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Surfactant protein A is an innate immune system collectin.
Our findings further characterize the signal transduction pathways that control surfactant protein gene expression.
DMBT1 has been shown to interact with Surfactant protein D.
Surfactant protein B is an essential lipid-associated protein found in lung surfactant.
Surfactant proteins C are a family of related pulmonary surfactant proteins.
Pulmonary surfactant protein D (SP-D), has an important role in acting as a lung host defence protein.
The role of Surfactant protein A (or SP-A) in childbirth is indicated in studies with mice.
For example, Surfactant protein C regulatory elements have been used extensively to drive high level expression of transgenes in the lung [ 1, 2, 3, 4].
Surfactant protein A (SP-A) is a protein of 248 amino acids usually found in large oligomeric structures.
She has extensively worked on Aspergillosis and lung surfactant proteins and now her research is more focussed on role of innate immunity in host-pathogen interactions.
For example, a mutation in Surfactant protein C (SP-C) has been found to exist in some families with a history of pulmonary fibrosis.
FDC-SP is an amphipathic molecule, similar to surfactant proteins A and D, which are thought to be involved in the innate immune system of the lung.
In molecular biology, Pulmonary surfactant protein D (SP-D) is a protein domain predominantly found in lung surfactant.
The presence of Surfactant Protein A seemed to trigger an inflammatory response in the uterus of the mice, but later studies found an anti-inflammatory response in humans.
Taruna M. Gupta is a prolific author and has published more than 40 peer reviewed journal articles where most of articles have covered the research over fungal aspergilosis and lung surfactant proteins.
Pulmonary surfactant-associated protein A2 (PSP-A) also known as surfactant protein A2 (SP-A2) is a protein that in humans is encoded by the SFTPA2 gene.
Using specific monoclonal antibodies for Surfactant protein A, the protein can be detected in lung alveolar type II pneumocytes, Clara cells, and alveolar macrophages, but no extrapulmonary SP-A immunoreactivity was observed.
In the 1990s, while at Washington, where he was chairman of the department of pediatrics, Dr. Colten guided a team of scientists in identifying the gene responsible for producing a protein, pulmonary surfactant protein B, needed to ensure normal function of the lungs.
Although the role of PG and PI are not clear, they appear to interact with hydrophobic surfactant proteins SP-B and SP-C to prevent the irreversible removal of the phospholipids from the surfactant film during alveolar compression and collapse for rapid reinsertion upon re-expansion.