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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

Arhgap17  -  Rho GTPase activating protein 17

Mus musculus

Synonyms: 5730403H17Rik, Nadrin, Nadrin2, Neuron-associated developmentally-regulated protein, Rho GTPase-activating protein 17, ...
 
 
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Disease relevance of Arhgap17

  • Differences noted in enzyme II directed RNA synthesis under varying salt conditions in nuclei isolated from uninfected and Friend virus (FV)-infected spleen cells, have been attributed to chromosomal modifications (Babcock and Rich 1973) [1].
  • Regulation of Secreted Protein Acidic and Rich in Cysteine during Adipose Conversion and Adipose Tissue Hyperplasia [2].
 

High impact information on Arhgap17

  • Using synthetic peptides, we have identified two distinct regions of the glycoprotein SPARC (Secreted Protein Acidic and Rich in Cysteine) (osteonectin/BM-40) that inhibit cell spreading [3].
  • Oxidative Stress Induces Premature Senescence by Stimulating Caveolin-1 Gene Transcription through p38 Mitogen-Activated Protein Kinase/Sp1-Mediated Activation of Two GC-Rich Promoter Elements [4].
  • Here, we demonstrate that Secreted Protein, Acidic, Rich in Cysteine, SPARC, predominantly secreted by mesenchymal parietal endoderm specifically promotes early myocardial cell differentiation in embryoid bodies [5].
  • SPARC (Secreted Protein Acidic and Rich in Cysteine) is a multifunctional glycoprotein belonging to a group of matrix-associated factors that mediate cell-extracellular matrix interactions but have no structural roles [6].
  • Proliferating Leydig cells also exhibit elevated levels of mRNA for SPARC (Secreted Protein, Acidic and Rich in Cysteine), a Ca2(+)-binding glycoprotein associated with changes in cell shape that accompany morphogenesis and tissue remodeling [7].
 

Biological context of Arhgap17

 

Anatomical context of Arhgap17

  • SPARC (Secreted Protein that is Acidic and Rich in Cysteine) is a Ca2+-binding, stress-related protein released in vitro by both malignant and normal cells derived from all primordial germ layers [11].
 

Analytical, diagnostic and therapeutic context of Arhgap17

  • SPARC (Secreted Protein, Acidic, Rich in Cysteine) was detected by immunohistochemistry in the sensorial layer of the bilayered embryonic epidermis of Xenopus laevis during neurulation, when a subset of the sensorial cells are selected to differentiate into ciliated cell precursors [12].

References

  1. Temporal changes in chromatin isolated from Friend virus-infected mouse spleens. Musser, D.A., Fiel, R.J. Cancer Biochem. Biophys. (1976) [Pubmed]
  2. Regulation of Secreted Protein Acidic and Rich in Cysteine during Adipose Conversion and Adipose Tissue Hyperplasia. Chavey, C., Boucher, J., Monthou??l-Kartmann, M.N., Sage, E.H., Castan-Laurell, I., Valet, P., Tartare-Deckert, S., Van Obberghen, E. Obesity (Silver Spring, Md.) (2006) [Pubmed]
  3. Functional mapping of SPARC: peptides from two distinct Ca+(+)-binding sites modulate cell shape. Lane, T.F., Sage, E.H. J. Cell Biol. (1990) [Pubmed]
  4. Oxidative Stress Induces Premature Senescence by Stimulating Caveolin-1 Gene Transcription through p38 Mitogen-Activated Protein Kinase/Sp1-Mediated Activation of Two GC-Rich Promoter Elements. Dasari, A., Bartholomew, J.N., Volonte, D., Galbiati, F. Cancer Res. (2006) [Pubmed]
  5. Parietal endoderm secreted SPARC promotes early cardiomyogenesis in vitro. Stary, M., Pasteiner, W., Summer, A., Hrdina, A., Eger, A., Weitzer, G. Exp. Cell Res. (2005) [Pubmed]
  6. Development of UV-induced squamous cell carcinomas is suppressed in the absence of SPARC. Aycock, R.L., Bradshaw, A.C., Sage, E.H., Starcher, B. J. Invest. Dermatol. (2004) [Pubmed]
  7. Adhesion, shape, proliferation, and gene expression of mouse Leydig cells are influenced by extracellular matrix in vitro. Vernon, R.B., Lane, T.F., Angello, J.C., Sage, H. Biol. Reprod. (1991) [Pubmed]
  8. Expression of SC1 is associated with the migration of myotomes along the dermomyotome during somitogenesis in early mouse embryos. Ringuette, M., Rogers, I., Varmuza, S., Rush, S., Brown, I.R. Dev. Genes Evol. (1998) [Pubmed]
  9. Structures and structure-activity relationships of three mitogenic and complement fixing pectic arabinogalactans from the malian antiulcer plants Cochlospermum tinctorium A. Rich and Vernonia kotschyana Sch. Bip. ex Walp. Nergard, C.S., Kiyohara, H., Reynolds, J.C., Thomas-Oates, J.E., Matsumoto, T., Yamada, H., Patel, T., Petersen, D., Michaelsen, T.E., Diallo, D., Paulsen, B.S. Biomacromolecules (2006) [Pubmed]
  10. Regulated expression of an osteonectin variant in bovine aortic endothelial cells. Jeon, H., Niimi, T., Taniguchi, Y., Miki, K., Kitagawa, Y. Biosci. Biotechnol. Biochem. (1994) [Pubmed]
  11. SPARC: a Ca2+-binding extracellular protein associated with endothelial cell injury and proliferation. Sage, H., Decker, J., Funk, S., Chow, M. J. Mol. Cell. Cardiol. (1989) [Pubmed]
  12. Association of SPARC (osteonectin, BM-40) with extracellular and intracellular components of the ciliated surface ectoderm of Xenopus embryos. Huynh, M.H., Hong, H., Delovitch, S., Desser, S., Ringuette, M. Cell Motil. Cytoskeleton (2000) [Pubmed]
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