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Affiliation

1 Institute of Interdisciplinary Research, School of Medicine, Free University of Brussels, Belgium.

T Saito et al.

Exp Cell Res .

1994 May .

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1 Institute of Interdisciplinary Research, School of Medicine, Free University of Brussels, Belgium.

Meberg PJ, Ono S, Minamide LS, Takahashi M, Bamburg JR.
Meberg PJ, et al.
Cell Motil Cytoskeleton. 1998;39(2):172-90. doi: 10.1002/(SICI)1097-0169(1998)39:2<172::AID-CM8>3.0.CO;2-8.
Cell Motil Cytoskeleton. 1998.

PMID: 9484959

Shaw AE, Minamide LS, Bill CL, Funk JD, Maiti S, Bamburg JR.
Shaw AE, et al.
Electrophoresis. 2004 Aug;25(15):2611-20. doi: 10.1002/elps.200406017.
Electrophoresis. 2004.

PMID: 15300782

Yeoh S, Pope B, Mannherz HG, Weeds A.
Yeoh S, et al.
J Mol Biol. 2002 Jan 25;315(4):911-25. doi: 10.1006/jmbi.2001.5280.
J Mol Biol. 2002.

PMID: 11812157

Ono S.
Ono S.
Biochemistry. 2003 Nov 25;42(46):13363-70. doi: 10.1021/bi034600x.
Biochemistry. 2003.

PMID: 14621980

Review.

Kuhn TB, Meberg PJ, Brown MD, Bernstein BW, Minamide LS, Jensen JR, Okada K, Soda EA, Bamburg JR.
Kuhn TB, et al.
J Neurobiol. 2000 Aug;44(2):126-44.
J Neurobiol. 2000.

PMID: 10934317

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Go YM, Orr M, Jones DP.
Go YM, et al.
Am J Physiol Lung Cell Mol Physiol. 2013 Dec;305(11):L831-43. doi: 10.1152/ajplung.00203.2013. Epub 2013 Sep 27.
Am J Physiol Lung Cell Mol Physiol. 2013.

PMID: 24077948
Free PMC article.

Castano E, Philimonenko VV, Kahle M, Fukalová J, Kalendová A, Yildirim S, Dzijak R, Dingová-Krásna H, Hozák P.
Castano E, et al.
Histochem Cell Biol. 2010 Jun;133(6):607-26. doi: 10.1007/s00418-010-0701-2. Epub 2010 May 5.
Histochem Cell Biol. 2010.

PMID: 20443021

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Bamburg JR, Bernstein BW, Davis RC, Flynn KC, Goldsbury C, Jensen JR, Maloney MT, Marsden IT, Minamide LS, Pak CW, Shaw AE, Whiteman I, Wiggan O.
Bamburg JR, et al.
Curr Alzheimer Res. 2010 May;7(3):241-50. doi: 10.2174/156720510791050902.
Curr Alzheimer Res. 2010.

PMID: 20088812
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Ono K, Ono S.
Ono K, et al.
Cell Motil Cytoskeleton. 2009 Jul;66(7):398-408. doi: 10.1002/cm.20383.
Cell Motil Cytoskeleton. 2009.

PMID: 19459188
Free PMC article.

Ouellet F, Carpentier E, Cope MJ, Monroy AF, Sarhan F.
Ouellet F, et al.
Plant Physiol. 2001 Jan;125(1):360-8. doi: 10.1104/pp.125.1.360.
Plant Physiol. 2001.

PMID: 11154343
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Using separation of total cellular proteins by two dimensional (2-D) gel electrophoresis (isoelectric focusing/SDS-PAGE) we have characterized two regulated proteins, p21 and p19, in dog thyroid cells. We have used the same 2-D gel technique to purify these proteins before their trypsin cleavage and partial sequencing. Three peptides were sequenced in the case of p19 and two peptides in the case of p21. The Swiss-Prot protein sequence database revealed that p19 was identical to destrin/ADF (actin depolymerizing factor) and p21 to cofilin, two closely related and widely distributed actin-binding proteins. This was further verified by cross-reactivity with specific antibodies against brain cofilin and chicken ADF. We have demonstrated, using 2-D gel electrophoresis with a nonequilibrium pH gradient in the first dimension (nonequilibrium pH gradient in the first dimension (nonequilibrium pH gradient electrophoresis/SDS-PAGE) that, in the thyroid cell, cofilin and destrin/ADF were present, under control conditions, in two forms: a phosphorylated and an unphosphorylated one. Thyrotropin (TSH), through cyclic AMP, provoked a very rapid dephosphorylation of these two proteins, which was already maximal after 20 min of action, whereas their dephosphorylation in response to 12-O-tetradecanoylphorbol-13-acetate (TPA) was slower. This suggests that dephosphorylation of cofilin and destrin/ADF by TSH could be implicated in the disruption of actin-containing stress fibers and in the reorganization of microfilaments induced by this hormone. Epidermal growth factor, which does not induce acute morphological changes in thyroid cells, did not affect the state of phosphorylation of cofilin and destrin/ADF except for a delayed decrease (after 24 h) of destrin/ADF phosphorylation. A 10% dimethyl sulfoxide treatment of thyroid cells also induced rapid dephosphorylation of destrin and cofilin. This was accompanied by a reorganization of actin microfilaments that clearly resembles the one induced by TSH and by the appearance of intranuclear cofilin-containing rods. However, these rod structures were not observed in response to TSH, forskolin, or TPA, suggesting that dephosphorylation of cofilin correlates with the reorganization of actin microfilaments but not with the nuclear transport of cofilin. We propose that the dephosphorylation of destrin and cofilin could be involved in the TSH-stimulated macropinocytic activity, a key process in thyroid hormone secretion.

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