminus of Mutated Connexin26

Arita, Ken ; Akiyama, Masashi ; Aizawa, Tomoyasu ; Umetsu, Yoshitaka ; Segawa, Ikuo ; Goto, Maki ; Sawamura, Daisuke ; Demura, Makoto ; Kawano, Keiichi ; Shimizu, Hiroshi

Bethesda, MD: ASIP

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