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

The role of surfactant proteins A an...

Alcorn, John F., Jr.

Linked to FindBook

Google Book

Amazon

博客來

The role of surfactant proteins A and D in innate immunity: Regulation of inflammation and bacterial abrogation of protein function.

Record Type:	Electronic resources : Monograph/item
Title/Author:	The role of surfactant proteins A and D in innate immunity: Regulation of inflammation and bacterial abrogation of protein function./
Author:	Alcorn, John F., Jr.
Description:	157 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0029.
Contained By:	Dissertation Abstracts International65-01B.
Subject:	Biology, Cell. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3120170
ISBN:	0496675427

The role of surfactant proteins A and D in innate immunity: Regulation of inflammation and bacterial abrogation of protein function.
Alcorn, John F., Jr.

The role of surfactant proteins A and D in innate immunity: Regulation of inflammation and bacterial abrogation of protein function. - 157 p.

Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0029.

Thesis (Ph.D.)--Duke University, 2003.

The alveolar epithelium is lined by surfactant, a lipoprotein complex which both reduces surface tension and mediates several innate immune functions including alteration of alveolar macrophage function and regulation of bacterial clearance. The goal of this thesis is to examine the anti-inflammatory properties of surfactant proteins---A and D (SP-A, SP-D). In addition, we propose that the lung pathogen, Pseudomonas aeruginosa, via proteolysis, can subvert the normal immune function of SP-A and SP-D.

ISBN: 0496675427Subjects--Topical Terms:

1017686
Biology, Cell.

The role of surfactant proteins A and D in innate immunity: Regulation of inflammation and bacterial abrogation of protein function.
LDR:03440nmm 2200325 4500 001 1844131
005 20051017073437.5
008 130614s2003 eng d
020 $a 0496675427
035 $a (UnM)AAI3120170
035 $a AAI3120170
040 $a UnM $c UnM
100 1 $a Alcorn, John F., Jr. $3 1932334
245 1 4 $a The role of surfactant proteins A and D in innate immunity: Regulation of inflammation and bacterial abrogation of protein function.
300 $a 157 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0029.
500 $a Adviser: Jo Rae Wright.
502 $a Thesis (Ph.D.)--Duke University, 2003.
520 $a The alveolar epithelium is lined by surfactant, a lipoprotein complex which both reduces surface tension and mediates several innate immune functions including alteration of alveolar macrophage function and regulation of bacterial clearance. The goal of this thesis is to examine the anti-inflammatory properties of surfactant proteins---A and D (SP-A, SP-D). In addition, we propose that the lung pathogen, Pseudomonas aeruginosa, via proteolysis, can subvert the normal immune function of SP-A and SP-D.
520 $a We and others have previously shown that SP-A inhibits the macrophage production of tumor necrosis factor-alpha (TNF-alpha) stimulated by lipopolysaccharide (LPS). We propose that SP-A decreases the production of pro-inflammatory cytokines by alveolar macrophages via a CD14-independent mechanism. SP-A and SP-D inhibited TNF-alpha production by alveolar macrophages stimulated with LPS. Furthermore, SP-A also diminished ultra-pure LPS-induced TNF-alpha produced by wild-type and CD14 null alveolar macrophages. Additionally, SP-A inhibited TNF-alpha stimulated by phorbol ester myristate (PMA). These data suggest that SP-A inhibits inflammatory cytokine production in a CD 14-independent manner and also by mechanisms independent of the LPS signaling pathway.
520 $a Several studies provide evidence that SP-A and SP-D have an important role in the innate immune response to the gram-negative bacteria, Pseudomonas aeruginosa. In preliminary experiments characterizing the binding of SP-A to this bacteria, we observed the appearance of apparent degradation products of SP-A and therefore, we hypothesized that P. aeruginosa produces an enzyme that degrades SP-A. The degradative enzyme was purified and identified as Pseudomonas elastase, which was shown to directly degrade SP-A and SP-D. Furthermore, SP-A and SP-D degradation fragments were detectable in bronchoalveolar lavage (BAL) from lung transplant patients with cystic fibrosis.
520 $a SP-D is cleaved by elastase to produce a stable 35 kDa fragment. Unlike intact SP-D, the SP-D cleavage fragment fails to bind or aggregate bacteria. Additionally, the SP-D fragment fails to enhance the uptake of bacteria by alveolar macrophages. We speculate that degradation of SP-A and SP-D by P. aeruginosa elastase presents a novel virulence mechanism. Degradation of SP-A and SP-D by P. aeruginosa would lead to greater production of inflammatory mediators and reduced clearance in the lung.
590 $a School code: 0066.
650 4 $a Biology, Cell. $3 1017686
650 4 $a Health Sciences, Immunology. $3 1017716
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0379
690 $a 0982
690 $a 0487
710 2 0 $a Duke University. $3 569686
773 0 $t Dissertation Abstracts International $g 65-01B.
790 1 0 $a Wright, Jo Rae, $e advisor
790 $a 0066
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3120170