東華大學圖書館 |

語系: 繁體中文

說明(常見問題)

回圖書館首頁

手機版館藏查詢

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

Modulation of cell migration, nuclea...

Cassella, Melanie.

FindBook

Google Book

Amazon

博客來

Modulation of cell migration, nuclear localization and cell cycle progression by the L1-CAM cytoplasmic domain: Implications for tumor progression and metastasis.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Modulation of cell migration, nuclear localization and cell cycle progression by the L1-CAM cytoplasmic domain: Implications for tumor progression and metastasis./
作者:	Cassella, Melanie.
面頁冊數:	210 p.
附註:	Adviser: Dan Felsenfeld.
Contained By:	Dissertation Abstracts International68-11B.
標題:	Biology, Cell. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3290047
ISBN:	9780549333067

Modulation of cell migration, nuclear localization and cell cycle progression by the L1-CAM cytoplasmic domain: Implications for tumor progression and metastasis.
Cassella, Melanie.

Modulation of cell migration, nuclear localization and cell cycle progression by the L1-CAM cytoplasmic domain: Implications for tumor progression and metastasis. - 210 p.

Adviser: Dan Felsenfeld.

Thesis (Ph.D.)--Mount Sinai School of Medicine of New York University, 2008.

As cancer progresses from a benign to a metastatic phenotype, tumor cells lose adhesive contacts with neighboring cells and gain the capacity to invade the surrounding tissue and blood vessels. As the adhesion and migration of tumor cells depends on the activity of cell adhesion receptors, characterizing the regulation of these proteins is critical to our understanding of cancer progression. L1-CAM, a neuronal adhesion protein, is expressed in cancer and is associated with tumor progression, invasive growth, and increased metastasis. In cancer cells, the extra-cellular domain of L1-CAM is cleaved from the cell surface and can bind to the extra-cellular matrix and act as a ligand for integrin-mediated cell migration. Although the role of the L1-CAM-extracellular domain in this process is well characterized, the cytoplasmic domain of L1-CAM, which remains in the cell following cleavage, may also contribute to tumor cell migration and other aspects of cancer progression. We examined the role of the L1-CAM cytoplasmic domain in regulating ADAM-mediated proteolysis, L1-mediated cell migration, nuclear localization and cell cycle progression. Mutations that disrupt L1-CAM-cytoskeletal interactions lead to an increase in proteolysis of L1-CAM, and also disrupt L1-mediated migration in both HEK-293 cells and melanoma cells, in a manner similar to what is seen in neural cells. The L1-CAM cytoplasmic tail fragment can be detected in cells up to 1 hour following induced proteolysis, and can be detected in the nucleus by both biochemical and immunohistochemical methods. L1-CAM expression increases the number of mitotic cells, raising the possibility that processing of the L1-CAM cytoplasmic tail may regulate cell division. Cytoplasmic tail truncations and site directed mutagenesis revealed distinct regions of the L1-CAM cytoplasmic tail that mediate nuclear localization as well as L1-mediated cell cycle progression. The discovery of these biological activities of L1-CAM shows the complex role of L1-CAM in tumor cells, and suggests novel mechanisms by which L1-CAM expression results in increased tumor growth, invasion and metastasis. Understanding this pathway may ultimately lead to improved treatment of patients with highly aggressive tumors.

ISBN: 9780549333067Subjects--Topical Terms:

1017686
Biology, Cell.

Modulation of cell migration, nuclear localization and cell cycle progression by the L1-CAM cytoplasmic domain: Implications for tumor progression and metastasis.
LDR:03286nam 2200289 a 45 001 943715
005 20110520
008 110520s2008 ||||||||||||||||| ||eng d
020 $a 9780549333067
035 $a (UMI)AAI3290047
035 $a AAI3290047
040 $a UMI $c UMI
100 1 $a Cassella, Melanie. $3 1267753
245 1 0 $a Modulation of cell migration, nuclear localization and cell cycle progression by the L1-CAM cytoplasmic domain: Implications for tumor progression and metastasis.
300 $a 210 p.
500 $a Adviser: Dan Felsenfeld.
500 $a Source: Dissertation Abstracts International, Volume: 68-11, Section: B, page: 7057.
502 $a Thesis (Ph.D.)--Mount Sinai School of Medicine of New York University, 2008.
520 $a As cancer progresses from a benign to a metastatic phenotype, tumor cells lose adhesive contacts with neighboring cells and gain the capacity to invade the surrounding tissue and blood vessels. As the adhesion and migration of tumor cells depends on the activity of cell adhesion receptors, characterizing the regulation of these proteins is critical to our understanding of cancer progression. L1-CAM, a neuronal adhesion protein, is expressed in cancer and is associated with tumor progression, invasive growth, and increased metastasis. In cancer cells, the extra-cellular domain of L1-CAM is cleaved from the cell surface and can bind to the extra-cellular matrix and act as a ligand for integrin-mediated cell migration. Although the role of the L1-CAM-extracellular domain in this process is well characterized, the cytoplasmic domain of L1-CAM, which remains in the cell following cleavage, may also contribute to tumor cell migration and other aspects of cancer progression. We examined the role of the L1-CAM cytoplasmic domain in regulating ADAM-mediated proteolysis, L1-mediated cell migration, nuclear localization and cell cycle progression. Mutations that disrupt L1-CAM-cytoskeletal interactions lead to an increase in proteolysis of L1-CAM, and also disrupt L1-mediated migration in both HEK-293 cells and melanoma cells, in a manner similar to what is seen in neural cells. The L1-CAM cytoplasmic tail fragment can be detected in cells up to 1 hour following induced proteolysis, and can be detected in the nucleus by both biochemical and immunohistochemical methods. L1-CAM expression increases the number of mitotic cells, raising the possibility that processing of the L1-CAM cytoplasmic tail may regulate cell division. Cytoplasmic tail truncations and site directed mutagenesis revealed distinct regions of the L1-CAM cytoplasmic tail that mediate nuclear localization as well as L1-mediated cell cycle progression. The discovery of these biological activities of L1-CAM shows the complex role of L1-CAM in tumor cells, and suggests novel mechanisms by which L1-CAM expression results in increased tumor growth, invasion and metastasis. Understanding this pathway may ultimately lead to improved treatment of patients with highly aggressive tumors.
590 $a School code: 1353.
650 4 $a Biology, Cell. $3 1017686
650 4 $a Health Sciences, Oncology. $3 1018566
650 4 $a Health Sciences, Pharmacology. $3 1017717
690 $a 0379
690 $a 0419
690 $a 0992
710 2 $a Mount Sinai School of Medicine of New York University. $3 1025278
773 0 $t Dissertation Abstracts International $g 68-11B.
790 $a 1353
790 1 0 $a Felsenfeld, Dan, $e advisor
791 $a Ph.D.
792 $a 2008
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3290047