Regulation of surfactant secretion

Rooney, Seamus A.

doi:10.1016/s1095-6433(01)00320-8

Cited by 143 publications

(127 citation statements)

References 77 publications

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“…viral replication might affect the outcome. In mammals site specific expression and secretion of collectins in the airways has been reported (Coalson et al, 1998;Rooney, 2001). Furthermore, down regulation of SP-A gene expression through p38 MAPK and PI-3 kinase pathways have been described in lung epithelial cells (Miakotina et al, 2002a;Miakotina and Snyder, 2002b).…”

Section: Discussionmentioning

confidence: 99%

Transcriptional expression levels of chicken collectins are affected by avian influenza A virus inoculation

Reemers

Veldhuizen

Fleming

et al. 2010

Veterinary Microbiology

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Section: Discussionmentioning

confidence: 99%

Transcriptional expression levels of chicken collectins are affected by avian influenza A virus inoculation

Reemers

Veldhuizen

Fleming

et al. 2010

Veterinary Microbiology

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“…The PLD pathway has been implicated in a number of physiological functions, including secretion. For example, as elaborated in LPPs and lung function, surfactant secretion can be controlled in this manner (209,212).…”

Section: Substrates For Lppmentioning

confidence: 99%

“…Surfactant secretion can be stimulated in isolated alveolar type II cells through three distinct signal transduction pathways: 1) A 2␤ -adenosine or ␤ 2 -adrenergic receptors influencing activation of adenyl cyclase; 2) stretch and other receptors leading to influx of Ca 2ϩ and activation of calcium-calmodulin effectors; and 3) P2Y2 purinergic receptors resulting in PI-PLC activation, DAG activation of PKC, and elevation of intracellular Ca 2ϩ by IP 3 . Considerable cross talk occurs between these systems (152,209,210,212).…”

Section: Pap1mentioning

confidence: 99%

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Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase

Nanjundan

Possmayer

2003

American Journal of Physiology-Lung Cellular and Molecular Phys

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The lung contains two distinct forms of phosphatidic acid phosphatase (PAP). PAP1 is a cytosolic enzyme that is activated through fatty acid-induced translocation to the endoplasmic reticulum, where it converts phosphatidic acid (PA) to diacylglycerol (DAG) for the biosynthesis of phospholipids and neutral lipids. PAP1 is Mg2+ dependent and sulfhydryl reagent sensitive. PAP2 is a six-transmembrane-domain integral protein localized to the plasma membrane. Because PAP2 degrades sphingosine-1-phosphate (S1P) and ceramide-1-phosphate in addition to PA and lyso-PA, it has been renamed lipid phosphate phosphohydrolase (LPP). LPP is Mg2+independent and sulfhydryl reagent insensitive. This review describes LPP isoforms found in the lung and their location in signaling platforms (rafts/caveolae). Pulmonary LPPs likely function in the phospholipase D pathway, thereby controlling surfactant secretion. Through lowering the levels of lyso-PA and S1P, which serve as agonists for endothelial differentiation gene receptors, LPPs regulate cell division, differentiation, apoptosis, and mobility. LPP activity could also influence transdifferentiation of alveolar type II to type I cells. It is considered likely that these lipid phosphohydrolases have critical roles in lung morphogenesis and in acute lung injury and repair.

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“…Furthermore, LPS also induces acute pulmonary inflammation, causing rapid changes in the composition of the surfactant pool in human lung (Rooney, 2001). Pulmonary alveolar type II epithelial cells, located in the corners of the alveoli, highly specialize functions for synthesizing, secreting and reutilizing surfactants (Rooney, 2001).…”

Section: Introductionmentioning

confidence: 99%

Apoptosis and surfactant protein-C expression inhibition induced by lipopolysaccharide in AEC II cell may associate with NF-κB pathway

et al. 2017

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-Lipopolysaccharide (LPS), a Gram-negative bacterial outer membrane component, is one of the major causes of septic shock. Herein we investigate LPS-induced apoptosis of rat alveolar epithelial type II cells (AEC II) and the effects of LPS on surfactant protein-C (SP-C) expression in AEC II, along with the possible molecular mechanisms. LPS exposure impaired cell viability and increased apoptosis of AEC II significantly in concentration-dependent manner embodied in increased caspase-3 expression and the activity of caspase-3. Simultaneously, our results also indicated that LPS inhibited surfactant protein-C (SP-C) expression in AEC II. Mechanistic studies revealed that LPS treatment significantly increased the expression of NF-κB p50, NF-κB p65 and IKKβ proteins as well as induced IκB-α phosphorylation. Moreover, pretreatment with IKK inhibitor IKK-16 or NF-κB inhibitor PDTC ameliorated LPScaused alterations in cleaved caspase-3 expression, the activity of caspase-3 and SP-C expression. Taken together, these results demonstrate that LPS can induce apoptosis of AEC II and decrease SP-C expression partly through activating the NF-κB pathway.

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Regulation of surfactant secretion

Cited by 143 publications

References 77 publications

Transcriptional expression levels of chicken collectins are affected by avian influenza A virus inoculation

Transcriptional expression levels of chicken collectins are affected by avian influenza A virus inoculation

Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase

Apoptosis and surfactant protein-C expression inhibition induced by lipopolysaccharide in AEC II cell may associate with NF-κB pathway

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