Research article summary (published 30 Oct 2009):

Protein cytoskeleton and overexpression of Na(+),K(+)-ATPase in opossum kidney cells.

Full Abstract

Previous studies have shown that over time in culture opossum kidney (OK) cells are endowed with increased Na(+),K(+)-ATPase activity and expression (Silva et al., 2006, J Membr Biol 212:163-175; Silva and Soares-da-Silva, 2007, Am J Physiol Regul Integr Comp Physiol 293:R1764-R1770). The present work evaluated the cytoskeleton reorganization in OK cells at passages 40 and 80 in culture and its possible relationship with membrane transport proteins and cell morphology. It is shown that OK cells with 80 passages in culture have increased size, internal complexity, and total protein expression. In OK cells with 80 passages in culture the use of in-cell western showed that ezrin/radixin/moesin complex was increased by 20%. The most abundant ankyrin-G isoform in OK cells with 40 passages was the approximately 200/220 kDa isoform, whereas in OK cells with 80 passages the most abundant isoform was the approximately 170 kDa isoform. The spectrin-betaII approximately 240 kDa isoform, the predominant isoform in OK cells with 40 passages, was marginally detected in OK cells with 80 passages. Besides Na(+),K(+)-ATPase, GLUT2, and NHE3 expression was also significantly increased in OK cells with 80 passages. It is concluded that the prolonged cell passaging of OK cells results in an interesting and valuable experimental model to analyze the reorganization of the renal cell cytoskeleton proteins and its relationship with transporter and signaling membrane proteins.

Author information

Author/s: Silva, Elisabete (E); Soares-da-Silva, Patrício (P);

Affiliation: Faculty of Medicine, Institute of Pharmacology & Therapeutics, Porto, Portugal.

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

Journal: Journal of cellular physiology (J Cell Physiol), published in United States. (Language: eng)

Reference: 2009-Nov; vol 221 (issue 2) : pp 318-24

Dates: Created 2009/08/27; Completed 2009/09/09;

PMID: 19582774, status: MEDLINE (last retrieval date: 9/9/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Animals Cell Line Cell Polarity Cell Shape Cytoskeletal Proteins - metabolism Cytoskeleton - enzymology Flow Cytometry Gene Expression Regulation, Enzymologic

Glucose Transporter Type 2 - metabolism Kidney - cytology; enzymology Opossums - metabolism RNA, Messenger - genetics; metabolism Sodium-Hydrogen Antiporter - metabolism Sodium-Potassium-Exchanging ATPase - genetics; metabolism Subcellular Fractions - enzymology Tubulin - metabolism

Associated Chemicals: Cytoskeletal Proteins (0) ; Glucose Transporter Type 2 (0) ; RNA, Messenger (0) ; Sodium-Hydrogen Antiporter (0) ; Tubulin (0) ; sodium-hydrogen exchanger 3 (0) ; Sodium-Potassium-Exchanging ATPase (EC 3.6.3.9)

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