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{
"authors": [
"Mauro Pessia",
"Paola Imbrici",
"Maria Cristina",
"D ' Adamo",
"Lorena Salvatore",
"Stephen J Tucker"
],
"id": "653",
"paragraph_id": 1,
"section": "abstract",
"title": ""
} | Inwardly rectifying potassium (Kir) channels are found in almost every cell type where they play key roles in controlling membrane potential, cellular excitability and K + fluxes. A large number of clones have now been identified which encode Kir channels and these can be divided into seven major subfamilies (Kir1.0-Kir7.0). Until recently very little was known about the only member of the Kir5.0 subfamily, Kir5.1 (Bond et al. 1994). This subunit is unusual in that it only appears to form functional K + channels when assembled as a heteromeric channel with members of the Kir4.0 subfamily, Kir4.1 and Kir4.2. | [
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] | [
"Kir4.1",
"Kir4.2",
"Kir5.1"
] |
{
"authors": [
"Mauro Pessia",
"Paola Imbrici",
"Maria Cristina",
"D ' Adamo",
"Lorena Salvatore",
"Stephen J Tucker"
],
"id": "653",
"paragraph_id": 2,
"section": "abstract",
"title": ""
} | The functional role of these heteromeric Kir4.0-Kir5.1 channels remains unclear. However, recent studies have shown that Kir4.1-Kir5.1 heteromeric channels exist in vivo in renal tubular epithelia. In addition these heteromeric channels have been shown to be extremely sensitive to inhibition by protons within the physiological pH range Xu et al. 2000;. There is therefore an emerging role for these channels in the pH-dependent regulation of K + fluxes and acid-base homeostasis. | [
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] | [
"Kir4.1",
"Kir5.1"
] |
{
"authors": [
"Mauro Pessia",
"Paola Imbrici",
"Maria Cristina",
"D ' Adamo",
"Lorena Salvatore",
"Stephen J Tucker"
],
"id": "653",
"paragraph_id": 3,
"section": "abstract",
"title": ""
} | Extensive studies with Kir1.1, another pH-sensitive channel, have shown that the primary pH sensor is a lysine residue found within a highly conserved region of the proximal N-terminus. Lysine is normally fully protonated under physiological conditions. However, this lysine residue in Kir1.1 (K80) exhibits anomalous titration due to its close association with two highly conserved arginine residues, one in the intracellular N-terminus and one in Differential pH sensitivity of Kir4.1 and Kir4.2 potassium channels and their modulation by heteropolymerisation with Kir5.1 | [
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] | [
"Kir1.1",
"Kir4.1",
"Kir4.2"
] |
{
"authors": [
"Mauro Pessia",
"Paola Imbrici",
"Maria Cristina",
"D ' Adamo",
"Lorena Salvatore",
"Stephen J Tucker"
],
"id": "653",
"paragraph_id": 1,
"section": "methods",
"title": ""
} | 1. The inwardly rectifying potassium channel Kir5.1 appears to form functional channels only by coexpression with either Kir4.1 or Kir4.2. Kir4.1-Kir5.1 heteromeric channels have been shown to exist in vivo in renal tubular epithelia. However, Kir5.1 is expressed in many other tissues where Kir4.1 is not found. Using Kir5.1-specific antibodies we have localised Kir5.1 expression in the pancreas, a tissue where Kir4.2 is also highly expressed. | [
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] | [
"Kir4.1",
"Kir4.2",
"Kir5.1"
] |
{
"authors": [
"Mauro Pessia",
"Paola Imbrici",
"Maria Cristina",
"D ' Adamo",
"Lorena Salvatore",
"Stephen J Tucker"
],
"id": "653",
"paragraph_id": 2,
"section": "methods",
"title": ""
} | 2. Heteromeric Kir5.1-Kir4.1 channels are significantly more sensitive to intracellular acidification than Kir4.1 currents. We demonstrate that this increased sensitivity is primarily due to modulation of the intrinsic Kir4.1 pH sensitivity by Kir5.1. | [
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] | [
"Kir4.1",
"Kir5.1"
] |
{
"authors": [
"Mauro Pessia",
"Paola Imbrici",
"Maria Cristina",
"D ' Adamo",
"Lorena Salvatore",
"Stephen J Tucker"
],
"id": "653",
"paragraph_id": 3,
"section": "methods",
"title": ""
} | 3. Kir4.2 was found to be significantly more pH sensitive (pK a = 7.1) than Kir4.1 (pK a = 5.99) due to an additional pH-sensing mechanism involving the C-terminus. As a result, coexpression with Kir5.1 does not cause a major shift in the pH sensitivity of the heteromeric Kir4.2-Kir5.1 channel. | [
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] | [
"Kir4.1",
"Kir4.2",
"Kir5.1"
] |
{
"authors": [
"Mauro Pessia",
"Paola Imbrici",
"Maria Cristina",
"D ' Adamo",
"Lorena Salvatore",
"Stephen J Tucker"
],
"id": "653",
"paragraph_id": 4,
"section": "methods",
"title": ""
} | 4. Cell-attached single channel analysis of Kir4.2 revealed a channel with a high open probability (P o > 0.9) and single channel conductance of ›25 pS, whilst coexpression with Kir5.1 produced novel bursting channels (P o < 0.3) and a principal conductance of ›54 pS with several subconductance states. | [
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] | [
"Kir4.2",
"Kir5.1"
] |
{
"authors": [
"Mauro Pessia",
"Paola Imbrici",
"Maria Cristina",
"D ' Adamo",
"Lorena Salvatore",
"Stephen J Tucker"
],
"id": "653",
"paragraph_id": 5,
"section": "methods",
"title": ""
} | 5. These results indicate that Kir5.1 may form heteromeric channels with Kir4.2 in tissues where Kir4.1 is not expressed (e.g. pancreas) and that these novel channels are likely to be regulated by changes in intracellular pH. In addition, the extreme pH sensitivity of Kir4.2 has implications for the role of this subunit as a homotetrameric channel. | [
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] | [
"Kir4.1",
"Kir4.2",
"Kir5.1"
] |
{
"authors": [
"Mauro Pessia",
"Paola Imbrici",
"Maria Cristina",
"D ' Adamo",
"Lorena Salvatore",
"Stephen J Tucker"
],
"id": "653",
"paragraph_id": 7,
"section": "methods",
"title": ""
} | Several different studies have also revealed that there is a correlation between the intrinsic sensitivity of a Kir channel to intracellular pH and the presence of a lysine residue at the equivalent position to K80 in Kir1.1. One such example is Kir4.1, which also forms pH-sensitive homomeric channels. Like Kir1.1, the pH sensitivity of Kir4.1 channels is primarily determined by a similar titratable lysine residue in the proximal N-terminus (K67), which is equivalent to K80 in Kir1.1. However the intrinsic pH sensitivity of Kir4.1 channels (pK = 6.0) is significantly lower than that of Kir1.1 (pK a = 6.9) and regulation of Kir4.1 channels by pH i is only likely to be significant in cases of extreme intracellular acidosis. | [
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] | [
"Kir1.1",
"Kir4.1"
] |
{
"authors": [
"Mauro Pessia",
"Paola Imbrici",
"Maria Cristina",
"D ' Adamo",
"Lorena Salvatore",
"Stephen J Tucker"
],
"id": "653",
"paragraph_id": 8,
"section": "methods",
"title": ""
} | We and others have recently shown that the intrinsic pH sensitivity of Kir4.1 can be modified by heteropolymerisation with Kir5.1. Coexpression of Kir4.1 with Kir5.1 produces novel K + channels with a significantly 'enhanced' pH sensitivity (pK a = 7.35). Inhibition of these channels by protons is direct and does not involve a reduction in the single-channel conductance. Interestingly, the pH sensitivity of these heteromeric channels still appears to be governed by the Kir4.1 subunit. Mutation of the titratable lysine residue (K67M) in Kir4.1 almost completely abolishes the pH sensitivity of the heteromeric Kir4.1-Kir5.1 channels. However, the mechanism by which Kir5.1 alters the intrinsic pH sensitivity of Kir4.1 remains to be determined. | [
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] | [
"Kir4.1",
"Kir5.1"
] |
{
"authors": [
"Mauro Pessia",
"Paola Imbrici",
"Maria Cristina",
"D ' Adamo",
"Lorena Salvatore",
"Stephen J Tucker"
],
"id": "653",
"paragraph_id": 9,
"section": "methods",
"title": ""
} | Although Kir4.1 and Kir5.1 have been shown to form heteromeric channels in vivo their tissue specific patterns of expression do not completely overlap. RT-PCR and Northern blot analysis have shown Kir5.1 to be expressed in several tissues where Kir4.1 is not, and vice versa. It is therefore highly likely that other subunits permit functional expression of Kir5.1 in tissues where Kir4.1 is not found. We have therefore investigated the properties of the related subunit Kir4.2 which is also pH sensitive and which forms heteromeric channels with Kir5.1. | [
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] | [
"Kir4.1",
"Kir4.2",
"Kir5.1"
] |
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