Uses of Conventional and Monoclonal Antibodies to Intermediate Filament Proteins in the Diagnosis of Human Tumours

1984 ◽  
pp. 148-159 ◽  
Author(s):  
M. Osborn ◽  
E. Debus ◽  
M. Altmannsberger ◽  
K. Weber
Keyword(s):  
Monoclonal Antibodies ◽  
Intermediate Filament ◽  
Intermediate Filament Proteins ◽  
Human Tumours

Differential diagnosis of genitourinary tumors using monoclonal antibodies to intermediate filament proteins

Urology ◽  
1989 ◽  
Vol 33 (5) ◽  
pp. 433-439
Author(s):  
Steven A. Lofton ◽  
Allen M. Gown ◽  
Arthur M. Vogel ◽  
John N. Krieger
Keyword(s):  
Differential Diagnosis ◽  
Monoclonal Antibodies ◽  
Intermediate Filament ◽  
Intermediate Filament Proteins

scholarly journals Two Drosophila melanogaster proteins related to intermediate filament proteins of vertebrate cells.

1981 ◽  
Vol 91 (1) ◽  
pp. 175-183 ◽  
Author(s):  
F G Falkner ◽  
H Saumweber ◽  
H Biessmann
Keyword(s):  
Drosophila Melanogaster ◽  
Monoclonal Antibodies ◽  
Heat Shock ◽  
Indirect Immunofluorescence ◽  
Intermediate Filament ◽  
Cross Reaction ◽  
Cytoplasmic Protein ◽  
Baby Hamster Kidney ◽  
Intermediate Filament Proteins ◽  
Bhk Cells

Monoclonal antibodies were prepared against a 46,000 mol wt major cytoplasmic protein from Drosophila melanogaster Kc cells. These antibodies reacted with the 46,000 and a 40,000 mol wt protein from Kc cells. Some antibodies showed cross-reaction with 55,000 (vimentin) and 52,000 mol wt (desmin) proteins from baby hamster kidney (BHK) cells that form intermediate sized filaments in vertebrate cells. In indirect immunofluorescence, the group of cross reacting antibodies stained a filamentous meshwork in the cytoplasm of vertebrate cells. In Kc cells the fluorescence seemed to be localized in a filamentous meshwork that became more obvious after the cells had flattened out on a surface. These cytoskeletal structures are heat-labile; the proteins in Kc or BHK cells rearrange after a brief heat shock, forming juxtanuclear cap structures.

scholarly journals Clathrin assembly involves a light chain-binding region.

1987 ◽  
Vol 105 (5) ◽  
pp. 2011-2019 ◽  
Author(s):  
G S Blank ◽  
F M Brodsky
Keyword(s):  
Monoclonal Antibodies ◽  
Binding Site ◽  
Heavy Chain ◽  
Light Chain ◽  
Intermediate Filament ◽  
Binding Sites ◽  
Light Chains ◽  
Binding Region ◽  
Intermediate Filament Proteins ◽  
Interaction Site

Two regions on the clathrin heavy chain that are involved in triskelion interactions during assembly have been localized on the triskelion structure. These regions were previously identified with anti-heavy chain monoclonal antibodies X19 and X35, which disrupt clathrin assembly (Blank, G. S., and F. M. Brodsky, 1986, EMBO (Eur. Mol. Biol. Organ.) J., 5:2087-2095). Antibody-binding sites were determined based on their reactivity with truncated triskelions, and were mapped to an 8-kD region in the middle of the proximal portion of the triskelion arm (X19) and a 6-kD region at the triskelion elbow (X35). The elbow site implicated in triskelion assembly was also shown to be included within a heavy chain region involved in binding the light chains and to constitute part of the light chain-binding site. We postulate that this region of the heavy chain binds to the interaction site identified on the light chains that has homology to intermediate filament proteins (Brodsky, F. M., C. J. Galloway, G. S. Blank, A. P. Jackson, H.-F. Seow, K. Drickamer, and P. Parham, 1987, Nature (Lond.), 326:203-205). These findings suggest the existence of a heavy chain site, near the triskelion elbow, which is involved in both intramolecular and intermolecular interactions during clathrin assembly.

Reactivity of monoclonal antibodies against intermediate filament proteins during embryonic development

Development ◽  
1981 ◽  
Vol 64 (1) ◽  
pp. 45-60
Author(s):  
Rolf Kemler ◽  
Philippe Brûlet ◽  
Marie-Thérèse Schnebelen ◽  
Jean Gaillard ◽  
François Jacob
Keyword(s):  
Monoclonal Antibodies ◽  
Epithelial Cells ◽  
Embryonic Development ◽  
Tissue Distribution ◽  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Adult Tissue ◽  
Reactivity Pattern ◽  
Germ Layers ◽  
Intermediate Filament Proteins

Monoclonal antibodies (mAbs) against a preparation of intermediate filaments from trophoblastoma cells were studied for their reactivity pattern during embryonic development and on adult tissue cells. Up to day 12 of embryonic development, epithelial cells of the three germ layers reacted with these mAbs. Later during development and in adult tissues, positive reactions could be observed only with epithelial cells derived from mesoderm and endoderm. Because of their tissue distribution, the proteins reacting with these mAbs might belong to the keratin family of intermediate filaments or they might represent a new group of intermediate filaments.

scholarly journals Cross-reactivity of antibodies specific for flagellar tektin and intermediate filament subunits.

1987 ◽  
Vol 104 (6) ◽  
pp. 1563-1568 ◽  
Author(s):  
X J Chang ◽  
G Piperno
Keyword(s):  
Monoclonal Antibodies ◽  
Intermediate Filament ◽  
Immunofluorescence Microscopy ◽  
Polyclonal Antibodies ◽  
Nuclear Lamina ◽  
Helical Structure ◽  
Cross Reactivity ◽  
Cytoskeletal Proteins ◽  
Intermediate Filament Proteins ◽  
Double Label

Monoclonal antibodies specific for each of the flagellar tektins were prepared and used to determine whether structures similar to tektin filaments are present in cells lacking cilia or flagella. This analysis was performed by double-label immunofluorescence microscopy of several cell lines and by immunoblots of protein fractions. Two of the four anti-tektin antibodies, the antibodies 3-7-1 and 3-10-1, which bind different epitopes of the C-tektin, label 3T3, HeLa, PtK2, and BHK-21 cells as well as myotubes. The antibody 3-7-1 stains intermediate filament structures in the cells and binds vimentin or desmin in preparations of cytoskeletal proteins; whereas the antibody 3-10-1 stains nuclear envelopes in the cells and binds lamin A and C in preparations of cytoskeletal proteins or nuclear lamina. Structural similarities between the C-tektin and intermediate filament proteins probably are extended to more than two epitopes because polyclonal antibodies anti-vimentin and anti-desmin bind to C-tektin. These polyclonal antibodies also bind to A-tektin. The cross-reaction of monoclonal and polyclonal antibodies binding to epitopes in tektin and intermediate filament components and the existence of a high content of alpha-helical structure in the tektin subunits (Linck, R. W., and G. L. Langevin, 1982, J. Cell Sci., 58:1-22) indicate that tektin and intermediate filaments are homologous in several parts of their structure.

Antibodies to intermediate filament proteins in the immunohistochemical identification of human tumours: an overview

1983 ◽  
Vol 15 (7) ◽  
pp. 691-713 ◽  
Author(s):  
F. C. S. Ramaekers ◽  
J. J. G. Puts ◽  
O. Moesker ◽  
A. Kant ◽  
A. Huysmans ◽  
...  
Keyword(s):  
Intermediate Filament ◽  
Intermediate Filament Proteins ◽  
Human Tumours ◽  
Immunohistochemical Identification

Monoclonal antibodies to plant nuclear matrix reveal intermediate filamentrelated components within the nucleus

1991 ◽  
Vol 98 (3) ◽  
pp. 293-302
Author(s):  
ALISON BEVEN ◽  
YUHONG GUAN ◽  
JAN PEART ◽  
CHRISTINE COOPER ◽  
PETER SHAW
Keyword(s):  
Monoclonal Antibodies ◽  
Nuclear Matrix ◽  
Intermediate Filament ◽  
Nuclear Periphery ◽  
Nuclear Lamina ◽  
Protein S ◽  
Intermediate Filament Proteins ◽  
Daucus Carota L ◽  
Culture Cells ◽  
Matrix Fraction

We have prepared a nuclear matrix fraction from purified nuclei of carrot (Daucus carota L.) suspension culture cells, and used this fraction to produce a library of monoclonal antibodies. We report the preliminary characterisation of two antibodies-JIM 62 and JIM 63. The antibodies recognise a polypeptide doublet band at 92xl03Mr, which has been partially purified by differential urea extraction. Other intermediate filament antibodies-ME101, which recognises an epitope conserved among many intermediate filament proteins, and AFB, a monoclonal antibody to plant intermediate filament proteins, and an autoimmune serum directed against human lamina A and C (LSI), also label these bands, suggesting they are related to the intermediate filament/lamin family. IFA, another intermediate filament antibody, labels a band at approximately 60x103Mr, which is also enriched in the urea extracts of nuclear matrices. Immunofluorescence microscopy with JIM 63, ME 101, AFB and LSI shows network-like staining, often extending around the nucleolus. In many cases the staining reveals structures that appear to be bundles of fibres. JIM 63 also shows a weak staining of the nuclear rim in carrot nuclei, which can be greatly enhanced by treatment of the specimen with cold methanol after fixation. JIM 63 cross-reacts with all the other plant species we have tested. Vibratome sections of pea roots, extracted as for nuclear matrix preparation and stained with JIM 63 show a clear, strong nuclear rim labelling. Furthermore, JIM 63 strongly labels the nuclear lamina in rat liver nuclei. We suggest that the 92x103Mr protein(s) are related to intermediate filaments and/or lamins, and are distributed both within the nucleus and at the nuclear periphery.

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