scholarly journals Identifying the Role of Specific Motifs in the Lens Fiber Cell–Specific Intermediate Filament Phakosin

2007 ◽  
Vol 48 (11) ◽  
pp. 5132 ◽  
Author(s):  
Joshua T. Pittenger ◽  
John F. Hess ◽  
Paul G. FitzGerald
Keyword(s):  
Intermediate Filament ◽  
Fiber Cell ◽  
Lens Fiber ◽  
Lens Fiber Cell

Chicken filensin: a lens fiber cell protein that exhibits sequence similarity to intermediate filament proteins

1993 ◽  
Vol 105 (4) ◽  
pp. 1057-1068 ◽  
Author(s):  
S.G. Remington
Keyword(s):  
Amino Acid ◽  
Intermediate Filament ◽  
Fiber Cell ◽  
Heptad Repeat ◽  
Lens Fiber ◽  
Lens Fiber Cell ◽  
Intermediate Filament Proteins ◽  
Fiber Cells ◽  
Amino Terminal ◽  
Sequence Identity

Filensin, a 100 kDa, membrane-associated, cytoskeletal protein, is uniquely expressed in the lens fiber cell (Merdes, A., Brunkener, M., Horstmann, H., and Georgatos, S. D. (1991) J. Cell Biol. 115, 397–410). I cloned and sequenced a full-length chicken lens cDNA encoding filensin, also known as CP95 (Ireland, M. and Maisel, H. (1989) Lens and Eye Toxicity Research 6, 623–638). The deduced amino acid sequence of 657 residues contained an internal 280 residue heptad repeat domain with sequence similarities to the rod domain of intermediate filament proteins. The putative filensin rod domain could be divided into three alpha-helical segments (1A, 1B and 2) separated by short, non-helical linkers. The sequence of the amino-terminal end of the filensin rod domain contained the highly conserved intermediate filament segment 1A motif (Conway, J. F. and Parry, D. A. D. (1988) Int. J. Biol. Macromol. 10, 79–98). Allowing conservative amino acid substitutions, the sequence of the carboxy-terminal end of the filensin rod domain was similar to that of the highly conserved intermediate filament rod carboxy terminus. The alpha-helical segments of the shorter filensin rod domain aligned with the corresponding segments of intermediate filament proteins by allowing a gap of four heptad repeats in the amino-terminal half of filensin segment 2. Filensin rod segment 2 contained the characteristic stutter in heptad repeat phasing, nine heptads from the end of the intermediate filament rod. The overall sequence identity between the rod domains of filensin and individual intermediate filament proteins was 20 to 25%, approximately the level of sequence identity observed between intermediate filament proteins of different types. The open reading frame of chicken filensin predicted a 657 amino acid protein with molecular mass of 76 kDa. Embryonic chicken filensin migrated in SDS-PAGE as a triplet of 102, 105 and 109 kDa, while rooster filensin migrated as a 105 and 109 kDa doublet. Antibodies to filensin labeled lens fiber cells but not lens epithelial cells. By immunofluorescence methods filensin was localized to the fiber cell plasma membranes, including the ends of elongated fiber cells.

The Role of MIP in Lens Fiber Cell Membrane Transport

1999 ◽  
Vol 170 (3) ◽  
pp. 191-203 ◽  
Author(s):  
K. Varadaraj ◽  
C. Kushmerick ◽  
G.J. Baldo ◽  
S. Bassnett ◽  
A. Shiels ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Membrane Transport ◽  
Fiber Cell ◽  
Lens Fiber ◽  
Lens Fiber Cell ◽  
Cell Membrane Transport

Targeted Deletion of the Lens Fiber Cell–Specific Intermediate Filament Protein Filensin

2003 ◽  
Vol 44 (12) ◽  
pp. 5252 ◽  
Author(s):  
Azita Alizadeh ◽  
John Clark ◽  
Teri Seeberger ◽  
John Hess ◽  
Tom Blankenship ◽  
...  
Keyword(s):  
Intermediate Filament ◽  
Fiber Cell ◽  
Intermediate Filament Protein ◽  
Lens Fiber ◽  
Lens Fiber Cell ◽  
Targeted Deletion ◽  
Filament Protein

scholarly journals Fibroblast growth factor receptor signaling is essential for lens fiber cell differentiation

2008 ◽  
Vol 318 (2) ◽  
pp. 276-288 ◽  
Author(s):  
Haotian Zhao ◽  
Tianyu Yang ◽  
Bhavani P. Madakashira ◽  
Cornelius A. Thiels ◽  
Chad A. Bechtle ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Fibroblast Growth Factor Receptor ◽  
Growth Factor Receptor ◽  
Fiber Cell ◽  
Fibroblast Growth ◽  
Lens Fiber ◽  
Lens Fiber Cell ◽  
Growth Factor Receptor Signaling

scholarly journals Proteomics and Phosphoproteomics Analysis of Human Lens Fiber Cell Membranes

2013 ◽  
Vol 54 (2) ◽  
pp. 1135 ◽  
Author(s):  
Zhen Wang ◽  
Jun Han ◽  
Larry L. David ◽  
Kevin L. Schey
Keyword(s):  
Cell Membranes ◽  
Fiber Cell ◽  
Human Lens ◽  
Lens Fiber ◽  
Lens Fiber Cell

The distribution of the fiber cell intrinsic membrane proteins MP20 and connexin46 in the bovine lens

1992 ◽  
Vol 103 (1) ◽  
pp. 245-257 ◽  
Author(s):  
E. Tenbroek ◽  
M. Arneson ◽  
L. Jarvis ◽  
C. Louis
Keyword(s):  
Monoclonal Antibody ◽  
Fiber Cell ◽  
Immunogold Electron Microscopy ◽  
Lens Fiber ◽  
Lens Fiber Cell ◽  
Western Blots ◽  
Fiber Cells ◽  
Bovine Lens ◽  
Narrow Side ◽  
Lens Membranes

MP20 is an intrinsic membrane protein previously identified in mammalian lens fiber cells. To identify a possible role for this protein in the lens, the distribution of MP20 and connexin46 has now been examined. Western immunoblotting with an anti-peptide antibody generated to the C-terminal 8 amino acids of MP20 confirmed the presence of this protein in the lens of several different mammalian species. A monoclonal antibody 5H1 was prepared that, in Western blots of bovine lesn membranes, recognized the same component as an antibody to rat connexin46 (Cx46). The apparent molecular mass of this component decreased from 59 kDa to 55 kDa following treatment of lens membranes with alkaline phosphatase. A monoclonal antibody to connexin-related MP70 recognized a 70 kDa component in bovine lens membranes confirming the presence of these two different connexin proteins in bovine lens membranes. To localize MP20 and Cx46 in the bovine lens membrane, lens fiber cell bundles were immunofluorescently labeled with both the MP20 antibody, and the monoclonal antibody to Cx46. Cx46 was identified in large plaques on the broad faces of the lens fiber cells throughout the outer 1 mm of the lens cortex. MP20 colocalized with Cx46 only in a restricted area 0.5 mm to 1.0 mm into the lens. In other regions of the lens, MP20 appeared more diffusely distributed over the fiber cell surface, although apparently concentrated in the ball-and-socket regions at the corners of the narrow side of the inner cortical lens fiber cells. These inner cortical regions were devoid of Cx46. A difference in distribution of these two proteins was confirmed in studies of immunofluorescently labeled lens cryosections. Furthermore, immunogold electron microscopy of purified lens membranes identified MP20 in both junctional regions (with Cx46) and in single membranes. These results provide evidence for a role for MP20 in mammalian lens fiber cell junctional formation or organization.

scholarly journals Ultrastructural analysis of the human lens fiber cell remodeling zone and the initiation of cellular compaction

2013 ◽  
Vol 116 ◽  
pp. 411-418 ◽  
Author(s):  
M. Joseph Costello ◽  
Ashik Mohamed ◽  
Kurt O. Gilliland ◽  
W. Craig Fowler ◽  
Sönke Johnsen
Keyword(s):  
Ultrastructural Analysis ◽  
Fiber Cell ◽  
Human Lens ◽  
Lens Fiber ◽  
Lens Fiber Cell ◽  
Cell Remodeling
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