In Situ Hybridization of SP-A mRNA in Adult Human Conducting Airways

Khubchandani, Kavita R.; Goss, Kelli L.; Engelhardt, John F.; Snyder, Jeanne M.

doi:10.1080/15513810109168620

Cited by 12 publications

(6 citation statements)

References 26 publications

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“…The SP-A1 and SP-A2 genes are differentially expressed in different tissues. Only the SP-A2 gene is predominantly detected in the trachea [25] and submucosal gland cells in the airway [20], whereas SP-A1 and SP-A2 transcript expressions are both detected in the small and large intestines of humans [26]. If the SP-A1 gene is only expressed, then the SP-A cDNA fragment (439 bp) can be digested by Apa I.…”

Section: Discussionmentioning

confidence: 99%

Lipopolysaccharide-induced expression of surfactant proteins A1 and A2 in human renal tubular epithelial cells

Liu

Wang

et al. 2013

J Inflamm

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BackgroundSurfactant protein A (SP-A), encoded by two functional genes, SP-A1 and SP-A2, is essential for the inflammatory process and host defence in the lungs. Recent studies have demonstrated the extrapulmonary expression of SP-A. Similar to the lungs, the kidneys are organs exposed to external pathogens. The present study evaluated the expression and location of SP-A in the kidneys. The effect of lipopolysaccharide (LPS) on the expression of SP-A subtypes was also studied in renal tubular epithelial (HK-2) cells.MethodsImmunohistochemical staining was performed using polyclonal antibody against SP-A. RT-PCR was also performed using mRNA from normal human renal tissues and HK-2 cells. The expressions of the SP-A1 and SP-A2 genes were determined by PCR-based RFLP analysis, gene-specific amplification, and direct sequencing of RT-PCR products. Western blot was conducted to analyse the SP-A protein. HK-2 cells were treated with LPS at various concentrations (0, 0.1, 1, 2, 5, and 10 μg/mL) for 8 h and at 5 μg/mL at various time points (0, 2, 4, 8, 16, and 24 h). The LPS-induced expressions of SP-A1 and SP-A2 mRNA and protein were analysed by RT-PCR and Western blot.ResultsSP-A was localised in the renal tubular epithelial cells in the proximal and distal convoluted tubules. SP-A1 and SP-A2 mRNA and protein were expressed in HK-2 cells and human renal tissues, which were significantly increased in time- and dose-dependent manners after LPS treatment (P < 0.05).ConclusionsHuman renal tubular epithelial cells can express both SP-A1 and SP-A2 genes, which may play important roles in the inflammatory modulation of the kidney.

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Section: Discussionmentioning

confidence: 99%

Lipopolysaccharide-induced expression of surfactant proteins A1 and A2 in human renal tubular epithelial cells

Liu

Wang

et al. 2013

J Inflamm

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“…SP-A is an antimicrobial protein that contains both a collagenlike domain and a calcium dependent (C-type) lectin domain (collectins) and is produced by airway epithelial cells in the conducting airway (6,22,42). In knockout murine models, loss of SP-A increases susceptibility to bacterial infection (26).…”

Section: Discussionmentioning

confidence: 99%

Bordetella bronchisepticaAdherence to Cilia Is Mediated by Multiple Adhesin Factors and Blocked by Surfactant Protein A

Edwards¹,

Groathouse

Boitano

2005

Infect Immun

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“…As multimeric forms of SP-A are more active, we speculate that in CF and in part in bronchitis they may result from disease-induced systemic activation and enhanced formation. The lack of correlation between serum and lavage compartments may reflect no direct feed of the serum compartment from the alveolar space [22], [23].…”

Section: Discussionmentioning

confidence: 99%

Surfactant Protein A in Cystic Fibrosis: Supratrimeric Structure and Pulmonary Outcome

Griese

Heinrich²,

Ratjen³

et al. 2012

PLoS ONE

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BackgroundThe state of oligomerization of surfactant associated protein-A (SP-A) monomers differs between individuals. This likely affects SP-A’s functional properties and could thereby influence clinical status in patients with lung diseases. In this study we focus on SP-A structure in cystic fibrosis (CF) compared to both healthy subjects and disease controls.MethodsSP-A composition and function were assessed in both bronchoalveolar lavage (BAL) fluid and serum of 46 CF patients with mild disease, 25 patients with chronic bronchitis and 22 healthy subjects by gel chromatography and a functional agglutination assay. Relation of SP-A agglutination ability to disease severity of the subjects was explored.ResultsSP-A was present in seven major oligomeric forms with the majority of SP-A being structurally organized as complex oligomeric forms. More complex oligomeric forms were associated with better SP-A function with regard to its agglutination ability. These forms were more frequently observed in BAL than in serum, but there were no differences between disease groups. In CF patients, more complex forms of SP-A were associated with better lung function.ConclusionsOrganizational structure of SP-A affects its functional activity and is linked to disease severity in CF.

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In Situ Hybridization of SP-A mRNA in Adult Human Conducting Airways

Cited by 12 publications

References 26 publications

Lipopolysaccharide-induced expression of surfactant proteins A1 and A2 in human renal tubular epithelial cells

Lipopolysaccharide-induced expression of surfactant proteins A1 and A2 in human renal tubular epithelial cells

Bordetella bronchisepticaAdherence to Cilia Is Mediated by Multiple Adhesin Factors and Blocked by Surfactant Protein A

Surfactant Protein A in Cystic Fibrosis: Supratrimeric Structure and Pulmonary Outcome

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