東華大學圖書館 |

Language: English

Help

回圖書館首頁

手機版館藏查詢

Back

Switch To: Labeled | MARC Mode | ISBD

Structure/function studies of lipid ...

Subramanian, Vidya.

Linked to FindBook

Google Book

Amazon

博客來

Structure/function studies of lipid droplet-associated proteins perilipin A and CGI-58.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Structure/function studies of lipid droplet-associated proteins perilipin A and CGI-58./
Author:	Subramanian, Vidya.
Description:	275 p.
Notes:	Source: Dissertation Abstracts International, Volume: 67-01, Section: B, page: 0187.
Contained By:	Dissertation Abstracts International67-01B.
Subject:	Health Sciences, Nutrition. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3203406
ISBN:	9780542514159

Structure/function studies of lipid droplet-associated proteins perilipin A and CGI-58.
Subramanian, Vidya.

Structure/function studies of lipid droplet-associated proteins perilipin A and CGI-58. - 275 p.

Source: Dissertation Abstracts International, Volume: 67-01, Section: B, page: 0187.

Thesis (Ph.D.)--Rutgers The State University of New Jersey - New Brunswick, 2006.

In mammalian cells, proteins coat the surfaces of intracellular lipid droplets. The goal of this dissertation was to study the structure-function relationships of two lipid droplet associated proteins, perilipin A and CGI-58. Perilipin A is a major lipid droplet associated protein in adipocytes that plays a key role in regulating the storage and hydrolysis of triacylglycerol. Three moderately hydrophobic sequences present within the central region of perilipin A in conjunction with either an amino terminal sequence predicted to form amphipathic beta-strands or a central acidic region are important for targeting perilipin A to lipid droplets. These moderately hydrophobic sequences also mediate the anchoring of perilipin A to lipid droplets. Other sequences within perilipin A likely interact with cellular proteins; CGI-58 requires perilipin A for localization to lipid droplets. Both endogenous and GFP-tagged ectopic CGI-58 localize to perilipin coated lipid droplets in 3T3-L1 adipocytes and in preadipocytes expressing ectopic perilipin A. In adipocytes under basal conditions, CGI-58 localizes to perilipin-coated lipid droplets, however, upon stimulation of beta-adrenergic receptors, CGI-58 disperses off of lipid droplets and shows diffuse cytoplasmic localization, suggesting that the interaction between CGI-58 and perilipin A is sensitive to metabolic status. We mapped the site of interaction of CGI-58 to a 48-amino acid sequence within the carboxyl terminus of perilipin A. Mutations in CGI-58 cause NLSD, which is characterized by accumulation of triacylglycerol-rich lipid droplets in many tissues; however, the function of CGI-58 in triacylglycerol metabolism is unknown. Expression of ectopic CGI-58 in NLSD fibroblasts clears the excessive triacylglycerol without altering the triacylglycerol lipase activity of cell lysates. In contrast, expression of ectopic hormone-sensitive lipase decreases triacylglycerol accumulation in NLSD fibroblasts lacking CGI-58 by increasing cellular triacylglycerol lipase activity, suggesting that CGI-58 is not required for this pathway of lipolysis. In conclusion, three central hydrophobic sequences target and anchor perilipin A to lipid droplets, whereas a 48-amino acid sequence within the carboxyl terminus of perilipin A mediates an interaction with CGI-58. In addition, CGI58 facilitates the clearance of triacylglycerol in human skin fibroblasts without altering triacylglycerol lipase activity, and CGI-58 is not a component of all lipolytic pathways.

ISBN: 9780542514159Subjects--Topical Terms:

1017801
Health Sciences, Nutrition.

Structure/function studies of lipid droplet-associated proteins perilipin A and CGI-58.
LDR:03485nmm 2200289 4500 001 1825086
005 20061201092002.5
008 130610s2006 eng d
020 $a 9780542514159
035 $a (UnM)AAI3203406
035 $a AAI3203406
040 $a UnM $c UnM
100 1 $a Subramanian, Vidya. $3 1914110
245 1 0 $a Structure/function studies of lipid droplet-associated proteins perilipin A and CGI-58.
300 $a 275 p.
500 $a Source: Dissertation Abstracts International, Volume: 67-01, Section: B, page: 0187.
500 $a Adviser: Dawn L. Brasaemle.
502 $a Thesis (Ph.D.)--Rutgers The State University of New Jersey - New Brunswick, 2006.
520 $a In mammalian cells, proteins coat the surfaces of intracellular lipid droplets. The goal of this dissertation was to study the structure-function relationships of two lipid droplet associated proteins, perilipin A and CGI-58. Perilipin A is a major lipid droplet associated protein in adipocytes that plays a key role in regulating the storage and hydrolysis of triacylglycerol. Three moderately hydrophobic sequences present within the central region of perilipin A in conjunction with either an amino terminal sequence predicted to form amphipathic beta-strands or a central acidic region are important for targeting perilipin A to lipid droplets. These moderately hydrophobic sequences also mediate the anchoring of perilipin A to lipid droplets. Other sequences within perilipin A likely interact with cellular proteins; CGI-58 requires perilipin A for localization to lipid droplets. Both endogenous and GFP-tagged ectopic CGI-58 localize to perilipin coated lipid droplets in 3T3-L1 adipocytes and in preadipocytes expressing ectopic perilipin A. In adipocytes under basal conditions, CGI-58 localizes to perilipin-coated lipid droplets, however, upon stimulation of beta-adrenergic receptors, CGI-58 disperses off of lipid droplets and shows diffuse cytoplasmic localization, suggesting that the interaction between CGI-58 and perilipin A is sensitive to metabolic status. We mapped the site of interaction of CGI-58 to a 48-amino acid sequence within the carboxyl terminus of perilipin A. Mutations in CGI-58 cause NLSD, which is characterized by accumulation of triacylglycerol-rich lipid droplets in many tissues; however, the function of CGI-58 in triacylglycerol metabolism is unknown. Expression of ectopic CGI-58 in NLSD fibroblasts clears the excessive triacylglycerol without altering the triacylglycerol lipase activity of cell lysates. In contrast, expression of ectopic hormone-sensitive lipase decreases triacylglycerol accumulation in NLSD fibroblasts lacking CGI-58 by increasing cellular triacylglycerol lipase activity, suggesting that CGI-58 is not required for this pathway of lipolysis. In conclusion, three central hydrophobic sequences target and anchor perilipin A to lipid droplets, whereas a 48-amino acid sequence within the carboxyl terminus of perilipin A mediates an interaction with CGI-58. In addition, CGI58 facilitates the clearance of triacylglycerol in human skin fibroblasts without altering triacylglycerol lipase activity, and CGI-58 is not a component of all lipolytic pathways.
590 $a School code: 0190.
650 4 $a Health Sciences, Nutrition. $3 1017801
650 4 $a Biology, Cell. $3 1017686
650 4 $a Biology, Molecular. $3 1017719
690 $a 0570
690 $a 0379
690 $a 0307
710 2 0 $a Rutgers The State University of New Jersey - New Brunswick. $3 1017590
773 0 $t Dissertation Abstracts International $g 67-01B.
790 1 0 $a Brasaemle, Dawn L., $e advisor
790 $a 0190
791 $a Ph.D.
792 $a 2006
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3203406