For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
10
views
32
references
 Top references
cited by
3
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
1 collections
    0
    shares
      176
      similar
       All similar

      To submit to Bentham Journals, please click here

      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Actin and Keratin are Binding Partners of the 1,25D 3-MARRS Receptor/PDIA3/ERp57

      research-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          We have shown that the 1,25D 3-MARRS receptor is necessary for the rapid, pre-genomic effects of 1,25(OH) 2D 3 on phosphate and/or calcium absorption in chick intestines. However, a clear understanding of the proteins involved in the signaling mechanisms by which the 1,25D 3-MARRS receptor facilitates 1,25(OH) 2D 3-mediated phosphate or calcium uptake, as well as other cellular effects, is still under investigation. We used co-immunoprecipitation studies and mass spectroscopy to identify actin and keratin as proteins that interact with the 1,25D 3-MARRS receptor. Using confocal microscopy, we visualized 1,25(OH) 2D 3- MARRS receptor localizations relative to actin and/or keratin distribution in chick enterocytes. Cells cultured in media containing phenol red had the 1,25D 3-MARRS receptor and actin localized largely in the nucleus, which was dispersed upon addition of (OH) 2 1,25(OH) 2D 3. In the absence of phenol red, staining was cytoplasmic. Addition of steroid caused diminished staining at 10 s and 30 s, with a return of intensity between 1 and 5 min. Nuclear staining was observed after 1 min. We found that F-actin concentrations are maximal when 1,25D 3-MARRS receptor localizations within enterocytes are low suggesting that cyclical conversions of F-actin to G-actin are involved in the 1,25(OH) 2D 3-mediated redistribution of the 1,25D 3-MARRS receptor within the cell. We also found that keratin distribution remains constant with 1,25(OH) 2D 3 exposure when Factin depolymerizes into G-actin, which suggests that actin and keratin work in concert to facilitate hormonemediated redistribution of the 1,25D 3-MARRS receptor. We subsequently investigated whether the cyclical redistribution was related to either 1,25(OH) 2D 3-stimulated phosphate or calcium uptake, but no congruent pattern was found.

          Related collections

          Most cited references32

          • Record: found
          • Abstract: found
          • Article: not found

          Ribozyme knockdown functionally links a 1,25(OH)2D3 membrane binding protein (1,25D3-MARRS) and phosphate uptake in intestinal cells.

          B Rohe, Mary Farach-Carson, S Safford … (2004)
          We used a ribozyme loss-of-function approach to demonstrate that the protein product of a cDNA encoding a multifunctional membrane-associated protein binds the seco-steroid 1,25(OH)(2)D(3) and transduces its stimulatory effects on phosphate uptake. These results are paralleled by studies in which the ability of the hormone to stimulate phosphate uptake in isolated chick intestinal epithelial cells is abolished by preincubation with Ab099 directed against the amino terminus of the protein. We now report the complete sequence of the cloned chicken cDNA for the 1,25D(3)-MARRS (membrane-associated, rapid-response steroid-binding) protein and reveal it to be identical to the multifunctional protein ERp57. Functional studies showed that active ribozyme, but not a scrambled control, decreased specific membrane-associated 1,25(OH)(2)D(3) binding, but did not affect binding to the nuclear receptor for 1,25(OH)(2)D(3). Seco-steroid-dependent stimulation of protein kinase C activity was diminished as 1,25D(3)-MARRS protein levels were reduced in the presence of the ribozyme, as judged by Western blot analyses. Phosphate uptake in isolated cells is an index of intestinal phosphate transport that occurs during growth and maturation. Whereas cells and perfused duodena robustly responded to 1,25(OH)(2)D(3) in preparations from young birds, older animals no longer responded with stimulated phosphate uptake or transport. The age-related decline was accompanied by a decrease in 1,25D(3)-MARRS mRNA that was apparent up to 1 year of age. Together, these studies functionally link phosphate transport in the chick duodenum with the 1,25D(3)-MARRS protein and point to a previously uncharacterized role for this multifunctional protein class.
          Article 0 comments Cited 39 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            A systematic model to predict transcriptional regulatory mechanisms based on overrepresentation of transcription factor binding profiles.

            Rakesh Nagarajan, Gary Stormo, Wei-Ting Chang … (2006)
            An important aspect of understanding a biological pathway is to delineate the transcriptional regulatory mechanisms of the genes involved. Two important tasks are often encountered when studying transcription regulation, i.e., (1) the identification of common transcriptional regulators of a set of coexpressed genes; (2) the identification of genes that are regulated by one or several transcription factors. In this study, a systematic and statistical approach was taken to accomplish these tasks by establishing an integrated model considering all of the promoters and characterized transcription factors (TFs) in the genome. A promoter analysis pipeline (PAP) was developed to implement this approach. PAP was tested using coregulated gene clusters collected from the literature. In most test cases, PAP identified the transcription regulators of the input genes accurately. When compared with chromatin immunoprecipitation experiment data, PAP's predictions are consistent with the experimental observations. When PAP was used to analyze one published expression-profiling data set and two novel coregulated gene sets, PAP was able to generate biologically meaningful hypotheses. Therefore, by taking a systematic approach of considering all promoters and characterized TFs in our model, we were able to make more reliable predictions about the regulation of gene expression in mammalian organisms.
            Article 0 comments Cited 32 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Identification of a specific binding protein for 1 alpha,25-dihydroxyvitamin D3 in basal-lateral membranes of chick intestinal epithelium and relationship to transcaltachia.

              Suzan Hammond, W. Okamura, W. Ray Norman … (1994)
              The steroid hormone 1 alpha,25-dihydroxyvitamin D3 (1 alpha,25-(OH)2D3) elicits biological responses by both genomic and nongenomic pathways. This report describes purification of a receptor for 1 alpha,25-(OH)2D3 (VDR) located in the basal-lateral membrane (BLM) of vitamin D-replete chick intestinal epithelium, which is implicated in the nongenomic stimulation of calcium transport (transcaltachia). The BLM-VDR exhibited saturable binding for [3H]1,25-(OH)2D3 (KD = 0.72 x 10(-9)M, Bmax = 0.24 pmol/mg of protein). A 4500-fold purification of the BLM-VDR receptor was achieved. In addition, saturable binding was observed for [3H]24R,25-(OH)2D3 at physiologically relevant levels (KD = 19 x 10(-9) M, Bmax = 2.4 pmol/mg of protein) to a component apparently distinct from the 1 alpha,25-(OH)2D3 BLM-VDR. A functional correlation between the BLM-VDR and transcaltachia was observed in three experimental situations: (i) vitamin D deficiency, which suppresses transcaltachia, resulted in reduced specific [3H]1 alpha,25-(OH)2D3 binding in the BLM-VDR, relative to corresponding fractions from vitamin D-replete chicks; (ii) the BLM-VDR exhibited down-regulation of specific [3H]1 alpha,25-(OH)2D3 binding following exposure to nonradioactive 1 alpha,25-(OH)2D3; and (iii) the relative potencies of two "6-s-cis" analogs of 1 alpha,25-(OH)2D3 to initiate transcaltachia and their ability to compete with [3H]1 alpha,25-(OH)2D3 for binding to the BLM-VDR were parallel. The combined results support the existence of a plasmalemal 1 alpha,25-(OH)2D3 receptor which is a prime candidate for signal transduction in transcaltachia.
              Article 0 comments Cited 23 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Journal
                Journal ID (nlm-ta): Immunol Endocr Metab Agents Med Chem
                Journal ID (iso-abbrev): Immunol Endocr Metab Agents Med Chem
                Journal ID (publisher-id): IEMAMC
                Title: Immunology, Endocrine & Metabolic Agents in Medicinal Chemistry
                Publisher: Bentham Science Publishers
                ISSN (Print): 1871-5222
                ISSN (Electronic): 1875-6115
                Publication date (Print): August 2014
                Publication date (Electronic): August 2014
                Volume: 14
                Issue: 2
                Pages: 55-66
                Affiliations
                Department of Nutrition, Dietetic and Food Science, Utah State University, Logan, UT 84322-8700, USA
                Author notes
                [* ]Address correspondence to this author at the Department of Nutrition, Dietetic and Food Science, Utah State University, Logan, UT 84322-8700, USA; Tel: 435 797-3286; E-mail: Ilka.nemere@ 123456usu.edu
                Article
                Publisher ID: IEMAMC-14-55
                DOI: 10.2174/1871522214666140704171342
                PMC ID: 4443791
                PubMed ID: 26029286
                SO-VID: 26f86aa5-634a-4e2a-851d-61a58db16ce8
                Copyright © © 2014 Bentham Science Publishers
                License:

                This is an open access article licensed under the terms of the Creative Commons Attribution Non-Commercial License ( http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.

                History
                Date received : 23 September 2013
                Date revision received : 7 July 2014
                Date accepted : 23 July 2014
                Categories
                Subject: Article

                Keywords: 1,25d3-marrs receptor/pdia3/erp57,binding partner,microfilaments,intestinal cells,vitamin d
                Data availability:
                Keywords: 1,25d3-marrs receptor/pdia3/erp57, binding partner, microfilaments, intestinal cells, vitamin d

                Comments

                Comment on this article

                scite_

                Similar content176

                See all similar

                Cited by3

                See all cited by

                Most referenced authors120

                See all reference authors