Paralemnin of the lens

Bagchi, M.; Katar, M.; Lo, Woo-Kuen; Maisel, H.

doi:10.1002/jcb.10574

Cited by 9 publications

(10 citation statements)

References 11 publications

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“…Two proteins that showed such a clear pattern, were brain abundant signal protein 1 (BASP1) and paralemmin 1 (Fig. 4B); both of which have been reported to be present in the lens (Bagchi et al 2003;Castellini et al 2005;Bagchi et al 2008). BASP1 belongs to a family of growth-associated proteins that modulate nerve sprouting, and are enriched in both the brain and nerve endings (Mosevitskya et al 1997;Mosevitsky 2005).…”

Section: Discussionmentioning

confidence: 95%

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Tight binding of proteins to membranes from older human cells

Truscott

Comte‐Walters

Schwacke

et al. 2010

AGE

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The lens is an ideal model system for the study of macromolecular aging and its consequences for cellular function, since there is no turnover of lens fibre cells. To examine biochemical processes that take place in the lens and that may also occur in other long-lived cells, membranes were isolated from defined regions of human lenses that are synthesised at different times during life, and assayed for the presence of tightly bound cytosolic proteins using quantitative iTRAQ proteomics technology. A majority of lens beta crystallins and all gamma crystallins became increasingly membrane bound with age, however, the chaperone proteins alpha A and alpha B crystallin, as well as the thermally-stable protein, βB2 crystallin, did not. Other proteins such as brain-associated signal protein 1 and paralemmin 1 became less tightly bound in the older regions of the lens. It is evident that protein-membrane interactions change significantly with age. Selected proteins that were formerly cytosolic become increasingly tightly bound to cell membranes with age and are not removed even by treatment with 7 M urea. It is likely that such processes reflect polypeptide denaturation over time and the untoward binding of proteins to membranes may alter membrane properties and contribute to impairment of communication between older cells.

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Section: Discussionmentioning

confidence: 95%

“…Alterations in membrane lipids could also contribute to the observed loss of BASP1 with fibre age. Paralemmin 1 is a prenyl-palmitoylanchored membrane protein involved in neuronal membrane and process formation and is hypothesised to play a role in lens membrane and interdigitation formation (Bagchi et al 2003;Castellini et al 2005).…”

Section: Discussionmentioning

confidence: 99%

Tight binding of proteins to membranes from older human cells

Truscott

Comte‐Walters

Schwacke

et al. 2010

AGE

View full text Add to dashboard Cite

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“…Further, this gene is downregulated in lenses overexpressing the Pax6(5a) splice variant [25] and the protein is detected in lens cells from both mice and chickens [25,26]. Overexpression of Palm in both neuronal and non-neuronal cell lines initiates the expansion of the plasma membrane and the development of extended processes and microspikes which is dependent on Palm targeting to the cytoplasmic face of the plasma membrane via a palmitoyl group covalently linked near the protein's C-terminus [24,27].…”

Section: Introductionmentioning

confidence: 99%

Palm is expressed in both developing and adult mouse lens and retina

et al. 2005

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“…Paralemmin-1 is abundant in renal distal tubule cells with their elaborate infoldings of the basolateral plasma membrane, and in extremely Xattened cell types like the epithelia of the thin limbs of Henle's loops, and subpopulations of the parietal epithelial cells of Bowman's capsule and vascular endothelial cells. Paralemmin-1 expression has been shown to be up-regulated during the maturation of eye lens Wber cells (Chauhan et al 2002;Bagchi et al 2003), which are extremely elongated (100 times as long as in diameter) and have an elaborate cortical cytoskeleton. All these observations are in line with a role for paralemmin-1 in the formation and/or stabilization of extreme plasma membrane shapes.…”

Section: Discussionmentioning

confidence: 99%

“…Paralemmin-1 is also found in the eye lens, where its expression is up-regulated as the Wber cells of the lens undergo terminal diVerentiation and assume their extremely elongated shape. Paralemmin-1 expression in the lens is inXuenced by the transcription factor, Pax6, known to be important for the morphogenesis of the eye and the nervous system (Chauhan et al 2002;Bagchi et al 2003;Castellini et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Cellular and subcellular localization of paralemmin-1, a protein involved in cell shape control, in the rat brain, adrenal gland and kidney

Kutzleb

Petrasch‐Parwez

Kilimann

2006

Histochem Cell Biol

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Paralemmin-1 is a phosphoprotein, lipid-anchored to the cytoplasmic face of membranes and implicated in plasma membrane dynamics and cell process formation. We report an immunoperoxidase histochemical analysis of the cellular and subcellular localization of paralemmin-1 in the rat tissues where its expression is highest: the brain, the adrenal gland and the kidney. Paralemmin-1 is detected throughout the brain, in neuronal perikarya, axons and dendrites including dendritic spines and also in glial processes. In the adrenal gland, paralemmin-1 is highly expressed in the medulla. The kidney displays a pattern of differential paralemmin-1 expression in various structures and cell types, with high concentrations in cells of the parietal epithelium of Bowman's capsule, intermediate tubules, distal tubules and principal cells of outer medullary collecting ducts. Mosaics of paralemmin-positive and paralemmin-negative cells are observed in proximal tubules, the parietal epithelium of Bowman's capsule and the endothelium of many blood vessels. Plasma membrane association in epithelia is often polarized: paralemmin-1 concentrates at the apical membranes of adrenal chromaffin cells, but at the basolateral plasma membranes of proximal and distal tubule cells in the kidney. Paralemmin-1 immunoreactivity exhibits a spotted pattern and can be seen both at plasma membranes and within the cytoplasm, where it is often associated with endomembranes. This discontinuous distribution and the detergent extraction properties of paralemmin-1 suggest an association with lipid microdomains. The findings are consistent with a role for paralemmin-1 in the formation and stabilization of plasma membrane elaborations, in neurons as well as in other cell types.

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Paralemnin of the lens

Cited by 9 publications

References 11 publications

Tight binding of proteins to membranes from older human cells

Tight binding of proteins to membranes from older human cells

Palm is expressed in both developing and adult mouse lens and retina

Cellular and subcellular localization of paralemmin-1, a protein involved in cell shape control, in the rat brain, adrenal gland and kidney

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