2001
4.
Gonen, Tamir; Grey, Angus C; Jacobs, Marc D; Donaldson, Paul J; Kistler, Joerg
In: BMC Cell Biol., vol. 2, no. 17, 2001.
@article{pmid11532191,
title = {MP20, the second most abundant lens membrane protein and member of the tetraspanin superfamily, joins the list of ligands of galectin-3},
author = {Tamir Gonen and Angus C Grey and Marc D Jacobs and Paul J Donaldson and Joerg Kistler},
url = {https://cryoem.ucla.edu/wp-content/uploads/gonen_2001.pdf, Main text},
doi = {10.1186/1471-2121-2-17},
year = {2001},
date = {2001-08-14},
urldate = {2001-08-14},
journal = {BMC Cell Biol.},
volume = {2},
number = {17},
abstract = {Although MP20 is the second most highly expressed membrane protein in the lens its function remains an enigma. Putative functions for MP20 have recently been inferred from its assignment to the tetraspanin superfamily of integral membrane proteins. Members of this family have been shown to be involved in cellular proliferation, differentiation, migration, and adhesion. In this study, we show that MP20 associates with galectin-3, a known adhesion modulator. MP20 and galectin-3 co-localized in selected areas of the lens fiber cell plasma membrane. Individually, these proteins purified with apparent molecular masses of 60 kDa and 22 kDa, respectively. A 104 kDa complex was formed in vitro upon mixing the purified proteins. A 102 kDa complex of MP20 and galectin-3 could also be isolated from detergent-solubilized native fiber cell membranes. Binding between MP20 and galectin-3 was disrupted by lactose suggesting the lectin site was involved in the interaction. MP20 adds to a growing list of ligands of galectin-3 and appears to be the first representative of the tetraspanin superfamily identified to possess this specificity.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Although MP20 is the second most highly expressed membrane protein in the lens its function remains an enigma. Putative functions for MP20 have recently been inferred from its assignment to the tetraspanin superfamily of integral membrane proteins. Members of this family have been shown to be involved in cellular proliferation, differentiation, migration, and adhesion. In this study, we show that MP20 associates with galectin-3, a known adhesion modulator. MP20 and galectin-3 co-localized in selected areas of the lens fiber cell plasma membrane. Individually, these proteins purified with apparent molecular masses of 60 kDa and 22 kDa, respectively. A 104 kDa complex was formed in vitro upon mixing the purified proteins. A 102 kDa complex of MP20 and galectin-3 could also be isolated from detergent-solubilized native fiber cell membranes. Binding between MP20 and galectin-3 was disrupted by lactose suggesting the lectin site was involved in the interaction. MP20 adds to a growing list of ligands of galectin-3 and appears to be the first representative of the tetraspanin superfamily identified to possess this specificity.
2000
3.
Gonen, Tamir; Donaldson, Paul; Kistler, Joerg
Galectin-3 Is Associated with the Plasma Membrane of Lens Fiber Cells
In: Investigative Ophthalmology and Visual Science, vol. 41, no. 1, pp. 199–203, 2000.
@article{gonen_2000,
title = {Galectin-3 Is Associated with the Plasma Membrane of Lens Fiber Cells},
author = {Tamir Gonen and Paul Donaldson and Joerg Kistler},
url = {https://cryoem.ucla.edu/wp-content/uploads/gonen_2000.pdf, Main text},
year = {2000},
date = {2000-01-01},
journal = {Investigative Ophthalmology and Visual Science},
volume = {41},
number = {1},
pages = {199--203},
abstract = {PURPOSE: To discover proteins that have the potential to contribute to the tight packing of fiber cells in the lens.
METHODS: Crude fiber cell membranes were isolated from ovine lens cortex. Proteins were separated by two-dimensional gel electrophoresis, and selected protein spots identified by micro-sequencing. The identification of galectin-3 was confirmed by immunoblotting with a specific antibody. The association of galectin-3 with the fiber cell plasma membrane was investigated using immunofluorescence microscopy, solubilization trials with selected reagents, and immunoprecipitation to identify candidate ligands.
RESULTS: A cluster of three protein spots with an apparent molecular weight of 31,000 and isoelectric points ranging between 7 and 8.5 were resolved and identified as galectin-3. This protein was associated peripherally with the fiber cell plasma membrane and interacted with MP20, an abundant intrinsic membrane protein that had been identified previously as a component of membrane junctions between fiber cells.
CONCLUSIONS: The detection of galectin-3 in the lens is a novel result and adds to the growing list of lens proteins with adhesive properties. Its location at the fiber cell membrane and its association with the junction-forming MP20 is consistent with a potential role in the development or maintenance of the tightly packed lens tissue architecture. (Invest Ophthalmol Vis Sci. 2000;41:199 –203)},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
PURPOSE: To discover proteins that have the potential to contribute to the tight packing of fiber cells in the lens.
METHODS: Crude fiber cell membranes were isolated from ovine lens cortex. Proteins were separated by two-dimensional gel electrophoresis, and selected protein spots identified by micro-sequencing. The identification of galectin-3 was confirmed by immunoblotting with a specific antibody. The association of galectin-3 with the fiber cell plasma membrane was investigated using immunofluorescence microscopy, solubilization trials with selected reagents, and immunoprecipitation to identify candidate ligands.
RESULTS: A cluster of three protein spots with an apparent molecular weight of 31,000 and isoelectric points ranging between 7 and 8.5 were resolved and identified as galectin-3. This protein was associated peripherally with the fiber cell plasma membrane and interacted with MP20, an abundant intrinsic membrane protein that had been identified previously as a component of membrane junctions between fiber cells.
CONCLUSIONS: The detection of galectin-3 in the lens is a novel result and adds to the growing list of lens proteins with adhesive properties. Its location at the fiber cell membrane and its association with the junction-forming MP20 is consistent with a potential role in the development or maintenance of the tightly packed lens tissue architecture. (Invest Ophthalmol Vis Sci. 2000;41:199 –203)
METHODS: Crude fiber cell membranes were isolated from ovine lens cortex. Proteins were separated by two-dimensional gel electrophoresis, and selected protein spots identified by micro-sequencing. The identification of galectin-3 was confirmed by immunoblotting with a specific antibody. The association of galectin-3 with the fiber cell plasma membrane was investigated using immunofluorescence microscopy, solubilization trials with selected reagents, and immunoprecipitation to identify candidate ligands.
RESULTS: A cluster of three protein spots with an apparent molecular weight of 31,000 and isoelectric points ranging between 7 and 8.5 were resolved and identified as galectin-3. This protein was associated peripherally with the fiber cell plasma membrane and interacted with MP20, an abundant intrinsic membrane protein that had been identified previously as a component of membrane junctions between fiber cells.
CONCLUSIONS: The detection of galectin-3 in the lens is a novel result and adds to the growing list of lens proteins with adhesive properties. Its location at the fiber cell membrane and its association with the junction-forming MP20 is consistent with a potential role in the development or maintenance of the tightly packed lens tissue architecture. (Invest Ophthalmol Vis Sci. 2000;41:199 –203)
1999
2.
Kistler, Joerg; Merriman-Smith, Rachelle; Young, Miriam; Gonen, Tamir; Cowan, Dougal; Chee, Kaa-Sandra; Lin, Jun Sheng; Green, Colin; Hasler, Lorenz; Engel, Andreas; Donaldson, Paul
Molecular Solutions To Tissue Transparency
In: N.Z. Biosciences, pp. 35–37, 1999.
@article{kistler_1999,
title = {Molecular Solutions To Tissue Transparency},
author = {Joerg Kistler and Rachelle Merriman-Smith and Miriam Young and Tamir Gonen and Dougal Cowan and Kaa-Sandra Chee and Jun Sheng Lin and Colin Green and Lorenz Hasler and Andreas Engel and Paul Donaldson},
url = {https://cryoem.ucla.edu/wp-content/uploads/kistler_1999.pdf, Main text},
year = {1999},
date = {1999-08-01},
journal = {N.Z. Biosciences},
pages = {35--37},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
1.
Baker, Ted; Metcalf, Peter; Smith, Clyde; Arcus, Vic; Ashton, Rachael; Baker, Heather; Banfield, Mark; Cross, Jenny; Drew, David; Goldstone, David; Gonen, Tamir; Haebel, Peter; Holliss, Caroline; Ivanovich, Ivan; Kagawa, Todd; Kidd, Richard; Koon, Nayden; Leydier, Sabine; Lott, Shaun; McCarthy, Andrew; Nurizzo, Didier; Shewry, Steve; Sigrell, Jill; Sun, Xiaolin
More Than Just A Pretty Picture
In: N.Z. Biosciences, pp. 32–35, 1999.
@article{baker_1999,
title = {More Than Just A Pretty Picture},
author = {Ted Baker and Peter Metcalf and Clyde Smith and Vic Arcus and Rachael Ashton and Heather Baker and Mark Banfield and Jenny Cross and David Drew and David Goldstone and Tamir Gonen and Peter Haebel and Caroline Holliss and Ivan Ivanovich and Todd Kagawa and Richard Kidd and Nayden Koon and Sabine Leydier and Shaun Lott and Andrew McCarthy and Didier Nurizzo and Steve Shewry and Jill Sigrell and Xiaolin Sun},
url = {https://cryoem.ucla.edu/wp-content/uploads/baker_1999.pdf, Main text},
year = {1999},
date = {1999-08-01},
journal = {N.Z. Biosciences},
pages = {32--35},
keywords = {},
pubstate = {published},
tppubtype = {article}
}