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The role of surfactant proteins A an...

Alcorn, John F., Jr.

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

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	The role of surfactant proteins A and D in innate immunity: Regulation of inflammation and bacterial abrogation of protein function./
作者:	Alcorn, John F., Jr.
面頁冊數:	157 p.
附註:	Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0029.
Contained By:	Dissertation Abstracts International65-01B.
標題:	Biology, Cell. -
電子資源:	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.
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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.
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650 4 $a Biology, Cell. $3 1017686
650 4 $a Health Sciences, Immunology. $3 1017716
650 4 $a Chemistry, Biochemistry. $3 1017722
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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
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791 $a Ph.D.
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