title: Surfactant proteins in the digestive tract, mesentery, and other organs: evolutionary significance.
abstract: For years, the so-called surfactant proteins (SPs) that were discovered in the phospholipid-rich material designated pulmonary surfactant, were considered to be lung-specific. The fact that surfactant-like materials composed of phospholipids are secreted by a number of other organs recently prompted several groups to search for SP expression in these organs also. The hydrophilic proteins SP-A and SP-D and their transcripts have been found in a number of tissues, including gastric and intestinal mucosae, mesothelial tissues (mesentery, peritoneum, and pleura), synovial cells, Eustachian tube and sinus, and possibly in salivary glands, pancreas, and urinary tract. By contrast, the hydrophobic proteins SP-B and SP-C actually appear to be expressed in lung epithelium only. SP-A and SP-D belong to the innate defence system against pathogens and play a role as opsonins for facilitating phagocytosis. Their expression appears as a general feature of organs exposed to pathogens because they present an interface with the external milieu. Although this function has thus far been investigated in the lung only through the gene-targeting approach, increased expression of SP-A in the infected middle ear and of SP-D in the Helicobacter-infected antrum argues for such a function also in other organs. In organs that are not exposed to external pathogens, their role is likely to exert anti-inflammatory and immunomodulatory functions, as suggested by increased SP-A immunoreactivity in rheumatoid disease. SP-A and SP-B have been found in association with phospholipids in the lung of all air-breathing vertebrates, including the most primitive forms represented by lungfish, which implies that the surfactant system had a single evolutionary origin. Immunochemical proximity of the proteins among vertebrates indicates considerable conservation during evolution. Moreover, the finding of an SP-A-like protein in intestine and swim bladder of actinopterygian fish implies that the ancestral form of the protein was already present before the emergence of lung structures.
authors.affiliation: INSERM Unité 319, Université Paris 7-Denis Diderot, 2 place Jussieu, 75251 Cedex 05, Paris, France. bourbon@paris7.jussieu.fr
authors.forename: J R
authors.initials: JR
authors.lastname: Bourbon
authors.forename: B
authors.initials: B
authors.lastname: Chailley-Heu
mesh_terms: D000818:Animals; D004064:Digestive System / Q000378:metabolism*; D019143:Evolution, Molecular; D006023:Glycoproteins / Q000235:genetics / Q000378:metabolism*; D008643:Mesentery / Q000378:metabolism*; D011510:Proteolipids / Q000235:genetics / Q000378:metabolism*; D037662:Pulmonary Surfactant-Associated Protein A; D037663:Pulmonary Surfactant-Associated Protein D; D037661:Pulmonary Surfactant-Associated Proteins; D011663:Pulmonary Surfactants / Q000235:genetics / Q000378:metabolism*
chemical_list: D006023:Glycoproteins; D011510:Proteolipids; D037662:Pulmonary Surfactant-Associated Protein A; D037663:Pulmonary Surfactant-Associated Protein D; D037661:Pulmonary Surfactant-Associated Proteins; D011663:Pulmonary Surfactants