All classes of intermediate filaments share a common antigenic determinant defined by a monoclonal antibody

Pruss, Rebecca M.; Mirsky, Rhona; Raff, Martin; Thorpe, Robin; Dowding, Alan J.; Anderton, Brian H.

doi:10.1016/0092-8674(81)90383-4

Cited by 632 publications

(284 citation statements)

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“…The IFA monoclonal antibody (33), which reacts with all known intermediate filament proteins, has been shown to react with nuclear lamins A, B, and C (34).…”

Section: Discussionmentioning

confidence: 99%

Molecular cloning of matrin F/G: A DNA binding protein of the nuclear matrix that contains putative zinc finger motifs.

Hakes

Berezney²

1991

Proc. Natl. Acad. Sci. U.S.A.

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We have isolated a 2.7-kilobase rat liver cDNA clone that contains the entire 544-amino acid coding sequence for matrin F/G. This protein has previously been localized to the internal, fibrogranular areas of the nuclear matrix and shown to bind to DNA on nitrocellulose blots. The predicted amino acid sequence from the coding region of this cDNA shows that this protein contains -50% hydrophobic amino acids with secondary structure predictions suggesting a large percentage of fl-sheet regions. No significant homologies were found with any other known proteins, including the nuclear lamins. The predicted amino acid sequence was also searched for DNA binding motifs. Two putative zinc finger motifs were found. In addition, a 7-mer palindromic sequence (Ser-Ser-Thr-Asn-Thr-Ser-Ser) was discovered within one of these zinc finger DNA binding regions. A possible regulatory role for this element is discussed.The nuclear matrix consists of a nuclear lamina, residual nucleoli, and an internal nuclear matrix (1). It is typically prepared by nuclease, salt, and detergent treatments of isolated nuclei (for review, see ref.2). Many molecular processes have been found associated with the nuclear matrix (2), including DNA replication (3), transcription (4), RNA splicing (5), and attachment of supercoiled DNA loops (6).The nuclear lamins are the most characterized of the nuclear matrix proteins. Analysis of cloned sequences of lamins A and C (7, 8) and lamin B (9) reveal structural similarity to the intermediate filament proteins. In contrast, our knowledge of the rest of the nuclear matrix proteins is very limited. Appropriate two-dimensional analysis has revealed over 200 proteins in the nuclear matrix including those that are common in a variety of cell lines and those that are both cell type and differentiation state dependent (10-12).Research in our laboratory is concentrating on the analysis ofa limited number of major Coomassie blue-stained proteins that are common to nuclear matrices isolated from a variety of mammalian cells. Polyclonal antibodies generated to many of these proteins all show staining of the fibrogranular matrix by immunofluorescence microscopy (13). We have, therefore, termed these proteins the nuclear matrins to distinguish them from the nuclear lamins, which compose the nuclear lamina structure along the periphery ofthe nuclear matrix (H. Nakayasu and R.B., unpublished data).Several of these major nuclear matrix proteins specifically bound DNA on Southwestern blots (40). As a step toward further characterization of the nuclear matrins and their putative role as DNA binding proteins, we have been screening Agtll cDNA expression libraries with our polyclonal antibodies to these matrin proteins. In this manuscript, we report the isolation and sequencing of a cDNA clone for matrin protein F/G4. The predicted amino acid sequence shows a strikingly high content of hydrophobic amino acids (R50o) and predicted /3-sheet secondary structure (-45%) and contains two putative Cys-Cys zinc finger DNA bindi...

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“…The IFA monoclonal antibody (33), which reacts with all known intermediate filament proteins, has been shown to react with nuclear lamins A, B, and C (34).…”

Section: Discussionmentioning

confidence: 99%

Molecular cloning of matrin F/G: A DNA binding protein of the nuclear matrix that contains putative zinc finger motifs.

Hakes

Berezney²

1991

Proc. Natl. Acad. Sci. U.S.A.

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“…desmin and vimentin [6,7]. However, structural analogies do exist as antigenic determinants common to most epithelial keratins and to all IF proteins have been described [8,91, and different IF proteins can form heteropolymers [lo, 1 I]. Furthermore, recent primary sequence information has demonstrated significant homology both amongst the different IF proteins, and between I F proteins and wool microfibrillar keratins [12 -141. Keratins are the most complex class of I F proteins and up to twenty have been identified in both mouse and human epithelial tissues although rarely more than eight are present in a…”

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confidence: 99%

Proteolytic modification of acidic and basic keratins during terminal differentiation of mouse and human epidermis

Bowden

Quinlan

Breitkreutz

et al. 1984

European Journal of Biochemistry

112

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Keratins from the living cell layers of human and neonatal mouse epidermis (prekeratins) have been compared to those from the stratum corneum (SC keratins). Human and mouse epidermis contained four prekeratins, two ofeach keratin subfamily; type I1 basic (PI 6.5 -8.5 ; human 68 kDa, 60.5 kDa and mouse 67 kDa, 60 kDa) and type I acidic (PI 4.7 -5.7; human 57 kDa, 51 kDa and mouse 58 kDa, 53 kDa). While all four were present in equal amounts in adult human epidermis, two (67 kDa basic, 58 kDa acidic) were more prominent in neonatal mouse epidermis. Preliminary results with cell fractions (basal, spinous and granular) indicated that quantitative differences were a function of morphology, basal cells containing the smaller member of each subfamily and granular cells the larger. Mouse stratum corneum extracts contained four keratins (three in human): type 11 neutral -acidic (PI 5.7 -6.7; human 65 kDa and mouse 64 kDa, 62 kDa) and type I acidic (PI 4.9 -5.4; human 57.5 kDa, 55 kDa and mouse 58.5 kDa, 57.5 kDa). In both species, one-dimensional and two-dimensional peptide mapping (with V8 protease and trypsin respectively) indicated that while all four prekeratins were distinct gene products, similarities existed in the type I1 basic and the type I acidic keratin subfamilies. A strong homology also existed between type I1 SC keratins and the larger basic (type 11) prekeratin (human 68 kDa and mouse 67 kDa) and between type I SC keratins and the larger acidic (type I) prekeratin (human 57 kDa and mouse 58 kDa). These results indicate a precursor-product relationship within each keratin subfamily, between SC keratins and the prekeratins abundant in the adjacent granular layer. This differentiation-related keratin processing was similar in mouse and human epidermis, and may represent a widespread phenomenon amongst keratinising epithelia.

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“…The cytoskeletal reactivity of monoclonal anti-DNA antibodies derived from hybridomas of SLE of human and murine origin has been reported (13 (20). The high degree of structural homology present in the central a helical coiled core, which exists in all types of intermediate filaments (21), may also be responsible for the anti-vimentin reactivity in these epithelial cells.…”

Section: Discussionmentioning

confidence: 99%

Cytoskeletal binding of monoclonal anti‐dna antibodies derived from tonsillar lymphoid cells of a normal subject

Cairns

Komar

Bell

1986

Arthritis & Rheumatism

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The ability of monoclonal IgM anti‐DNA auto‐antibodies derived from normal human lymphoid cells to bind to cellular constituents of human epithelial cells (HEp‐2) was examined by immunofluorescence. Hybridoma supernatants from 10 different clones were studied. Four of them gave a strong fibrillar cytoplasmic staining that resembled cytoskeletal staining, 1 showed strong nuclear staining only, 3 showed weak nucleolar staining only, and 2 showed no staining. The hybridoma supernatants that reacted with HEp‐2 cytoskeleton were either polyspecific for various nucleic acid antigens, such as single‐stranded DNA, DNA, poly(dA:dT), poly(dG)·poly(dC), RNA, and cardiolipin, or were restricted to cardiolipin. Cytoskeletal staining identical to the hybridoma supernatant staining was also seen with mouse monoclonal anti‐vimentin antibody B11.5.1. Inhibition of the cytoskeletal staining was accomplished in 3 of the 4 hybridoma supernatants by preabsorption of these hybridoma supernatants with cardiolipin and/or single‐stranded DNA, or by preincubation of the HEp‐2 cells with the mouse monoclonal anti‐vimentin antibody.

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All classes of intermediate filaments share a common antigenic determinant defined by a monoclonal antibody

Cited by 632 publications

References 31 publications

Molecular cloning of matrin F/G: A DNA binding protein of the nuclear matrix that contains putative zinc finger motifs.

Molecular cloning of matrin F/G: A DNA binding protein of the nuclear matrix that contains putative zinc finger motifs.

Proteolytic modification of acidic and basic keratins during terminal differentiation of mouse and human epidermis

Cytoskeletal binding of monoclonal anti‐dna antibodies derived from tonsillar lymphoid cells of a normal subject

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