Abstract
Liver gap junctions and gap-junction-like structures from eye lenses are each comprised of a single major protein (Mr 28,000 and 26,000, respectively). These proteins display different two-dimensional peptide fingerprints, distinct amino acid compositions, nonhomologous N-terminal amino acid sequences and different sensitivities to proteases when part of the intact junction. However, the junctional protein of each tissue is well conserved between species, as demonstrated previously for lens and now for liver in several mammalian species. The possibility of tissue-specific gap junction proteins is discussed in the light of data suggesting that rat heart gap junctions are comprised of yet a third protein.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 967-978 |
| Number of pages | 12 |
| Journal | Cell |
| Volume | 32 |
| Issue number | 3 |
| DOIs | |
| State | Published - 1983 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Cell Biology
- Molecular Biology
- Medicine(all)
Cite this
Differences between liver gap junction protein and lens MIP 26 from rat : Implications for tissue specificity of gap junctions. / Nicholson, Bruce J; Takemoto, Larry J.; Hunkapiller, Michael W.; Hood, Leroy E.; Revel, Jean Paul.
In: Cell, Vol. 32, No. 3, 1983, p. 967-978.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Differences between liver gap junction protein and lens MIP 26 from rat
T2 - Implications for tissue specificity of gap junctions
AU - Nicholson, Bruce J
AU - Takemoto, Larry J.
AU - Hunkapiller, Michael W.
AU - Hood, Leroy E.
AU - Revel, Jean Paul
PY - 1983
Y1 - 1983
N2 - Liver gap junctions and gap-junction-like structures from eye lenses are each comprised of a single major protein (Mr 28,000 and 26,000, respectively). These proteins display different two-dimensional peptide fingerprints, distinct amino acid compositions, nonhomologous N-terminal amino acid sequences and different sensitivities to proteases when part of the intact junction. However, the junctional protein of each tissue is well conserved between species, as demonstrated previously for lens and now for liver in several mammalian species. The possibility of tissue-specific gap junction proteins is discussed in the light of data suggesting that rat heart gap junctions are comprised of yet a third protein.
AB - Liver gap junctions and gap-junction-like structures from eye lenses are each comprised of a single major protein (Mr 28,000 and 26,000, respectively). These proteins display different two-dimensional peptide fingerprints, distinct amino acid compositions, nonhomologous N-terminal amino acid sequences and different sensitivities to proteases when part of the intact junction. However, the junctional protein of each tissue is well conserved between species, as demonstrated previously for lens and now for liver in several mammalian species. The possibility of tissue-specific gap junction proteins is discussed in the light of data suggesting that rat heart gap junctions are comprised of yet a third protein.
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UR - http://www.scopus.com/inward/citedby.url?scp=0020560348&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(83)90081-8
DO - 10.1016/0092-8674(83)90081-8
M3 - Article
C2 - 6299583
AN - SCOPUS:0020560348
VL - 32
SP - 967
EP - 978
JO - Cell
JF - Cell
SN - 0092-8674
IS - 3
ER -