Quantitative analysis of low molecular weight G-actin-binding proteins, cofilin, ADF and profilin, expressed in developing and degenerating chicken skeletal muscles

1996 ◽  
Vol 17 (4) ◽  
pp. 463-473 ◽  
Author(s):  
Rie Nagaoka ◽  
Narihiro Minami ◽  
Kimihide Hayakawa ◽  
Hiroshi Abe ◽  
Takashi Obinata
Keyword(s):  
Molecular Weight ◽  
Quantitative Analysis ◽  
Skeletal Muscles ◽  
Binding Proteins ◽  
Actin Binding ◽  
Low Molecular Weight ◽  
Actin Binding Proteins

Isolation of Low Molecular Weight Actin-Binding Proteins from Porcine Brain1

1984 ◽  
Vol 95 (2) ◽  
pp. 377-385 ◽  
Author(s):  
Shohei MAEKAWA ◽  
Eisuke NISHIDA ◽  
Yasutaka OHTA ◽  
Hikoichi SAKAI
Keyword(s):  
Molecular Weight ◽  
Binding Proteins ◽  
Actin Binding ◽  
Low Molecular Weight ◽  
Actin Binding Proteins

scholarly journals Low Molecular-weight G-actin Binding Proteins Involved in the Regulation of Actin Assembly during Myofibrillogenesis.

1997 ◽  
Vol 22 (1) ◽  
pp. 181-189 ◽  
Author(s):  
Takashi Obinata ◽  
Rie Nagaoka-Yasuda ◽  
Shoichiro Ono ◽  
Kenichi Kusano ◽  
Kurato Mohri ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Binding Proteins ◽  
Actin Binding ◽  
Low Molecular Weight ◽  
Actin Assembly ◽  
Actin Binding Proteins

A quantitative analysis of G-actin binding proteins and the G-actin pool in developing chick brain

1999 ◽  
Vol 823 (1-2) ◽  
pp. 129-140 ◽  
Author(s):  
N Devineni ◽  
L.S Minamide ◽  
M Niu ◽  
D Safer ◽  
R Verma ◽  
...  
Keyword(s):  
Quantitative Analysis ◽  
Binding Proteins ◽  
Actin Binding ◽  
Chick Brain ◽  
Actin Binding Proteins

The Actin Lattice: Composition, Structure and Membrane Attachment

1980 ◽  
Vol 38 ◽  
pp. 420-423
Author(s):  
J. Condeelis ◽  
J. Wolosewick
Keyword(s):  
Molecular Weight ◽  
Binding Proteins ◽  
Muscle Cells ◽  
Actin Binding ◽  
Cellular Slime Mold ◽  
Actin Binding Proteins ◽  
Cellular Slime ◽  
Composition Structure ◽  
And Control

Actin containing structures in the cytoplasm of non-muscle cells have been implicated in cell locomotion and control of the distribution of cytoplasmic and cell surface components. Consistent with this versatility of actin function is the complexity of actin containing structures that are found in non-muscle cells. Actin is a highly conserved protein with identical functional properties from cell to cell. Recently a number of actin binding proteins have been purified that may account for the assembly of actin into the different structures found in vivo. We have been investigating the actin binding proteins that are responsible for Ca++ regulated gelation of actin that was first documented in cell free extracts of Dictyostelium discoideum, a cellular slime mold. In this case these actin binding proteins will be referred to as gelation factors. Our method for purifying the gelation factors from Dictyostelium is briefly outlined as follows. Cell free extracts that contained gelation activity were fractionated with ammonium sulfate into O-45 and 45-60% pellets. Gelation activity in each pellet was purified by chromatography. The 45-60% pellet contained 95% of the gelation activity in the extract and was resolved into two gelation factors that measure 250,000 daltons and 120,000 daltons in SDS (Figure 1 b and d respectively). The remaining 5? of the gelation activity that was collected in the 0-40% pellet was recovered with a complex of 5 low molecular weight components that measure 48,000, 38,000, 32,000, 24,000 and 20,000 daltons in SDS (Figure le). The polypeptides appear to be proteolytic breakdown products of higher molecular weight gelation factors since their presence in the extract was abolished by inclusion of proteolytic inhibtors.

Rap1b Association with the Platelet Cytoskeleton Occurs in the Absence of Glycoproteins IIb/IIIa

1998 ◽  
Vol 79 (04) ◽  
pp. 832-836 ◽  
Author(s):  
Thomas Fischer ◽  
Christina Duffy ◽  
Gilbert White
Keyword(s):  
Molecular Weight ◽  
Divalent Cation ◽  
Binding Proteins ◽  
Binding Protein ◽  
Platelet Membrane ◽  
Low Molecular Weight ◽  
Membrane Glycoproteins ◽  
Gtp Binding Protein ◽  
Gtp Binding Proteins ◽  
Gtp Binding

SummaryPlatelet membrane glycoproteins (GP) IIb/IIIa and rap1b, a 21 kDa GTP binding protein, associate with the triton-insoluble, activation-dependent platelet cytoskeleton with similar rates and divalent cation requirement. To examine the possibility that GPIIb/IIIa was required for rap1b association with the cytoskeleton, experiments were performed to determine if the two proteins were linked under various conditions. Chromatography of lysates from resting platelets on Sephacryl S-300 showed that GPIIb/IIIa and rap1b were well separated and distinct proteins. Immunoprecipitation of GPIIb/IIIa from lysates of resting platelets did not produce rap1b or other low molecular weight GTP binding proteins and immunoprecipitation of rap1b from lysates of resting platelets did not produce GPIIb/IIIa. Finally, rap1b was associated with the activation-dependent cytoskeleton of platelets from a patient with Glanzmann’s thrombasthenia who lacks surface expressed glycoproteins IIb and IIIa. Based on these findings, we conclude that no association between GPIIb/IIIa and rap1b is found in resting platelets and that rap1b association with the activation-dependent cytoskeleton is at least partly independent of GPIIb/IIIa.

Actin-binding proteins sensitively mediate actin bundle stiffness

2006 ◽  
Vol 39 ◽  
pp. S240
Author(s):  
M. Bathe ◽  
M. Claessens ◽  
E. Frey ◽  
A. Bausch
Keyword(s):  
Binding Proteins ◽  
Actin Binding ◽  
Actin Binding Proteins ◽  
Actin Bundle

A review of actin binding proteins: new perspectives

2007 ◽  
Vol 36 (1) ◽  
pp. 121-125 ◽  
Author(s):  
Ricardo Uribe ◽  
David Jay
Keyword(s):  
Binding Proteins ◽  
Actin Binding ◽  
Actin Binding Proteins
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