TY - JOUR
T1 - Surfactant proteins SP-A and SP-D in human health and disease
AU - Kishore, Uday
AU - Bernal, Andrés López
AU - Kamran, Mohammed F.
AU - Saxena, Shweta
AU - Singh, Mamta
AU - Sarma, P. Usha
AU - Madan, Taruna
AU - Chakraborty, Trinad
PY - 2005
Y1 - 2005
N2 - Surfactant proteins A (SP-A) and D (SP-D) are lung surfactant-associated hydrophilic proteins that have been implicated in surfactant homeostasis and pulmonary innate immunity. They are collagen-containing C-type (calcium-dependent) lectins, called collectins, and are structurally similar to mannose-binding protein of the lectin pathway of the complement system. Being carbohydrate pattern-recognition molecules, they recognize a broad spectrum of pathogens and allergens via the lectin domain, with subsequent activation of immune cells via the collagen region, thus offering protection against infection and allergenic challenge. SP-A and SP-D have been shown to be involved in viral neutralization, clearance of bacteria, fungi, and apoptotic and necrotic cells, down-regulation of allergic reaction, and resolution of inflammation. Studies on single-nucleotide polymorphism, protein levels in broncho-alveolar lavage, and gene knock-out mice have clearly indicated an association between SP-A and SP-D and a range of pulmonary diseases. In addition, recent studies using murine models of allergy and infection have raised the possibility that the recombinant forms of SP-A and SP-D may have therapeutic potential in controlling pulmonary infection, inflammation, and allergies in humans.
AB - Surfactant proteins A (SP-A) and D (SP-D) are lung surfactant-associated hydrophilic proteins that have been implicated in surfactant homeostasis and pulmonary innate immunity. They are collagen-containing C-type (calcium-dependent) lectins, called collectins, and are structurally similar to mannose-binding protein of the lectin pathway of the complement system. Being carbohydrate pattern-recognition molecules, they recognize a broad spectrum of pathogens and allergens via the lectin domain, with subsequent activation of immune cells via the collagen region, thus offering protection against infection and allergenic challenge. SP-A and SP-D have been shown to be involved in viral neutralization, clearance of bacteria, fungi, and apoptotic and necrotic cells, down-regulation of allergic reaction, and resolution of inflammation. Studies on single-nucleotide polymorphism, protein levels in broncho-alveolar lavage, and gene knock-out mice have clearly indicated an association between SP-A and SP-D and a range of pulmonary diseases. In addition, recent studies using murine models of allergy and infection have raised the possibility that the recombinant forms of SP-A and SP-D may have therapeutic potential in controlling pulmonary infection, inflammation, and allergies in humans.
KW - Allergy
KW - Disease
KW - Innate immunity
KW - Lung
KW - Pathogen
KW - Pregnancy
KW - Surfactant
UR - http://www.scopus.com/inward/record.url?scp=30944433587&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=30944433587&partnerID=8YFLogxK
M3 - Review article
C2 - 16314824
AN - SCOPUS:30944433587
SN - 0004-069X
VL - 53
SP - 399
EP - 417
JO - Archivum Immunologiae et Therapiae Experimentalis
JF - Archivum Immunologiae et Therapiae Experimentalis
IS - 5
ER -