Biochemical and immunological characterization of pea nuclear intermediate filament proteins

Planta ◽  
2004 ◽  
Vol 218 (6) ◽  
pp. 965-975 ◽  
Author(s):  
Gregory B. Clark ◽  
Stanley J. Roux ◽  
Sonal S. D. Blumenthal
Keyword(s):  
Intermediate Filament ◽  
Intermediate Filament Proteins ◽  
Immunological Characterization

scholarly journals The characterization of an acidic calmodulin-binding protein in brain cytoskeleton and membrane fractions

1986 ◽  
Vol 240 (2) ◽  
pp. 593-596
Author(s):  
P Strocchi ◽  
J M Gilbert
Keyword(s):  
Intermediate Filament ◽  
Gel Electrophoresis ◽  
Binding Protein ◽  
Two Dimensional ◽  
Proteolytic Digestion ◽  
Two Dimensional Gel Electrophoresis ◽  
Intermediate Filament Proteins ◽  
Calmodulin Binding ◽  
Acidic Proteins

One of the most abundant acidic proteins in rat brain has an Mr of 68,000 and a pI of 5.6 (68K 5.6 protein) when analysed by two-dimensional gel electrophoresis. The 68K 5.6 protein was found in large relative amounts in brain cytoskeleton preparations and in membrane and supernatant fractions. High-salt washing and proteolytic digestion did not remove this protein from the membrane elements. The 68K 5.6 protein was also found in the microtubule-associated protein fraction of purified microtubules and was present in large relative amounts in preparations of intermediate-filament proteins. The 68K 5.6 protein binds to calmodulin in the presence of Ca2+ ions, and we found it to be an abundant acidic calmodulin-binding protein in brain tissue.

Immunological characterization of lamins in the nuclear matrix of onion cells

1993 ◽  
Vol 106 (1) ◽  
pp. 431-439 ◽  
Author(s):  
A. Minguez ◽  
S. Moreno Diaz de la Espina
Keyword(s):  
Intermediate Filaments ◽  
Nuclear Matrix ◽  
Intermediate Filament ◽  
Higher Plants ◽  
Nuclear Periphery ◽  
Immunogold Labelling ◽  
Root Cells ◽  
Intermediate Filament Proteins ◽  
Lamin B

We have used polyclonal and monoclonal antibodies against different lamins from vertebrates, and the IFA antibody recognizing all kinds of intermediate filament proteins, to investigate the lamins of the nuclear matrix of Allium cepa meristematic root cells. All the antibodies react in the onion nuclear matrix with bands in the range of 60–65 kDa, which are enriched in the nuclear matrix after urea extraction, and do not crossreact with other antibodies recognizing intermediate filaments in plants (AFB, anti-vimentin and MAC 322), ruling out crossreaction with contaminating intermediate filaments of cytoplasmic bundles. In 2-D blots the chicken anti-lamin serum reacts with one spot at 65 kDa and pI 6.8 and the anti B-type lamin antibodies with another one at 64 kDa and pI 5.75. Both crossreact with IFA. The lamin is localized at the nuclear periphery and the lamina by indirect immunofluorescence. Immunogold labelling of nuclear matrix sections reveals that the protein is not only associated with the lamina, but also with the internal matrix. Taken together these results reveal that higher plants, which do not possess an organized network of cytoplasmic intermediate filaments, nevertheless present a well-organized lamina containing lamins in which at least one of them is immunologically related to vertebrate lamin B. Our data confirm that lamins are very old members of the intermediate filament proteins that have been better conserved in plants during evolution than their cytoplasmic counterparts.

Characterization of the in vitro co-assembly process of the intermediate filament proteins vimentin and desmin: mixed polymers at all stages of assembly

2005 ◽  
Vol 84 (2-3) ◽  
pp. 379-391 ◽  
Author(s):  
Ute Wickert ◽  
Norbert Mücke ◽  
Tatjana Wedig ◽  
Shirley A. Müller ◽  
Ueli Aebi ◽  
...  
Keyword(s):  
Intermediate Filament ◽  
Assembly Process ◽  
Intermediate Filament Proteins

Characterization of dimer subunits of intermediate filament proteins

1986 ◽  
Vol 192 (2) ◽  
pp. 337-349 ◽  
Author(s):  
Roy A. Quinlan ◽  
Mechthild Hatzfeld ◽  
Werner W. Franke ◽  
Ariel Lustig ◽  
Theresa Schulthess ◽  
...  
Keyword(s):  
Intermediate Filament ◽  
Intermediate Filament Proteins

Expression of Intermediate Filament Proteins in the Adult Human Vestibular Labyrinth

1992 ◽  
Vol 101 (6) ◽  
pp. 479-486 ◽  
Author(s):  
Louis J. J. M. Bauwens ◽  
John C. M. J. De Groot ◽  
Jan E. Veldman ◽  
Frans C. S. Ramaekers ◽  
Egbert H. Huizing
Keyword(s):  
Intermediate Filament ◽  
Neurofilament Proteins ◽  
Intense Staining ◽  
Intermediate Filament Proteins ◽  
Vestibular Labyrinth ◽  
Mechanoelectrical Transduction ◽  
Adult Human ◽  
Sensory Epithelia ◽  
Human Cochlea

The immunohistochemical detection of intermediate filament proteins, cytoskeletal constituents that allow the characterization of tissues, was investigated in frozen sections of the chemically fixed, nondecalcified, adult human vestibular labyrinth. Cytokeratins (CKs) were detected in all epithelia (including the sensory epithelia), although substantial differences in the degree of staining between individual cells occurred. The expression of CKs 7, 8, 18, and 19 as detected with our subunit-specific monoclonal antibodies in the vestibular epithelia is typical of “simple” epithelia and is identical to the CK subtypes found in the human cochlea. Although immunostaining for CK 7 was very weak and was limited to certain vestibular wall cells, the other CKs demonstrated a pronounced and rather uniform distribution throughout the different epithelia. All epithelia (including the sensory epithelia) displayed expression of vimentin, thus demonstrating co-expression with CKs. Vimentin was also present in the subepithelial connective tissue fibroblasts and mesothelial lining of the vestibular labyrinth. Neurofilament proteins were detected in all neuronal structures. The intense staining for CKs in the maculae and cristae implies that these sensory organs are rigid structures, a finding that may possibly be of importance in the mechanoelectrical transduction process for the sense of equilibrium.

Sign in / Sign up

Export Citation Format

Share Document