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Gene Review

Dstnl1  -  destrin-like 1

Rattus norvegicus

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Disease relevance of LOC296197

  • Since p17a and p17b were predominant forms even in nonstimulated cells, peptides were generated from them with Staphylococcus aureus V8 protease or cyanogen bromide; subsequent sequencing of these peptides and homology search allowed identification of p17a and p17b as destrin- and cofilin-like proteins, respectively [1].
  • Collectively, these data indicate that ischemia induces ADF activation and relocalization to the apical domain before microvillar destruction [2].

High impact information on LOC296197

  • This increase in F-actin content is dependent on NMDA receptor activation and involves the inactivation of actin depolymerizing factor/cofilin [3].
  • We also found that dBcAMP and ML-9 both cause a decrease in the phosphate content of actin depolymerizing factor, suggesting that this protein and myosin light chain are the effectors of actin cytoskeleton reorganization and process growth [4].
  • Because destrin and cofilin are actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation, the two parotid proteins reported here might be involved in cortical F-actin disruption observed in parallel with exocytotic amylase secretion [1].
  • Identification of two 17-kDa rat parotid gland phosphoproteins, subjects for dephosphorylation upon beta-adrenergic stimulation, as destrin- and cofilin-like proteins [1].
  • This repressor factor and the positively acting age-dependent factor, ADF, described earlier (Supakar, P. C., Song, C. S., Jung, M. H., Slomczynska, M. A., Kim, J.-M., Vellanoweth, R. L., Chatterjee, B. & Roy, A. K. (1993) J. Biol. Chem. 268, 26400-26408) function to coordinate the tissue-specific down-regulation of the rAR gene during aging [5].

Biological context of LOC296197


Anatomical context of LOC296197

  • Beta-adrenergic or cholinergic stimulation of the rat parotid gland was earlier shown to induce dephosphorylation of endogenous destrin- and cofilin-like proteins, which are phosphorylated in resting cells at Ser residues probably present near the N-terminals [6].
  • The results suggest that tropomyosin-free actin filaments under the membrane can participate in rapid, dynamic processes that depend on interactions between the activities of the Arp2/3 complex and ADF/cofilin that tropomyosin inhibits elsewhere in the cell [9].
  • Ischemic-induced cell injury results in rapid duration-dependent actin-depolymerizing factor (ADF)/cofilin-mediated disruption of the apical microvilli microfilament cores [10].
  • ADF immunoreactivity was found in Purkinje cells, but not in granule cells [11].
  • ADF staining was uniformly distributed throughout the entire dendritic arborization of the Purkinje cell, while filamentous actin is highly concentrated in the dendritic spines, indicating that ADF activity might vary according to its cellular localization [11].

Associations of LOC296197 with chemical compounds

  • Earlier work had shown that partial cleavage of the phosphorylated destrin- and cofilin-like proteins with cyanogen bromide provides unphosphorylated 16.7- and 18.3-kDa fragments, respectively [6].
  • The Triton-soluble ADF concentration remained stable throughout development [11].

Analytical, diagnostic and therapeutic context of LOC296197

  • To directly investigate this hypothesis, we examined the intracellular localization of ADF in ischemic rat cortical tissues by immunofluorescence and quantified the concentration of ADF in brush-border membrane vesicles prepared from ischemic rat kidneys by using Western blot techniques [2].
  • Light and electron microscopic immunocytochemistry showed that ADF was not detected in all cerebellar cells [11].
  • Initial immunofluorescence and Western blot studies on cortical tissue documented the presence of ADF in proximal tubule cells [12].


  1. Identification of two 17-kDa rat parotid gland phosphoproteins, subjects for dephosphorylation upon beta-adrenergic stimulation, as destrin- and cofilin-like proteins. Kanamori, T., Hayakawa, T., Suzuki, M., Titani, K. J. Biol. Chem. (1995) [Pubmed]
  2. Ischemic injury induces ADF relocalization to the apical domain of rat proximal tubule cells. Ashworth, S.L., Sandoval, R.M., Hosford, M., Bamburg, J.R., Molitoris, B.A. Am. J. Physiol. Renal Physiol. (2001) [Pubmed]
  3. Hippocampal LTP is accompanied by enhanced F-actin content within the dendritic spine that is essential for late LTP maintenance in vivo. Fukazawa, Y., Saitoh, Y., Ozawa, F., Ohta, Y., Mizuno, K., Inokuchi, K. Neuron (2003) [Pubmed]
  4. Astrocyte process growth induction by actin breakdown. Baorto, D.M., Mellado, W., Shelanski, M.L. J. Cell Biol. (1992) [Pubmed]
  5. Nuclear factor kappa B functions as a negative regulator for the rat androgen receptor gene and NF-kappa B activity increases during the age-dependent desensitization of the liver. Supakar, P.C., Jung, M.H., Song, C.S., Chatterjee, B., Roy, A.K. J. Biol. Chem. (1995) [Pubmed]
  6. Complete amino acid sequences and phosphorylation sites, determined by Edman degradation and mass spectrometry, of rat parotid destrin- and cofilin-like proteins. Kanamori, T., Suzuki, M., Titani, K. Arch. Oral Biol. (1998) [Pubmed]
  7. Phosphorylation of actin-depolymerizing factor/cofilin by LIM-kinase mediates amyloid beta-induced degeneration: a potential mechanism of neuronal dystrophy in Alzheimer's disease. Heredia, L., Helguera, P., de Olmos, S., Kedikian, G., Solá Vigo, F., LaFerla, F., Staufenbiel, M., de Olmos, J., Busciglio, J., Cáceres, A., Lorenzo, A. J. Neurosci. (2006) [Pubmed]
  8. Synthesis and preliminary pharmacological investigation of some 2-[4-(dialkylaminoalkoxy)phenyl]benzotriazoles and their N-oxides. Sparatore, A., Sparatore, F. Farmaco (1998) [Pubmed]
  9. Spatial regulation of actin dynamics: a tropomyosin-free, actin-rich compartment at the leading edge. DesMarais, V., Ichetovkin, I., Condeelis, J., Hitchcock-DeGregori, S.E. J. Cell. Sci. (2002) [Pubmed]
  10. Renal ischemia induces tropomyosin dissociation-destabilizing microvilli microfilaments. Ashworth, S.L., Wean, S.E., Campos, S.B., Temm-Grove, C.J., Southgate, E.L., Vrhovski, B., Gunning, P., Weinberger, R.P., Molitoris, B.A. Am. J. Physiol. Renal Physiol. (2004) [Pubmed]
  11. Actin-depolymerizing factor (ADF) in the cerebellum of the developing rat: a quantitative and immunocytochemical study. Léna, J.Y., Bamburg, J.R., Rabié, A., Faivre-Sarrailh, C. J. Neurosci. Res. (1991) [Pubmed]
  12. Ischemia activates actin depolymerizing factor: role in proximal tubule microvillar actin alterations. Schwartz, N., Hosford, M., Sandoval, R.M., Wagner, M.C., Atkinson, S.J., Bamburg, J., Molitoris, B.A. Am. J. Physiol. (1999) [Pubmed]
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