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Metabolomics,Unknown,Transcriptomics,Genomics,Proteomics

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Transcription profiling of human clinical pediatric acute lymphatic leukemai - ALL samples after in vitro exposure to Lasp (and matched controls)

ABSTRACT: Samples of pediatric acute lymphoblastic leukemia. All samples contain at least 90% blasts. Each sample was split into two flasks, one of which was exposed to 2IU/ml of L-asparaginase. The other flask served as a control. Cells were lysed at the times indicated.

ORGANISM(S): Homo sapiens

SUBMITTER: Janos Demeter

PROVIDER: E-SMDB-26 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Transcription profiling of clinical pediatric acute lymphoblastic leukemia ALL samples after in vitro exposure to Lasp (and matched controls)

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Project description:Samples of pediatric acute lymphoblastic leukemia. All samples contain at least 90% blasts. Each sample was split into two flasks, one of which was exposed to 2IU/ml of L-asparaginase. The other flask served as a control. Cells were lysed at the times indicated. Set of arrays organized by shared biological context, such as organism, tumors types, processes, etc. Keywords: Logical Set

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Lasp-1 regulates podosome function.

Project description:Eukaryotic cells form a variety of adhesive structures to connect with their environment and to regulate cell motility. In contrast to classical focal adhesions, podosomes, highly dynamic structures of different cell types, are actively engaged in matrix remodelling and degradation. Podosomes are composed of an actin-rich core region surrounded by a ring-like structure containing signalling molecules, motor proteins as well as cytoskeleton-associated proteins. Lasp-1 is a ubiquitously expressed, actin-binding protein that is known to regulate cytoskeleton architecture and cell migration. This multidomain protein is predominantely present at focal adhesions, however, a second pool of Lasp-1 molecules is also found at lamellipodia and vesicle-like microdomains in the cytosol.In this report, we show that Lasp-1 is a novel component and regulator of podosomes. Immunofluorescence studies reveal a localization of Lasp-1 in the podosome ring structure, where it colocalizes with zyxin and vinculin. Life cell imaging experiments demonstrate that Lasp-1 is recruited in early steps of podosome assembly. A siRNA-mediated Lasp-1 knockdown in human macrophages affects podosome dynamics as well as their matrix degradation capacity. In summary, our data indicate that Lasp-1 is a novel component of podosomes and is involved in the regulation of podosomal function.

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