Sequence and tissue distribution of a second protein of hepatic gap junctions, Cx26, as deduced from its cDNA

Jian-Ting Zhang, B. J. Nicholson

Research output: Contribution to journalArticle

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Abstract

While a number of different gap junction proteins have now been identified, hepatic gap junctions are unique in being the first demonstrated case where two homologous, but distinct, proteins (28,000 and 21,000 M(r)) are found within a single gap junctional plaque (Nicholson, B.J., R. Dermietzel, D. Teplow, O. Traub, K. Willecke, and J.-P. Revel. 1987. Nature [Lond.]. 329: 732-734). The cDNA for the major 28,000-M(r) component has been cloned (Paul, D.L. 1986. J. Cell Biol. 103: 123-134) (Kumar, N.M., and N.B. Gilula. 1986. J. Cell Biol. 103: 767-776) and, based on its deduced formula weight of 32,007, has been designated connexin 32 (or Cx32 as used here). We now report the selection and characterization of clones for the second 21,000-M(r) protein using an oligonucleotide derived from the amino-terminal protein sequence. Together the cDNAs represent 2.4 kb of the single 2.5-kb message detected in Northern blots. An open reading frame of 678 bp coding for a protein with a calculated molecular mass of 26,453 D was identified. Overall sequence homology with Cx32 and Cx43 (64 and 51% amino acid identities, respectively) and a similar predicted tertiary structure confirm that this protein forms part of the connexin family and is consequently referred to as Cx26. Consistent with observations on Cx43 (Beyer, E.C., D.L. Paul, and D.A. Goodenough. 1987. J. Cell Biol. 105: 2621-2629) the most marked divergence between Cx26 and other members of the family lies in the sequence of the cytoplasmic domains. The Cx26 gene is present as a single copy per haploid genome in rat and, based on Southern blots, appears to contain at least one intron outside the open reading frame. Northern blots indicate that Cx32 and Cx26 are typically coexpressed, messages for both having been identified in liver, kidney, intestine, lung, spleen, stomach, testes, and brain, but not heart and adult skeletal muscle. This raises the interesting prospect of having differential modes of regulating intercellular channels within a given tissue and, at least in the case of liver, a given cell.

Original languageEnglish (US)
Pages (from-to)3391-3401
Number of pages11
JournalJournal of Cell Biology
Volume109
Issue number6 II
DOIs
StatePublished - 1989
Externally publishedYes

Fingerprint

Connexins
Tissue Distribution
Complementary DNA
Connexin 43
Liver
Northern Blotting
Open Reading Frames
Proteins
Myeloma Proteins
Gap Junctions
Haploidy
Sequence Homology
Southern Blotting
Tertiary Protein Structure
Oligonucleotides
Introns
Intestines
Testis
Stomach
Skeletal Muscle

ASJC Scopus subject areas

  • Cell Biology

Cite this

Sequence and tissue distribution of a second protein of hepatic gap junctions, Cx26, as deduced from its cDNA. / Zhang, Jian-Ting; Nicholson, B. J.

In: Journal of Cell Biology, Vol. 109, No. 6 II, 1989, p. 3391-3401.

Research output: Contribution to journalArticle

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abstract = "While a number of different gap junction proteins have now been identified, hepatic gap junctions are unique in being the first demonstrated case where two homologous, but distinct, proteins (28,000 and 21,000 M(r)) are found within a single gap junctional plaque (Nicholson, B.J., R. Dermietzel, D. Teplow, O. Traub, K. Willecke, and J.-P. Revel. 1987. Nature [Lond.]. 329: 732-734). The cDNA for the major 28,000-M(r) component has been cloned (Paul, D.L. 1986. J. Cell Biol. 103: 123-134) (Kumar, N.M., and N.B. Gilula. 1986. J. Cell Biol. 103: 767-776) and, based on its deduced formula weight of 32,007, has been designated connexin 32 (or Cx32 as used here). We now report the selection and characterization of clones for the second 21,000-M(r) protein using an oligonucleotide derived from the amino-terminal protein sequence. Together the cDNAs represent 2.4 kb of the single 2.5-kb message detected in Northern blots. An open reading frame of 678 bp coding for a protein with a calculated molecular mass of 26,453 D was identified. Overall sequence homology with Cx32 and Cx43 (64 and 51{\%} amino acid identities, respectively) and a similar predicted tertiary structure confirm that this protein forms part of the connexin family and is consequently referred to as Cx26. Consistent with observations on Cx43 (Beyer, E.C., D.L. Paul, and D.A. Goodenough. 1987. J. Cell Biol. 105: 2621-2629) the most marked divergence between Cx26 and other members of the family lies in the sequence of the cytoplasmic domains. The Cx26 gene is present as a single copy per haploid genome in rat and, based on Southern blots, appears to contain at least one intron outside the open reading frame. Northern blots indicate that Cx32 and Cx26 are typically coexpressed, messages for both having been identified in liver, kidney, intestine, lung, spleen, stomach, testes, and brain, but not heart and adult skeletal muscle. This raises the interesting prospect of having differential modes of regulating intercellular channels within a given tissue and, at least in the case of liver, a given cell.",
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N2 - While a number of different gap junction proteins have now been identified, hepatic gap junctions are unique in being the first demonstrated case where two homologous, but distinct, proteins (28,000 and 21,000 M(r)) are found within a single gap junctional plaque (Nicholson, B.J., R. Dermietzel, D. Teplow, O. Traub, K. Willecke, and J.-P. Revel. 1987. Nature [Lond.]. 329: 732-734). The cDNA for the major 28,000-M(r) component has been cloned (Paul, D.L. 1986. J. Cell Biol. 103: 123-134) (Kumar, N.M., and N.B. Gilula. 1986. J. Cell Biol. 103: 767-776) and, based on its deduced formula weight of 32,007, has been designated connexin 32 (or Cx32 as used here). We now report the selection and characterization of clones for the second 21,000-M(r) protein using an oligonucleotide derived from the amino-terminal protein sequence. Together the cDNAs represent 2.4 kb of the single 2.5-kb message detected in Northern blots. An open reading frame of 678 bp coding for a protein with a calculated molecular mass of 26,453 D was identified. Overall sequence homology with Cx32 and Cx43 (64 and 51% amino acid identities, respectively) and a similar predicted tertiary structure confirm that this protein forms part of the connexin family and is consequently referred to as Cx26. Consistent with observations on Cx43 (Beyer, E.C., D.L. Paul, and D.A. Goodenough. 1987. J. Cell Biol. 105: 2621-2629) the most marked divergence between Cx26 and other members of the family lies in the sequence of the cytoplasmic domains. The Cx26 gene is present as a single copy per haploid genome in rat and, based on Southern blots, appears to contain at least one intron outside the open reading frame. Northern blots indicate that Cx32 and Cx26 are typically coexpressed, messages for both having been identified in liver, kidney, intestine, lung, spleen, stomach, testes, and brain, but not heart and adult skeletal muscle. This raises the interesting prospect of having differential modes of regulating intercellular channels within a given tissue and, at least in the case of liver, a given cell.

AB - While a number of different gap junction proteins have now been identified, hepatic gap junctions are unique in being the first demonstrated case where two homologous, but distinct, proteins (28,000 and 21,000 M(r)) are found within a single gap junctional plaque (Nicholson, B.J., R. Dermietzel, D. Teplow, O. Traub, K. Willecke, and J.-P. Revel. 1987. Nature [Lond.]. 329: 732-734). The cDNA for the major 28,000-M(r) component has been cloned (Paul, D.L. 1986. J. Cell Biol. 103: 123-134) (Kumar, N.M., and N.B. Gilula. 1986. J. Cell Biol. 103: 767-776) and, based on its deduced formula weight of 32,007, has been designated connexin 32 (or Cx32 as used here). We now report the selection and characterization of clones for the second 21,000-M(r) protein using an oligonucleotide derived from the amino-terminal protein sequence. Together the cDNAs represent 2.4 kb of the single 2.5-kb message detected in Northern blots. An open reading frame of 678 bp coding for a protein with a calculated molecular mass of 26,453 D was identified. Overall sequence homology with Cx32 and Cx43 (64 and 51% amino acid identities, respectively) and a similar predicted tertiary structure confirm that this protein forms part of the connexin family and is consequently referred to as Cx26. Consistent with observations on Cx43 (Beyer, E.C., D.L. Paul, and D.A. Goodenough. 1987. J. Cell Biol. 105: 2621-2629) the most marked divergence between Cx26 and other members of the family lies in the sequence of the cytoplasmic domains. The Cx26 gene is present as a single copy per haploid genome in rat and, based on Southern blots, appears to contain at least one intron outside the open reading frame. Northern blots indicate that Cx32 and Cx26 are typically coexpressed, messages for both having been identified in liver, kidney, intestine, lung, spleen, stomach, testes, and brain, but not heart and adult skeletal muscle. This raises the interesting prospect of having differential modes of regulating intercellular channels within a given tissue and, at least in the case of liver, a given cell.

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