Journal Article10.1021/BI990353E
Introduction of mannose binding protein-type phosphatidylinositol recognition into pulmonary surfactant protein A.
Hirofumi Chiba,Hitomi Sano,Masaki Saitoh,Hitoshi Sohma,Dennis R. Voelker,Toyoaki Akino,Yoshio Kuroki +6 more
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TL;DR: It is demonstrated that the amino acid residues 174-194 of SP-A and the corresponding region of MBP-A are critical forSP-A-type II cell interaction and Ca2+-dependent lipid binding of collectins.
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Abstract: Pulmonary surfactant protein A (SP-A) and mannose-binding protein A (MBP-A) are collectins in the C-type lectin superfamily. These collectins exhibit unique lipid binding properties. SP-A binds to dipalmitoyl phosphatidylcholine (DPPC) and galactosylceramide (GalCer) and MBP-A binds to phosphatidylinositol (PI). SP-A also interacts with alveolar type II cells. Monoclonal antibodies (mAbs PE10 and PC6) that recognize human SP-A inhibit the interactions of SP-A with lipids and alveolar type II cells. We mapped the epitopes for anti-human SP-A mAbs by a phage display peptide library. Phage selected by mAbs displayed the consensus peptide sequences that are nearly identical to 184TPVNYTNWYRG194 of human SP-A. The synthetic peptide GTPVNYTNWYRG completely blocked the binding of mAbs to human SP-A. Chimeric proteins were generated in which the rat SP-A region Thr174-Gly194 or the human SP-A region Ser174-Gly194 was replaced with the MBP-A region Thr164-Asp184 (rat ama4 or hu ama4, respectively). The mAbs failed to bind hu ama4. Rat ama4 bound to an affinity matrix on mannose-sepharose but lost all of the SP-A functions except carbohydrate binding and Ca2+-independent GalCer binding. Strikingly, the rat ama4 chimera acquired the PI binding property that MBP-A exhibits. This study demonstrates that the amino acid residues 174-194 of SP-A and the corresponding region of MBP-A are critical for SP-A-type II cell interaction and Ca2+-dependent lipid binding of collectins.
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Citations
Surfactant Protein A Directly Interacts with TLR4 and MD-2 and Regulates Inflammatory Cellular Response: IMPORTANCE OF SUPRATRIMERIC OLIGOMERIZATION *
Chieko Yamada,Hitomi Sano,Takeyuki Shimizu,Hiroaki Mitsuzawa,Chiaki Nishitani,Tetsuo Himi,Yoshio Kuroki +6 more
TL;DR: The direct interaction betweenSP-A and TLR4/MD-2 is demonstrated for the first time and the importance of supratrimeric oligomerization in the immunomodulatory function of SP-A is suggested.
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Pulmonary Collectins Enhance Phagocytosis of Mycobacterium avium through Increased Activity of Mannose Receptor
Kazumi Kudo,Hitomi Sano,Hiroki Takahashi,Koji Kuronuma,Shin-ichi Yokota,Nobuhiro Fujii,Kenichi Shimada,Ikuya Yano,Yoshio Kumazawa,Dennis R. Voelker,Shosaku Abe,Yoshio Kuroki +11 more
TL;DR: Analysis by confocal microscopy and flow cytometry revealed that the lung collectins up-regulated the cell surface expression of mannose receptor on monocyte-derived macrophages, providing compelling evidence that SP-A and SP-D enhance mannosed receptor-mediated phagocytosis of M. avium.
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Effects of ageing and smoking on SP-A and SP-D levels in bronchoalveolar lavage fluid
TL;DR: Surfactant protein-A may decrease with age alone or due to the cumulative effects of long-term smoking and development of emphysema, while surfactantprotein-D decreases due to long- term smoking.
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Linkage of neutrophil serine proteases and decreased surfactant protein-A (SP-A) levels in inflammatory lung disease
TL;DR: The findings strongly suggest that the neutrophil serine proteases cathepsin G and/or elastase and/ or proteinase-3 contribute to degradation of SP-A and thereby diminish innate pulmonary antimicrobial defence.
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Domains of surfactant protein A that affect protein oligomerization, lipid structure and surface tension.
Nades Palaniyar,Machiko Ikegami,Thomas R. Korfhagen,Jeffrey A. Whitsett,Francis X. McCormack +4 more
TL;DR: This review focuses on the structural importance of each domain of SP-A in the functions of protein oligomerization, the structural organization of lipids and the surface-active properties of surfactant, with an emphasis on ultrastructural analyses.
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References
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TL;DR: The entire structure of the mannose-binding proteins is homologous to dog pulmonary surfactant apoprotein.
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Interaction of C1q receptor with lung surfactant protein A.
TL;DR: The results indicate that interaction of SP‐A with U937 cells triggers the expression of an intracellular pool of C1qR, which is specific, saturable, salt dependent and is inhibited by purified C 1qR and byC1q.
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