Characterization of a Human and Murine Gene (CLCN3) Sharing Similarities to Voltage-Gated Chloride Channels and to a Yeast Integral Membrane Protein

Borsani, Giuseppe; Rugarli, Elena I.; Taglialatela, Maurizio; Wong, Calvin J.H.; Ballabio, Andrea

doi:10.1006/geno.1995.1015

Cited by 72 publications

(61 citation statements)

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“…Investigation into the expression levels of both mRNA and protein in various tissues has led to conflicting results (24,33,36,60). Expression of cloned ClC-3 either from human (32,36,43), rat (24,33,34), or guinea pig (16,27,28) has led to differing biophysical and pharmacological properties or the inability to detect expressed ClC-3 chloride currents (36,37,61). There is also contradictory data as to whether the protein is an intracellular channel (35) or plasma membrane channel (33,43).…”

Section: Discussionmentioning

confidence: 99%

“…In Situ Hybridization Studies-733-bp in situ hybridization probes were obtained from HeLa cells cDNA, complementary to the human ClC-3 mRNA initiation codon region (37). An antisense probe was obtained using conventional procedures.…”

Section: Methodsmentioning

confidence: 99%

“…The ASO and MMO sequence was 5Ј-CGTCCCTCTTTAACTGGTT-3Ј and 5Ј-CTGCCTCCAT-TTGTCATTG-3Ј, respectively. The ASO sequence was complementary to the human ClC-3 mRNA initiation codon region (37), starting from the second base before the initiation codon (ATG corresponding to the third open reading frame). For electrophysiological and volume measurement experiments, the transfection efficiency was assessed with a fluorescein isothiocyanate (FITC)-or a rhodamine derivative (TAMRA)-labeled oligonucleotides at bases 1 and 19, or 1 and 2, respectively.…”

Section: Methodsmentioning

confidence: 99%

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ClC-3 Is a Fundamental Molecular Component of Volume-sensitive Outwardly Rectifying Cl− Channels and Volume Regulation in HeLa Cells and Xenopus laevis Oocytes

Hermoso

Satterwhite²,

Andrade

et al. 2002

Journal of Biological Chemistry

106

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

ClC-3 Is a Fundamental Molecular Component of Volume-sensitive Outwardly Rectifying Cl− Channels and Volume Regulation in HeLa Cells and Xenopus laevis Oocytes

Hermoso

Satterwhite²,

Andrade

et al. 2002

Journal of Biological Chemistry

106

View full text Add to dashboard Cite

“…Mutations in this chloride channel lead to X-linked kidney stone disease [11,17]. The function of other members of this gene family (CIC-Ka and CIC-Kb [7,8], C1C-3 [9,18] and C1C-4 [2,10]), however, is currently obscure. This problem is compounded by the fact that functional expression as chloride channels, as reported by one group [7,9], could not be reproduced by other groups [2,8,18].…”

Section: Introductionmentioning

confidence: 99%

ClC‐6 and ClC‐7 are two novel broadly expressed members of the CLC chloride channel family

1995

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We cloned two novel members of the CLC chloride channel family from rat and human brain. CIC-6 is a 97-kDa protein, and CIC-7 a 89-kDa protein roughly 45% identical with CIC-6. Together they define a new branch of this gene family. Both genes are very broadly expressed, e.g. in brain, testes, muscle and kidney. In mouse embryos, both genes are expressed as early as day 7. While the human gene for CIC-6 is located on human chromosome lp36 and shares this region with hCIC-Ka and hCIC-Kb, CIC-7 is on 16p13. CIC-6 has a highly conserved glycosylation site between transmembrane domains D8 and D9, while CIC-7 is the only known eukaryotic CIC protein which lacks this site. Hydropathy analysis indicates that domain D4 cannot serve as a transmembrane domain. Both CIC-6 and CIC-7 cannot be expressed as chloride channels in Xenopus oocytes, either singly or in combination.

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“…1C), shows an identity level of about 33% (some 63% similarity) to a segment of a putative chloride channel from several species (not shown). Among the sequences that can be aligned to Csk22 are residues 332 to 376 of a human and murine voltage-gated chloride channel (GenBank accession numbers X78520 and X78874) (6). Interestingly, this segment in several transporters may be phosphorylated to regulate the activity of the channel (6).…”

Section: Resultsmentioning

confidence: 99%

cse15, cse60, and csk22 are new members of mother-cell-specific sporulation regulons in Bacillus subtilis

et al. 1997

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We report on the characterization of three new transcription units expressed during sporulation in Bacillus subtilis. Two of the units, cse15 and cse60, were mapped at about 123؇ and 62؇ on the genetic map, respectively. Their transcription commenced around h 2 of sporulation and showed an absolute requirement for E . Maximal expression of both cse15 and cse60 further depended on the DNA-binding protein SpoIIID. Primer extension results revealed ؊10 and ؊35 sequences upstream of the cse15 and cse60 coding sequences very similar to those utilized by E -containing RNA polymerase. Alignment of these and other regulatory regions led to a revised consensus sequence for E -dependent promoters. A third transcriptional unit, designated csk22, was localized at approximately 173؇ on the chromosome. Transcription of csk22 was activated at h 4 of sporulation, required the late mother-cell regulator K , and was repressed by the GerE protein. Sequences in the csk22 promoter region were similar to those of other K -dependent promoters. The cse60 locus was deduced to encode an acidic product of only 60 residues. A 37.6-kDa protein apparently encoded by cse15 was weakly related to the heavy chain of myosins, as well as to other myosin-like proteins, and is predicted to contain a central, 100 residue-long coiled-coil domain. Finally, csk22 is inferred to encode a 18.2-kDa hydrophobic product with five possible membrane-spanning helices, which could function as a transporter.

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Characterization of a Human and Murine Gene (CLCN3) Sharing Similarities to Voltage-Gated Chloride Channels and to a Yeast Integral Membrane Protein

Cited by 72 publications

References 0 publications

ClC-3 Is a Fundamental Molecular Component of Volume-sensitive Outwardly Rectifying Cl− Channels and Volume Regulation in HeLa Cells and Xenopus laevis Oocytes

ClC-3 Is a Fundamental Molecular Component of Volume-sensitive Outwardly Rectifying Cl− Channels and Volume Regulation in HeLa Cells and Xenopus laevis Oocytes

ClC‐6 and ClC‐7 are two novel broadly expressed members of the CLC chloride channel family

cse15, cse60, and csk22 are new members of mother-cell-specific sporulation regulons in Bacillus subtilis

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