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Par3A is dispensable for the function of the glomerular filtration barrier of the kidney
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| Zeitschriftentitel: | American Journal of Physiology-Renal Physiology |
|---|---|
| Personen und Körperschaften: | , , , , , , , |
| In: | American Journal of Physiology-Renal Physiology, 311, 2016, 1, S. F112-F119 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Physiological Society
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| Schlagwörter: |
| author_facet |
Koehler, Sybille Tellkamp, Frederik Niessen, Carien M. Bloch, Wilhelm Kerjaschki, Dontscho Schermer, Bernhard Benzing, Thomas Brinkkoetter, Paul T. Koehler, Sybille Tellkamp, Frederik Niessen, Carien M. Bloch, Wilhelm Kerjaschki, Dontscho Schermer, Bernhard Benzing, Thomas Brinkkoetter, Paul T. |
|---|---|
| author |
Koehler, Sybille Tellkamp, Frederik Niessen, Carien M. Bloch, Wilhelm Kerjaschki, Dontscho Schermer, Bernhard Benzing, Thomas Brinkkoetter, Paul T. |
| spellingShingle |
Koehler, Sybille Tellkamp, Frederik Niessen, Carien M. Bloch, Wilhelm Kerjaschki, Dontscho Schermer, Bernhard Benzing, Thomas Brinkkoetter, Paul T. American Journal of Physiology-Renal Physiology Par3A is dispensable for the function of the glomerular filtration barrier of the kidney Physiology |
| author_sort |
koehler, sybille |
| spelling |
Koehler, Sybille Tellkamp, Frederik Niessen, Carien M. Bloch, Wilhelm Kerjaschki, Dontscho Schermer, Bernhard Benzing, Thomas Brinkkoetter, Paul T. 1931-857X 1522-1466 American Physiological Society Physiology http://dx.doi.org/10.1152/ajprenal.00171.2016 <jats:p>Polarity signaling through the atypical PKC (aPKC)-Par polarity complex is essential for the development and maintenance of the podocyte architecture and the function of the glomerular filtration barrier of the kidney. To study the contribution of Par3A in this complex, we generated a novel Pard3 podocyte-specific knockout mouse model by targeting exon 6 of the Pard3 gene. Genetic deletion of Pard3a did not impair renal function, neither at birth nor later in life. Even challenging the animals did not result in glomerular disease. Despite its well-established role in aPKC-mediated signaling, Par3A appears to be dispensable for the function of the glomerular filtration barrier. Moreover, its homolog Pard3b, and not Pard3a, is the dominant Par3 gene expressed in podocytes and found at the basis of the slit diaphragm, where it partially colocalizes with podocin. In conclusion, Par3A function is either dispensable for slit diaphragm integrity, or compensatory mechanisms and a high redundancy of the different polarity proteins, including Par3B, Lgl, or PALS1, maintain the function of the glomerular filtration barrier, even in the absence of Par3A.</jats:p> Par3A is dispensable for the function of the glomerular filtration barrier of the kidney American Journal of Physiology-Renal Physiology |
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10.1152/ajprenal.00171.2016 |
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American Physiological Society, 2016 |
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American Physiological Society, 2016 |
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1931-857X 1522-1466 |
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American Journal of Physiology-Renal Physiology |
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| title |
Par3A is dispensable for the function of the glomerular filtration barrier of the kidney |
| title_unstemmed |
Par3A is dispensable for the function of the glomerular filtration barrier of the kidney |
| title_full |
Par3A is dispensable for the function of the glomerular filtration barrier of the kidney |
| title_fullStr |
Par3A is dispensable for the function of the glomerular filtration barrier of the kidney |
| title_full_unstemmed |
Par3A is dispensable for the function of the glomerular filtration barrier of the kidney |
| title_short |
Par3A is dispensable for the function of the glomerular filtration barrier of the kidney |
| title_sort |
par3a is dispensable for the function of the glomerular filtration barrier of the kidney |
| topic |
Physiology |
| url |
http://dx.doi.org/10.1152/ajprenal.00171.2016 |
| publishDate |
2016 |
| physical |
F112-F119 |
| description |
<jats:p>Polarity signaling through the atypical PKC (aPKC)-Par polarity complex is essential for the development and maintenance of the podocyte architecture and the function of the glomerular filtration barrier of the kidney. To study the contribution of Par3A in this complex, we generated a novel Pard3 podocyte-specific knockout mouse model by targeting exon 6 of the Pard3 gene. Genetic deletion of Pard3a did not impair renal function, neither at birth nor later in life. Even challenging the animals did not result in glomerular disease. Despite its well-established role in aPKC-mediated signaling, Par3A appears to be dispensable for the function of the glomerular filtration barrier. Moreover, its homolog Pard3b, and not Pard3a, is the dominant Par3 gene expressed in podocytes and found at the basis of the slit diaphragm, where it partially colocalizes with podocin. In conclusion, Par3A function is either dispensable for slit diaphragm integrity, or compensatory mechanisms and a high redundancy of the different polarity proteins, including Par3B, Lgl, or PALS1, maintain the function of the glomerular filtration barrier, even in the absence of Par3A.</jats:p> |
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| author | Koehler, Sybille, Tellkamp, Frederik, Niessen, Carien M., Bloch, Wilhelm, Kerjaschki, Dontscho, Schermer, Bernhard, Benzing, Thomas, Brinkkoetter, Paul T. |
| author_facet | Koehler, Sybille, Tellkamp, Frederik, Niessen, Carien M., Bloch, Wilhelm, Kerjaschki, Dontscho, Schermer, Bernhard, Benzing, Thomas, Brinkkoetter, Paul T., Koehler, Sybille, Tellkamp, Frederik, Niessen, Carien M., Bloch, Wilhelm, Kerjaschki, Dontscho, Schermer, Bernhard, Benzing, Thomas, Brinkkoetter, Paul T. |
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| description | <jats:p>Polarity signaling through the atypical PKC (aPKC)-Par polarity complex is essential for the development and maintenance of the podocyte architecture and the function of the glomerular filtration barrier of the kidney. To study the contribution of Par3A in this complex, we generated a novel Pard3 podocyte-specific knockout mouse model by targeting exon 6 of the Pard3 gene. Genetic deletion of Pard3a did not impair renal function, neither at birth nor later in life. Even challenging the animals did not result in glomerular disease. Despite its well-established role in aPKC-mediated signaling, Par3A appears to be dispensable for the function of the glomerular filtration barrier. Moreover, its homolog Pard3b, and not Pard3a, is the dominant Par3 gene expressed in podocytes and found at the basis of the slit diaphragm, where it partially colocalizes with podocin. In conclusion, Par3A function is either dispensable for slit diaphragm integrity, or compensatory mechanisms and a high redundancy of the different polarity proteins, including Par3B, Lgl, or PALS1, maintain the function of the glomerular filtration barrier, even in the absence of Par3A.</jats:p> |
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| physical | F112-F119 |
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| series | American Journal of Physiology-Renal Physiology |
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| spelling | Koehler, Sybille Tellkamp, Frederik Niessen, Carien M. Bloch, Wilhelm Kerjaschki, Dontscho Schermer, Bernhard Benzing, Thomas Brinkkoetter, Paul T. 1931-857X 1522-1466 American Physiological Society Physiology http://dx.doi.org/10.1152/ajprenal.00171.2016 <jats:p>Polarity signaling through the atypical PKC (aPKC)-Par polarity complex is essential for the development and maintenance of the podocyte architecture and the function of the glomerular filtration barrier of the kidney. To study the contribution of Par3A in this complex, we generated a novel Pard3 podocyte-specific knockout mouse model by targeting exon 6 of the Pard3 gene. Genetic deletion of Pard3a did not impair renal function, neither at birth nor later in life. Even challenging the animals did not result in glomerular disease. Despite its well-established role in aPKC-mediated signaling, Par3A appears to be dispensable for the function of the glomerular filtration barrier. Moreover, its homolog Pard3b, and not Pard3a, is the dominant Par3 gene expressed in podocytes and found at the basis of the slit diaphragm, where it partially colocalizes with podocin. In conclusion, Par3A function is either dispensable for slit diaphragm integrity, or compensatory mechanisms and a high redundancy of the different polarity proteins, including Par3B, Lgl, or PALS1, maintain the function of the glomerular filtration barrier, even in the absence of Par3A.</jats:p> Par3A is dispensable for the function of the glomerular filtration barrier of the kidney American Journal of Physiology-Renal Physiology |
| spellingShingle | Koehler, Sybille, Tellkamp, Frederik, Niessen, Carien M., Bloch, Wilhelm, Kerjaschki, Dontscho, Schermer, Bernhard, Benzing, Thomas, Brinkkoetter, Paul T., American Journal of Physiology-Renal Physiology, Par3A is dispensable for the function of the glomerular filtration barrier of the kidney, Physiology |
| title | Par3A is dispensable for the function of the glomerular filtration barrier of the kidney |
| title_full | Par3A is dispensable for the function of the glomerular filtration barrier of the kidney |
| title_fullStr | Par3A is dispensable for the function of the glomerular filtration barrier of the kidney |
| title_full_unstemmed | Par3A is dispensable for the function of the glomerular filtration barrier of the kidney |
| title_short | Par3A is dispensable for the function of the glomerular filtration barrier of the kidney |
| title_sort | par3a is dispensable for the function of the glomerular filtration barrier of the kidney |
| title_unstemmed | Par3A is dispensable for the function of the glomerular filtration barrier of the kidney |
| topic | Physiology |
| url | http://dx.doi.org/10.1152/ajprenal.00171.2016 |