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LASP1, a Newly Identified Melanocytic Protein with a Possible Role in Melanin Release, but Not in Melanoma Progression.

Vaman V S A, Poppe H, Houben R, Grunewald TG, Goebeler M, Butt E - PLoS ONE (2015)

Bottom Line: In melanocytes, the protein is bound to dynamin and mainly localized at late melanosomes along the edges and at the tips of the cell.Knockdown of LASP1 results in increased melanin concentration in the cells.Collectively, we identified LASP1 as a hitherto unknown protein in melanocytes and as novel partner of dynamin in the physiological process of membrane constriction and melanosome vesicle release.

View Article: PubMed Central - PubMed

Affiliation: Institute of Clinical Biochemistry and Pathobiochemistry, University Hospital Würzburg, Würzburg, Germany.

ABSTRACT
The LIM and SH3 protein 1 (LASP1) is a focal adhesion protein. Its expression is increased in many malignant tumors. However, little is known about the physiological role of the protein. In the present study, we investigated the expression and function of LASP1 in normal skin, melanocytic nevi and malignant melanoma. In normal skin, a distinct LASP1 expression is visible only in the basal epidermal layer while in nevi LASP1 protein is detected in all melanocytes. Melanoma exhibit no increase in LASP1 mRNA compared to normal skin. In melanocytes, the protein is bound to dynamin and mainly localized at late melanosomes along the edges and at the tips of the cell. Knockdown of LASP1 results in increased melanin concentration in the cells. Collectively, we identified LASP1 as a hitherto unknown protein in melanocytes and as novel partner of dynamin in the physiological process of membrane constriction and melanosome vesicle release.

No MeSH data available.


Related in: MedlinePlus

Immunofluorescence of LASP1 and tyrosinase in NHEM cells.Black and white image of a NHEM cell with highlighted blue nucleus and circled enlarged dendrite tip (upper panel). LASP1 (red) and tyrosinase (green) immunofluorescence at the dendrite tip of the NHEM cell (middle panels). Co-localization of the merged LASP1-tyrosinase complex (white arrows) with pointed melanosomes (black arrows) in the bright-field image at the dendrite tip of the NHEM cell (lower panels).
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pone.0129219.g007: Immunofluorescence of LASP1 and tyrosinase in NHEM cells.Black and white image of a NHEM cell with highlighted blue nucleus and circled enlarged dendrite tip (upper panel). LASP1 (red) and tyrosinase (green) immunofluorescence at the dendrite tip of the NHEM cell (middle panels). Co-localization of the merged LASP1-tyrosinase complex (white arrows) with pointed melanosomes (black arrows) in the bright-field image at the dendrite tip of the NHEM cell (lower panels).

Mentions: In line with these results, co-localization of the LASP1-dynamin complex with melanosomes at the tips of melanocyte dendrites is visible in Fig 6C. Furthermore, co-localization of LASP1 and tyrosinase (Fig 7) perfectly matches with the peripheral melanosomes, visible as dark spots in the bright-field illumination.


LASP1, a Newly Identified Melanocytic Protein with a Possible Role in Melanin Release, but Not in Melanoma Progression.

Vaman V S A, Poppe H, Houben R, Grunewald TG, Goebeler M, Butt E - PLoS ONE (2015)

Immunofluorescence of LASP1 and tyrosinase in NHEM cells.Black and white image of a NHEM cell with highlighted blue nucleus and circled enlarged dendrite tip (upper panel). LASP1 (red) and tyrosinase (green) immunofluorescence at the dendrite tip of the NHEM cell (middle panels). Co-localization of the merged LASP1-tyrosinase complex (white arrows) with pointed melanosomes (black arrows) in the bright-field image at the dendrite tip of the NHEM cell (lower panels).
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4465371&req=5

pone.0129219.g007: Immunofluorescence of LASP1 and tyrosinase in NHEM cells.Black and white image of a NHEM cell with highlighted blue nucleus and circled enlarged dendrite tip (upper panel). LASP1 (red) and tyrosinase (green) immunofluorescence at the dendrite tip of the NHEM cell (middle panels). Co-localization of the merged LASP1-tyrosinase complex (white arrows) with pointed melanosomes (black arrows) in the bright-field image at the dendrite tip of the NHEM cell (lower panels).
Mentions: In line with these results, co-localization of the LASP1-dynamin complex with melanosomes at the tips of melanocyte dendrites is visible in Fig 6C. Furthermore, co-localization of LASP1 and tyrosinase (Fig 7) perfectly matches with the peripheral melanosomes, visible as dark spots in the bright-field illumination.

Bottom Line: In melanocytes, the protein is bound to dynamin and mainly localized at late melanosomes along the edges and at the tips of the cell.Knockdown of LASP1 results in increased melanin concentration in the cells.Collectively, we identified LASP1 as a hitherto unknown protein in melanocytes and as novel partner of dynamin in the physiological process of membrane constriction and melanosome vesicle release.

View Article: PubMed Central - PubMed

Affiliation: Institute of Clinical Biochemistry and Pathobiochemistry, University Hospital Würzburg, Würzburg, Germany.

ABSTRACT
The LIM and SH3 protein 1 (LASP1) is a focal adhesion protein. Its expression is increased in many malignant tumors. However, little is known about the physiological role of the protein. In the present study, we investigated the expression and function of LASP1 in normal skin, melanocytic nevi and malignant melanoma. In normal skin, a distinct LASP1 expression is visible only in the basal epidermal layer while in nevi LASP1 protein is detected in all melanocytes. Melanoma exhibit no increase in LASP1 mRNA compared to normal skin. In melanocytes, the protein is bound to dynamin and mainly localized at late melanosomes along the edges and at the tips of the cell. Knockdown of LASP1 results in increased melanin concentration in the cells. Collectively, we identified LASP1 as a hitherto unknown protein in melanocytes and as novel partner of dynamin in the physiological process of membrane constriction and melanosome vesicle release.

No MeSH data available.


Related in: MedlinePlus