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Paul G Fitzgerald - One of the best experts on this subject based on the ideXlab platform.

  • Primary sequence, secondary structure, gene structure, and assembly properties suggests that the lens-specific cytoskeletal protein filensin represents a novel class of Intermediate Filament protein.
    Experimental eye research, 1998
    Co-Authors: John F Hess, Jodi T. Casselman, Allen Kong, Paul G Fitzgerald
    Abstract:

    The ocular lens fiber cell assembles a novel cytoskeletal element, the Beaded Filament, from CP49 and filensin, two Proteins expressed only in the differentiated lens fiber cell. We report the primary sequence, secondary structural analysis, gene structure and Yeast Two Hybrid interaction data for human filensin, and develop a consensus model of filensin from the human and previously reported bovine and chicken filensin sequences. This consensus model, combined with gene structure and Yeast Two Hybrid studies establish that filensin is a member of the Intermediate Filament family of Proteins. Specifically, filensin exhibits (1) divergence at amino acid sequence motifs otherwise highly conserved among Intermediate Filament Proteins, (2) a loss of 29 amino acids from the central rod domain which is unique among cytoplasmic Intermediate Filament Proteins, (3) an absence of sequence identity with any existing class of Intermediate Filament protein, (4) a gene structure unique among Intermediate Filament family, (5) an inability to dimerize with representatives of Type I, II, and III Intermediate Filament Proteins. Thus, at each level of analysis, we find that filensin is similar to the consensus model of Intermediate Filament Proteins, supporting our conclusion that filensin's relatedness to the IF family is not the consequence of convergent evolution. However, filensin also shows unique or extreme distinctions from the consensus Intermediate Filament protein at each level of analysis, indicating that filensin constitutes a novel class of IF protein. Some of filensin's unique features are incompatible with current models of IF assembly. Analysis of filensin gene structure suggests that the 29 amino acid reduction in the central rod domain was not the result of a single splice site mutation, the mechanism suggested for the transition between nuclear lamins and cytoplasmic Intermediate Filament Proteins.

  • bovine filensin possesses primary and secondary structure similarity to Intermediate Filament Proteins
    Journal of Cell Biology, 1993
    Co-Authors: Fotini Gounari, Roy A. Quinlan, Andreas Merdes, John F Hess, Paul G Fitzgerald, Christos A Ouzounis, Spyros D Georgatos
    Abstract:

    The cDNA coding for calf filensin, a membrane-associated protein of the lens fiber cells, has been cloned and sequenced. The predicted 755-amino acid-long open reading frame shows primary and secondary structure similarity to Intermediate Filament (IF) Proteins. Filensin can be divided into an NH2-terminal domain (head) of 38 amino acids, a middle domain (rod) of 279 amino acids, and a COOH-terminal domain (tail) of 438 amino acids. The head domain contains a di-arginine/aromatic amino acid motif which is also found in the head domains of various Intermediate Filament Proteins and includes a potential protein kinase A phosphorylation site. By multiple alignment to all known IF protein sequences, the filensin rod, which is the shortest among IF Proteins, can be subdivided into three subdomains (coils 1a, 1b, and 2). A 29 amino acid truncation in the coil 2 region accounts for the smaller size of this domain. The filensin tail contains 6 1/2 tandem repeats which match analogous motifs of mammalian neuroFilament M and H Proteins. We suggest that filensin is a novel IF protein which does not conform to any of the previously described classes. Purified filensin fails to form regular Filaments in vitro (Merdes, A., M. Brunkener, H. Horstmann, and S. D. Georgatos. 1991. J. Cell Biol. 115:397-410), probably due to the missing segment in the coil 2 region. Participation of filensin in a Filamentous network in vivo may be facilitated by an assembly partner.

Lars-eric Thornell - One of the best experts on this subject based on the ideXlab platform.

  • Smoothelin and Intermediate Filament Proteins in Humanaortocoronary Saphenous Vein By-pass Grafts
    The Histochemical Journal, 1999
    Co-Authors: Bengt Johansson, Anders Eriksson, Frans Ramaekers, Lars-eric Thornell
    Abstract:

    The aim of this immunohistochemical investigation was to study the distribution of the novel cytoskeletal protein smoothelin and the Intermediate Filament Proteins vimentin and desmin in normal human great saphenous vein and in human aortocoronary by-pass vein grafts. Smoothelin was present in most smooth muscle cells in the media of the native vein. In the neointima of the vein grafts that had been in situ for three months or more, smoothelin was, in general, present only in few smooth muscle cells. Desmin was distributed in the same pattern as smoothelin in the native great saphenous vein. When desmin and smoothelin were present in the neointima, smoothelin was detected in more cells than desmin. Vimentin was present in most cells in all wall layers of both the native saphenous vein and the vein grafts. Vascular smooth muscle cells containing vimentin but not desmin or smoothelin are the principal cells in the neointima of human aortocoronary vein grafts. In some grafts, however, all three cytoskeletal Proteins were detected in the neointima. The distribution of smoothelin and desmin in aortocoronary vein grafts support the postulate that these Proteins are expressed mainly in the contractile smooth muscle cell phenotype.

  • Intermediate Filament Proteins in developing human arteries.
    Anatomy and embryology, 1999
    Co-Authors: Bengt Johansson, Anders Eriksson, Lars-eric Thornell
    Abstract:

    The distribution of Intermediate Filament Proteins in adult human blood vessels and in human fetal elastic arteries is relatively well-known. However, the distribution of these Proteins in the course from neonate to adult has not been established. In this investigation, human postnatal arteries were studied with immunohistochemistry, using antibodies targeted on the Intermediate Filament Proteins desmin, vimentin and cytokeratins 8, 18 and 19. Vimentin was present in most smooth muscle cells in all vessels and at all ages. The proportions of desmin-expressing cells increased in the elastic arteries during the first year of life and was higher in the pulmonary trunk than in the aorta. In the muscular arteries, the proportion of desmin-labelled cells increased in the coronary and the deep femoral arteries, but remained constant in the renal and the cerebral arteries. Cytokeratins were detected in the pulmonary trunk earlier than in the aorta. Cytokeratins were present throughout the wall of the ductus arteriosus, but desmin was present only in some cells. Thus, there are postnatal changes in the distribution of Intermediate Filament Proteins in the elastic arteries and in some muscular arteries, whereas the Intermediate Filament pattern remains unchanged in other muscular arteries.

  • Smoothelin and Intermediate Filament Proteins in human aortocoronary saphenous vein by-pass grafts.
    The Histochemical journal, 1999
    Co-Authors: Bengt Johansson, Anders Eriksson, Frans C. S. Ramaekers, Lars-eric Thornell
    Abstract:

    The aim of this immunohistochemical investigation was to study the distribution of the novel cytoskeletal protein smoothelin and the Intermediate Filament Proteins vimentin and desmin in normal human great saphenous vein and in human aortocoronary by-pass vein grafts. Smoothelin was present in most smooth muscle cells in the media of the native vein. In the neointima of the vein grafts that had been in situ for three months or more, smoothelin was, in general, present only in few smooth muscle cells. Desmin was distributed in the same pattern as smoothelin in the native great saphenous vein. When desmin and smoothelin were present in the neointima, smoothelin was detected in more cells than desmin. Vimentin was present in most cells in all wall layers of both the native saphenous vein and the vein grafts. Vascular smooth muscle cells containing vimentin but not desmin or smoothelin are the principal cells in the neointima of human aortocoronary vein grafts. In some grafts, however, all three cytoskeletal Proteins were detected in the neointima. The distribution of smoothelin and desmin in aortocoronary vein grafts support the postulate that these Proteins are expressed mainly in the contractile smooth muscle cell phenotype.

John F Hess - One of the best experts on this subject based on the ideXlab platform.

  • Primary sequence, secondary structure, gene structure, and assembly properties suggests that the lens-specific cytoskeletal protein filensin represents a novel class of Intermediate Filament protein.
    Experimental eye research, 1998
    Co-Authors: John F Hess, Jodi T. Casselman, Allen Kong, Paul G Fitzgerald
    Abstract:

    The ocular lens fiber cell assembles a novel cytoskeletal element, the Beaded Filament, from CP49 and filensin, two Proteins expressed only in the differentiated lens fiber cell. We report the primary sequence, secondary structural analysis, gene structure and Yeast Two Hybrid interaction data for human filensin, and develop a consensus model of filensin from the human and previously reported bovine and chicken filensin sequences. This consensus model, combined with gene structure and Yeast Two Hybrid studies establish that filensin is a member of the Intermediate Filament family of Proteins. Specifically, filensin exhibits (1) divergence at amino acid sequence motifs otherwise highly conserved among Intermediate Filament Proteins, (2) a loss of 29 amino acids from the central rod domain which is unique among cytoplasmic Intermediate Filament Proteins, (3) an absence of sequence identity with any existing class of Intermediate Filament protein, (4) a gene structure unique among Intermediate Filament family, (5) an inability to dimerize with representatives of Type I, II, and III Intermediate Filament Proteins. Thus, at each level of analysis, we find that filensin is similar to the consensus model of Intermediate Filament Proteins, supporting our conclusion that filensin's relatedness to the IF family is not the consequence of convergent evolution. However, filensin also shows unique or extreme distinctions from the consensus Intermediate Filament protein at each level of analysis, indicating that filensin constitutes a novel class of IF protein. Some of filensin's unique features are incompatible with current models of IF assembly. Analysis of filensin gene structure suggests that the 29 amino acid reduction in the central rod domain was not the result of a single splice site mutation, the mechanism suggested for the transition between nuclear lamins and cytoplasmic Intermediate Filament Proteins.

  • bovine filensin possesses primary and secondary structure similarity to Intermediate Filament Proteins
    Journal of Cell Biology, 1993
    Co-Authors: Fotini Gounari, Roy A. Quinlan, Andreas Merdes, John F Hess, Paul G Fitzgerald, Christos A Ouzounis, Spyros D Georgatos
    Abstract:

    The cDNA coding for calf filensin, a membrane-associated protein of the lens fiber cells, has been cloned and sequenced. The predicted 755-amino acid-long open reading frame shows primary and secondary structure similarity to Intermediate Filament (IF) Proteins. Filensin can be divided into an NH2-terminal domain (head) of 38 amino acids, a middle domain (rod) of 279 amino acids, and a COOH-terminal domain (tail) of 438 amino acids. The head domain contains a di-arginine/aromatic amino acid motif which is also found in the head domains of various Intermediate Filament Proteins and includes a potential protein kinase A phosphorylation site. By multiple alignment to all known IF protein sequences, the filensin rod, which is the shortest among IF Proteins, can be subdivided into three subdomains (coils 1a, 1b, and 2). A 29 amino acid truncation in the coil 2 region accounts for the smaller size of this domain. The filensin tail contains 6 1/2 tandem repeats which match analogous motifs of mammalian neuroFilament M and H Proteins. We suggest that filensin is a novel IF protein which does not conform to any of the previously described classes. Purified filensin fails to form regular Filaments in vitro (Merdes, A., M. Brunkener, H. Horstmann, and S. D. Georgatos. 1991. J. Cell Biol. 115:397-410), probably due to the missing segment in the coil 2 region. Participation of filensin in a Filamentous network in vivo may be facilitated by an assembly partner.

Spyros D Georgatos - One of the best experts on this subject based on the ideXlab platform.

  • bovine filensin possesses primary and secondary structure similarity to Intermediate Filament Proteins
    Journal of Cell Biology, 1993
    Co-Authors: Fotini Gounari, Roy A. Quinlan, Andreas Merdes, John F Hess, Paul G Fitzgerald, Christos A Ouzounis, Spyros D Georgatos
    Abstract:

    The cDNA coding for calf filensin, a membrane-associated protein of the lens fiber cells, has been cloned and sequenced. The predicted 755-amino acid-long open reading frame shows primary and secondary structure similarity to Intermediate Filament (IF) Proteins. Filensin can be divided into an NH2-terminal domain (head) of 38 amino acids, a middle domain (rod) of 279 amino acids, and a COOH-terminal domain (tail) of 438 amino acids. The head domain contains a di-arginine/aromatic amino acid motif which is also found in the head domains of various Intermediate Filament Proteins and includes a potential protein kinase A phosphorylation site. By multiple alignment to all known IF protein sequences, the filensin rod, which is the shortest among IF Proteins, can be subdivided into three subdomains (coils 1a, 1b, and 2). A 29 amino acid truncation in the coil 2 region accounts for the smaller size of this domain. The filensin tail contains 6 1/2 tandem repeats which match analogous motifs of mammalian neuroFilament M and H Proteins. We suggest that filensin is a novel IF protein which does not conform to any of the previously described classes. Purified filensin fails to form regular Filaments in vitro (Merdes, A., M. Brunkener, H. Horstmann, and S. D. Georgatos. 1991. J. Cell Biol. 115:397-410), probably due to the missing segment in the coil 2 region. Participation of filensin in a Filamentous network in vivo may be facilitated by an assembly partner.

Robert D Goldman - One of the best experts on this subject based on the ideXlab platform.

  • Intermediate Filament Proteins participate in signal transduction
    Trends in Cell Biology, 2005
    Co-Authors: Brian T Helfand, Ying Hao Chou, Dale K Shumaker, Robert D Goldman
    Abstract:

    How timely transport of chemical signals between the distal end of long axonal processes and the cell bodies of neurons occurs is an interesting and unresolved issue. Recently, Perlson et al. presented evidence that cleavage products of newly synthesized vimentin, an Intermediate Filament (IF) protein, interact with mitogen-activated protein (MAP) kinases at sites of axon injury. These IF fragments appear to be required for the transport of these kinases to the cell body along microtubule tracks. The truncated vimentin is instrumental in signal propagation as it provides a scaffold that brings together activated MAP kinases (such as Erk 1 and Erk2), as well as importin β and cytoplasmic dynein. The authors propose that this all-in-one transport complex has the extraordinary ability to travel towards the cell body and enter the nucleus where the kinases activate and influence gene expression so that a neuron can generate a timely response to injury.