| Glomerular Podocytes: a Study of Mechanical Properties and MechanoChemical Signaling. | |
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MedLine Citation:
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PMID: 21315064 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Kidney glomeruli function as filters, allowing the passage of small solutes and waste products into the urinary tract, while retaining essential proteins and macromolecules in the blood stream. These structures are under constant mechanical stress due to fluid pressure, driving filtration across the barrier. We mechanically stimulated adherent wildtype podocytes using the methods of magnetic tweezer and twisting as well as cell stretching. Attaching collagen IVcoated or polyLlysinecoated magnetic beads to cell receptors allowed the determination of the cellular stiffness. Angiotensin IItreated podocytes showed slightly higher stiffness than untreated cells. The cell fluidity (i.e. internal dynamics) remained similar under these conditions and showed an increase with force. The bead detachment (a measure of the binding strength) was higher in angiotensin IItreated compared to untreated podocytes. Using the magnetic twisting device confirmed that angiotensin II treatment of podocytes increases and CDTAtreatment decreases cell stiffness. However, treatment with both angiotensin II and CDTA increased only slightly cell stiffness compared to solely CDTAtreated cells. Exposing podocytes to cyclic, uniaxial stretch showed an earlier onset of ERK(1/2) phosphorylation compared to MEF (control) cells. These results indicate that angiotensin II might free intracellularly stored calcium and affects actomyosin contraction, and that mechanical stimulation influences cell signaling. |
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Authors:
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Alexander Eekhoff; Navid Bonakdar; José Luis Alonso; Bernd Hoffmann; Wolfgang H Goldmann |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-2-8 |
Journal Detail:
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Title: Biochemical and biophysical research communications Volume: - ISSN: 1090-2104 ISO Abbreviation: - Publication Date: 2011 Feb |
Date Detail:
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Created Date: 2011-2-14 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0372516 Medline TA: Biochem Biophys Res Commun Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2011. Published by Elsevier Inc. |
Affiliation:
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Center for Medical Physics and Technology, Biophysics Group Erlangen-Nuremberg, Erlangen, Germany. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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