scholarly journals Alveolar Type II cell transplantation restores pulmonary surfactant protein levels in lung fibrosis

2014 ◽  
Vol 33 (7) ◽  
pp. 758-765 ◽  
Author(s):  
Raquel Guillamat-Prats ◽  
Gemma Gay-Jordi ◽  
Antoni Xaubet ◽  
Victor I. Peinado ◽  
Anna Serrano-Mollar
Keyword(s):  
Cell Transplantation ◽  
Lung Fibrosis ◽  
Pulmonary Surfactant ◽  
Surfactant Protein ◽  
Alveolar Type ◽  
Type Ii ◽  
Protein Levels ◽  
Alveolar Type Ii Cell ◽  
Type Ii Cell ◽  
Pulmonary Surfactant Protein

Pulmonary surfactant protein A-mediated uptake of phosphatidylcholine by alveolar type II cells

1993 ◽  
Vol 265 (2) ◽  
pp. L193-L199 ◽  
Author(s):  
A. Tsuzuki ◽  
Y. Kuroki ◽  
T. Akino
Keyword(s):  
Pulmonary Surfactant ◽  
Protein A ◽  
Lamellar Body ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Alveolar Type ◽  
Type Ii Cells ◽  
Type Ii ◽  
Lamellar Bodies ◽  
Pulmonary Surfactant Protein

Pulmonary surfactant protein A (SP-A)-mediated uptake of phosphatidylcholine (PC) by alveolar type II cells was investigated. SP-A enhanced the uptake of liposomes containing dipalmitoylphosphatidylcholine (DPPC), 1-palmitoyl-2-linoleoyl phosphatidylcholine (PLPC), or 1,2-dihexadecyl-sn-glycero-3-phosphocholine (DPPC-ether), a diether analogue of DPPC, but about twice as much DPPC was taken up by type II cells as PLPC or DPPC-ether. When subcellular distribution was analyzed, 51.3 +/- 2.9% (mean +/- SD, n = 3) of cell-associated radiolabeled DPPC was recovered in the lamellar body-rich fraction in the presence of SP-A, whereas only 19.3 +/- 1.9% (mean +/- SD, n = 3) was found to this fraction in the absence of SP-A. When type II cells were incubated either with DPPC at 0 degree C or with DPPC-ether at 37 degrees C, or no cells were included, low proportions of the cell-associated lipids were present in the fractions corresponding to lamellar bodies even in the presence of SP-A. Anti-SP-A antibody significantly reduced the radioactivity incorporated into the lamellar body fraction. Phosphatidylcholine that had been incorporated into lamellar bodies remained largely intact when SP-A was present. Subcellular fractionations of type II cells with radiolabeled SP-A and DPPC revealed that the sedimentation characteristics of cell-associated SP-A are different from those of DPPC, although a small broad peak of radiolabeled SP-A was found in the lamellar body fraction.(ABSTRACT TRUNCATED AT 250 WORDS)

An En Bloc Staining Protocol Improves The Preservation of Lamellar Bodies in Alveolar Type II Epithelial Cells for Transgenic Mice Expressing Modified Pulmonary Surfactant Protein B

1998 ◽  
Vol 4 (S2) ◽  
pp. 852-853
Author(s):  
C.-L. Na ◽  
D. C. Beck ◽  
J. S. Breslin ◽  
S. E. Wert ◽  
T. E. Weaver
Keyword(s):  
Pulmonary Surfactant ◽  
Surfactant Protein ◽  
Alveolar Type ◽  
Type Ii ◽  
Lamellar Bodies ◽  
En Bloc ◽  
Surfactant Protein B ◽  
Staining Protocol ◽  
Pulmonary Surfactant Protein B ◽  
Pulmonary Surfactant Protein

The extraction of lipids and phospholipids during dehydration and plastic embedding steps results in poor preservation of the phospholipid rich lamellar bodies (LB) in alveolar type II epithelial cells. To achieve better retention of phospholipids, we combined inflation fixation and an en bloc staining protocol using 4% aqueous uranyl acetate (UA), thereby improving the preservation of the LBs for both the wild type and transgenic mice expressing modified pulmonary surfactant protein B (SP-B; Akinbi et al., 1997).Lungs of 6-8 week-old mice were inflation fixed (Bunkingham and Weyder, 1981) with ice cold 2% paraformaldehye and 2% glutaraldehyde in 0.1 M sodium cacodylate buffer (SCB), pH 7.3, postfixed in fresh fixative at 4 °C overnight, incubated with 1% osmium tetroxide in 0.1 M SCB at room temperature for 2 hours, and stained en bloc with 4% aqueous UA overnight.

Degradation of surfactant lipids and surfactant protein A by alveolar macrophages in vitro

1995 ◽  
Vol 268 (5) ◽  
pp. L772-L780 ◽  
Author(s):  
J. R. Wright ◽  
D. C. Youmans
Keyword(s):  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Alveolar Type ◽  
Dependent Manner ◽  
Type Ii ◽  
Alveolar Type Ii Cell ◽  
Degradation Rates ◽  
Type Ii Cell

Pulmonary surfactant is synthesized and secreted into the airspaces by the alveolar type II cell. After it is secreted, surfactant undergoes a series of poorly understood transformations resulting in formation of a surface tension-reducing surface at the air-liquid interface. The by-products of the surface film and/or other products of surfactant metabolism are eventually cleared from the alveolar space. Both the alveolar type II cell and the macrophage are thought to be involved in surfactant clearance and have been shown to internalize surfactant lipid in vitro. The goal of the current investigation was to characterize further and to quantitate the role of the macrophage in surfactant clearance by investigating the uptake and metabolism of surfactant lipids and surfactant protein A (SP-A) by macrophages in vitro. SP-A enhanced the uptake of lipids by macrophages in a time-, temperature-, and concentration-dependent manner. In contrast, neither of the collagen-like proteins SP-D or C1q enhanced the uptake. Phosphatidylcholine was rapidly degraded by macrophages and the degradation occurred both in the presence and absence of SP-A. In addition, macrophages degrade SP-A by a process that is time- and temperature-dependent. These results and calculations of uptake and degradation rates suggest that macrophages may contribute significantly to the process of surfactant clearance.

scholarly journals Altered surfactant homeostasis and alveolar type II cell morphology in mice lacking surfactant protein D

1998 ◽  
Vol 95 (20) ◽  
pp. 11869-11874 ◽  
Author(s):  
C. Botas ◽  
F. Poulain ◽  
J. Akiyama ◽  
C. Brown ◽  
L. Allen ◽  
...  
Keyword(s):  
Cell Morphology ◽  
Surfactant Protein ◽  
Surfactant Protein D ◽  
Alveolar Type ◽  
Type Ii ◽  
Alveolar Type Ii Cell ◽  
Type Ii Cell

Pulmonary surfactant protein SP‐B promotes exocytosis of lamellar bodies in alveolar type II cells

2018 ◽  
Vol 32 (8) ◽  
pp. 4600-4611 ◽  
Author(s):  
Marta Martínez‐Calle ◽  
Bárbara Olmeda ◽  
Paul Dietl ◽  
Manfred Frick ◽  
Jesús Pérez‐Gil
Keyword(s):  
Pulmonary Surfactant ◽  
Surfactant Protein ◽  
Alveolar Type ◽  
Type Ii Cells ◽  
Type Ii ◽  
Lamellar Bodies ◽  
Alveolar Type Ii Cells ◽  
Pulmonary Surfactant Protein

Colocalization Of Markers Of The Endocytic And Biosynthetic Pathways In Multivesicular Bodies Of Murine Alveolar Type Ii Epithelial Cells

1999 ◽  
Vol 5 (S2) ◽  
pp. 1268-1269
Author(s):  
Cheng-Lun Na ◽  
Timothy E. Weaver
Keyword(s):  
Epithelial Cells ◽  
Pulmonary Surfactant ◽  
Protein A ◽  
Surfactant Protein ◽  
Alveolar Type ◽  
Multivesicular Bodies ◽  
Type Ii ◽  
Fetal Bovine ◽  
Endocytic Compartments ◽  
Pulmonary Surfactant Protein

Immunocytochemistry studies have established that multivesicular bodies (MVBs) in alveolar type II epithelial cells are important for processing pulmonary surfactant protein precursors (proSP; Voorhout et al., 1992 and 1993). Localization of pulmonary surfactant protein A (SP-A) gold and cationic ferritin to the MVBs demonstrated that MVBs also serve as endosomal/lysosomal compartments for recycling SPs (Williams et al., 1984, Ryan et al., 1989). However, these studies did not elucidate whether the biosynthesis of pulmonary SPs and endocytosis occur in the same MVBs. In this study, we used primary murine alveolar type II epithelial cell cultures as a model to determine if the biosynthetic and endocytic compartments colocalized in MVBs. The endocytic compartments of MVBs were identified using BSA gold conjugates, while the biosynthetic pathway was detected with antibodies directed against proSPs.Alveolar type II epithelial cells isolated from 6 weeks old C57B/6 mice were grown on Transwell cell inserts in the presence of 6 nm BSA gold conjugates (BSAG6) adjusted to final concentration of OD520 5.0 in DMEM, 25 mM HEPES, and 10% fetal bovine serum, pH 7.3, at 37 °C for 20 hours.

scholarly journals Contribution of alveolar type II cell‐derived cyclooxygenase‐2 to basal airway function, lung inflammation, and lung fibrosis

2015 ◽  
Vol 30 (1) ◽  
pp. 160-173 ◽  
Author(s):  
Jennifer Cheng ◽  
Ryan T. Dackor ◽  
J. Alyce Bradbury ◽  
g Li ◽  
Laura M. DeGraff ◽  
...  
Keyword(s):  
Lung Inflammation ◽  
Lung Fibrosis ◽  
Cyclooxygenase 2 ◽  
Alveolar Type ◽  
Type Ii ◽  
Alveolar Type Ii Cell ◽  
Airway Function ◽  
Type Ii Cell
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