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      Role of Protein Kinase C in Podocytes and Development of Glomerular Damage in Diabetic Nephropathy

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          Abstract

          The early glomerular changes in diabetes include a podocyte phenotype with loss of slit diaphragm proteins, changes in the actin cytoskeleton and foot process architecture. This review focuses on the role of the protein kinase C (PKC) family in podocytes and points out the differential roles of classical, novel, and atypical PKCs in podocytes. Some PKC isoforms are indispensable for proper glomerular development and slit diaphragm maintenance, whereas others might be harmful when activated in the diabetic milieu. Therefore, some might be interesting treatment targets in the early phase of diabetes.

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          AP-1 function and regulation.

          Michael Karin, Zheng-gang Liu, Ebrahim Zandi (1997)
          AP-1 (activating protein-1) is a collective term referring to dimeric transcription factors composed of Jun, Fos or ATF (activating transcription factor) subunits that bind to a common DNA site, the AP-1-binding site. As the complexity of our knowledge of AP-1 factors has increased, our understanding of their physiological function has decreased. This trend, however, is beginning to be reversed due to the recent studies of gene-knockout mice and cell lines deficient in specific AP-1 components. Such studies suggest that different AP-1 factors may regulate different target genes and thus execute distinct biological functions. Also, the involvement of AP-1 factors in functions such as cell proliferation and survival has been made somewhat clearer as a result of such studies. In addition, there has been considerable progress in understanding some of the mechanisms and signaling pathways involved in the regulation of AP-1 activity. In addition to regulation by heterodimerization between Jun, Fos and ATF proteins, AP-1 activity is regulated through interactions with specific protein kinases and a variety of transcriptional coactivators.
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            The regulation of AP-1 activity by mitogen-activated protein kinases.

            M Karin (1995)
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              The human gene for vascular endothelial growth factor. Multiple protein forms are encoded through alternative exon splicing.

              E Tischer, R. Mitchell, T. Hartman … (1991)
              Vascular endothelial growth factor (VEGF) is an apparently endothelial cell-specific mitogen that is structurally related to platelet-derived growth factor. By Northern blot and protein analyses, we show that VEGF is produced by cultured vascular smooth muscle cells. Analysis of VEGF transcripts in these cells by polymerase chain reaction and cDNA cloning revealed three different forms of the VEGF coding region, as had been reported in HL60 cells. The three forms of the human VEGF protein chain predicted from these coding regions are 189, 165, and 121 amino acids in length. Comparison of cDNA nucleotide sequences with sequences derived from human VEGF genomic clones indicates that the VEGF gene is split among eight exons and that the various VEGF coding region forms arise from this gene by alternative splicing: the 165-amino-acid form of the protein is missing the residues encoded by exon 6, whereas the 121-amino-acid form is missing the residues encoded by exons 6 and 7. Analysis of the VEGF gene promoter region revealed a single major transcription start, which lies near a cluster of potential Sp1 factor binding sites. The promoter region also contains several potential binding sites for the transcription factors AP-1 and AP-2; consistent with the presence of these sites, Northern blot analysis demonstrated that the level of VEGF transcripts is elevated in cultured vascular smooth muscle cells after treatment with the phorbol ester 12-O-tetradecanoyl-phorbol-13-acetate.
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                Author and article information

                Contributors
                Journal
                Journal ID (nlm-ta): Front Endocrinol (Lausanne)
                Journal ID (iso-abbrev): Front Endocrinol (Lausanne)
                Journal ID (publisher-id): Front. Endocrinol.
                Title: Frontiers in Endocrinology
                Publisher: Frontiers Media S.A.
                ISSN (Electronic): 1664-2392
                Publication date (Electronic preprint): 19 September 2014
                Publication date (Electronic): 05 November 2014
                Publication date Collection: 2014
                Volume: 5
                Electronic Location Identifier: 179
                Affiliations
                [1] 1Department of Medicine/Nephrology, Hannover Medical School , Hannover, Germany
                Author notes

                Edited by: Barbara Lewko, Medical University of Gdansk, Poland

                Reviewed by: Undurti Narasimha Das, UND Life Sciences, USA; Chris R. J. Kennedy, Ottawa Hospital Research Institute, Canada

                *Correspondence: Mario Schiffer, Department of Medicine/Nephrology, Hannover Medical School, Carl Neuberg Street 1-OE6840, Hannover 30625, Germany e-mail: schiffer.mario@ 123456mh-hannover.de

                This article was submitted to Diabetes, a section of the journal Frontiers in Endocrinology.

                Article
                DOI: 10.3389/fendo.2014.00179
                PMC ID: 4220730
                PubMed ID: 25414693
                SO-VID: cb754834-a035-4147-8065-8f843a64cffe
                Copyright © Copyright © 2014 Teng, Duong, Tossidou, Yu and Schiffer.
                License:

                This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

                History
                Date received : 16 July 2014
                Date accepted : 06 October 2014
                Page count
                Figures: 1, Tables: 0, Equations: 0, References: 71, Pages: 6, Words: 5497
                Categories
                Subject: Endocrinology
                Subject: Mini Review

                ScienceOpen disciplines: Endocrinology & Diabetes
                Keywords: proteinuria,diabetic podocytopathy,glomerulosclerosis,nephrin endocytosis,effacement
                Data availability:
                ScienceOpen disciplines: Endocrinology & Diabetes
                Keywords: proteinuria, diabetic podocytopathy, glomerulosclerosis, nephrin endocytosis, effacement

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