PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27324153-2 2016 Bifunctional avidity of SP-A for pathogen-associated molecular patterns (PAMPs) such as lipid A and for dipalmitoylphosphatidylcholine (DPPC), the major component of surfactant membranes lining the air-liquid interface of the lung, ensures that the protein is poised for first-line interactions with inhaled pathogens. 1,2-Dipalmitoylphosphatidylcholine 104-134 surfactant protein A1 Homo sapiens 24-28 28719181-3 2017 SP-A binds to dipalmitoylphosphatidylcholine (DPPC), the major surfactant lipid component, but not phosphatidylinositol (PI), whereas SP-D shows the opposite preference. 1,2-Dipalmitoylphosphatidylcholine 14-44 surfactant protein A1 Homo sapiens 0-4 28719181-3 2017 SP-A binds to dipalmitoylphosphatidylcholine (DPPC), the major surfactant lipid component, but not phosphatidylinositol (PI), whereas SP-D shows the opposite preference. 1,2-Dipalmitoylphosphatidylcholine 46-50 surfactant protein A1 Homo sapiens 0-4 27324153-2 2016 Bifunctional avidity of SP-A for pathogen-associated molecular patterns (PAMPs) such as lipid A and for dipalmitoylphosphatidylcholine (DPPC), the major component of surfactant membranes lining the air-liquid interface of the lung, ensures that the protein is poised for first-line interactions with inhaled pathogens. 1,2-Dipalmitoylphosphatidylcholine 136-140 surfactant protein A1 Homo sapiens 24-28 27324153-3 2016 To improve our understanding of the motifs that are required for interactions with microbes and surfactant structures, we explored the role of the tyrosine-rich binding surface on the carbohydrate recognition domain of SP-A in the interaction with DPPC and lipid A using crystallography, site-directed mutagenesis, and molecular dynamics simulations. 1,2-Dipalmitoylphosphatidylcholine 248-252 surfactant protein A1 Homo sapiens 219-223 27324153-7 2016 These results suggest that the differential binding properties of SP-A favor transfer of the protein from surfactant DPPC to pathogen membranes containing appropriate lipid PAMPs to effect key host defense functions. 1,2-Dipalmitoylphosphatidylcholine 117-121 surfactant protein A1 Homo sapiens 66-70 20423923-8 2010 By contrast, SP-A shows features consistent with its preference for lipid ligands, including lipid A and the major surfactant lipid, dipalmitoylphosphatidylcholine. 1,2-Dipalmitoylphosphatidylcholine 133-163 surfactant protein A1 Homo sapiens 13-17 14507703-3 2003 Deuterium NMR was used to characterize the perturbation by SP-A, in the presence of 5 mM Ca(2+), of dipalmitoyl phosphatidylcholine (DPPC) properties in DPPC/egg-PG (7:3) bilayers. 1,2-Dipalmitoylphosphatidylcholine 100-131 surfactant protein A1 Homo sapiens 59-63 17693477-0 2007 Surfactant protein A forms extensive lattice-like structures on 1,2-dipalmitoylphosphatidylcholine/rough-lipopolysaccharide-mixed monolayers. 1,2-Dipalmitoylphosphatidylcholine 64-98 surfactant protein A1 Homo sapiens 0-20 17693477-1 2007 Due to the inhalation of airborne particles containing bacterial lipopolysaccharide (LPS), these molecules might incorporate into the 1,2-dipalmitoylphosphatidylcholine (DPPC)-rich monolayer and interact with surfactant protein A (SP-A), the major surfactant protein component involved in host defense. 1,2-Dipalmitoylphosphatidylcholine 170-174 surfactant protein A1 Homo sapiens 209-229 17693477-1 2007 Due to the inhalation of airborne particles containing bacterial lipopolysaccharide (LPS), these molecules might incorporate into the 1,2-dipalmitoylphosphatidylcholine (DPPC)-rich monolayer and interact with surfactant protein A (SP-A), the major surfactant protein component involved in host defense. 1,2-Dipalmitoylphosphatidylcholine 170-174 surfactant protein A1 Homo sapiens 231-235 17693477-2 2007 In this study, epifluorescence microscopy combined with a surface balance was used to examine the interaction of SP-A with mixed monolayers of DPPC/rough LPS (Re-LPS). 1,2-Dipalmitoylphosphatidylcholine 143-147 surfactant protein A1 Homo sapiens 113-117 17693477-6 2007 SP-A interacted strongly with Re-LPS and promoted the formation of DPPC-rich solid domains. 1,2-Dipalmitoylphosphatidylcholine 67-71 surfactant protein A1 Homo sapiens 0-4 17693477-7 2007 Fluorescently labeled Texas red-SP-A accumulated at the fluid-solid boundary regions and formed networks of interconnected filaments in the fluid phase of DPPC/Re-LPS monolayers in a Ca(2+)-independent manner. 1,2-Dipalmitoylphosphatidylcholine 155-159 surfactant protein A1 Homo sapiens 32-36 17128993-8 2006 Both SP-ADEL and SP-AINS mutants as well as wild-type SP-A bound to liposomes containing dipalmitoylphosphatidylcholine and galactosylceramide at equivalent levels, but the abilities of the mutants to induce phospholipid liposome aggregation were significantly less developed than that of the wild type. 1,2-Dipalmitoylphosphatidylcholine 89-119 surfactant protein A1 Homo sapiens 5-9 14507703-0 2003 Interaction of pulmonary surfactant protein SP-A with DPPC/egg-PG bilayers. 1,2-Dipalmitoylphosphatidylcholine 54-58 surfactant protein A1 Homo sapiens 44-48 14507703-3 2003 Deuterium NMR was used to characterize the perturbation by SP-A, in the presence of 5 mM Ca(2+), of dipalmitoyl phosphatidylcholine (DPPC) properties in DPPC/egg-PG (7:3) bilayers. 1,2-Dipalmitoylphosphatidylcholine 133-137 surfactant protein A1 Homo sapiens 59-63 14507703-3 2003 Deuterium NMR was used to characterize the perturbation by SP-A, in the presence of 5 mM Ca(2+), of dipalmitoyl phosphatidylcholine (DPPC) properties in DPPC/egg-PG (7:3) bilayers. 1,2-Dipalmitoylphosphatidylcholine 153-157 surfactant protein A1 Homo sapiens 59-63 14507703-4 2003 Effects of SP-A were uniformly distributed over the observed DPPC population. 1,2-Dipalmitoylphosphatidylcholine 61-65 surfactant protein A1 Homo sapiens 11-15 14507703-5 2003 SP-A reduced DPPC chain orientational order significantly in the gel phase but only slightly in the liquid-crystalline phase. 1,2-Dipalmitoylphosphatidylcholine 13-17 surfactant protein A1 Homo sapiens 0-4 14507703-6 2003 Quadrupole echo decay times for DPPC chain deuterons were sensitive to SP-A in the liquid-crystalline mixture but not in the gel phase. 1,2-Dipalmitoylphosphatidylcholine 32-36 surfactant protein A1 Homo sapiens 71-75 14507703-8 2003 The observed effects of SP-A on DPPC/egg-PG bilayer properties differ from those of the hydrophobic surfactant proteins SP-B and SP-C. 1,2-Dipalmitoylphosphatidylcholine 32-36 surfactant protein A1 Homo sapiens 24-28 11001826-3 2000 SP-A and SP-D are large hydrophilic proteins, which play an important role in host defense, whereas the small hydrophobic peptides SP-B and SP-C interact with DPPC to generate and maintain a surface-active film. 1,2-Dipalmitoylphosphatidylcholine 159-163 surfactant protein A1 Homo sapiens 0-4 11106621-10 2000 SP-A, combined with SP-B, induces a selective adsorption of DPPC from subphase vesicles into the surface film. 1,2-Dipalmitoylphosphatidylcholine 60-64 surfactant protein A1 Homo sapiens 0-4 11695915-0 2001 Thermal stability and DPPC/Ca2+ interactions of pulmonary surfactant SP-A from bulk-phase and monolayer IR spectroscopy. 1,2-Dipalmitoylphosphatidylcholine 22-26 surfactant protein A1 Homo sapiens 69-73 11695915-6 2001 Thermal denaturation of SP-A in the presence of either DPPC or Ca2+ ion reveals a sequence of events involving the initial melting of the collagen-like region, followed by formation of intermolecular extended forms. 1,2-Dipalmitoylphosphatidylcholine 55-59 surfactant protein A1 Homo sapiens 24-28 11695915-7 2001 Interestingly, these spectral changes were inhibited in the ternary system, showing that the combined presence of both DPPC and Ca2+ confers a remarkable thermal stability upon SP-A. 1,2-Dipalmitoylphosphatidylcholine 119-123 surfactant protein A1 Homo sapiens 177-181 11695915-9 2001 The IRRAS measurements indicated that incorporation of SP-A into preformed DPPC monolayers at a surface pressure of 10 mN/m induced a decrease in the average acyl chain tilt angle from 35 degrees to 28 degrees. 1,2-Dipalmitoylphosphatidylcholine 75-79 surfactant protein A1 Homo sapiens 55-59 10526225-4 1999 K(d)=5 microM is obtained for the complex between SP-A and dipalmitoylphosphatidylcholine (DPPC) liposomes. 1,2-Dipalmitoylphosphatidylcholine 59-89 surfactant protein A1 Homo sapiens 50-54 11030586-10 2000 We describe a model proposing that SP-A and SP-B create DPPC enriched domains which can readily be adsorbed to create a DPPC-rich monolayer at the interface. 1,2-Dipalmitoylphosphatidylcholine 56-60 surfactant protein A1 Homo sapiens 35-39 11030586-10 2000 We describe a model proposing that SP-A and SP-B create DPPC enriched domains which can readily be adsorbed to create a DPPC-rich monolayer at the interface. 1,2-Dipalmitoylphosphatidylcholine 120-124 surfactant protein A1 Homo sapiens 35-39 10526225-4 1999 K(d)=5 microM is obtained for the complex between SP-A and dipalmitoylphosphatidylcholine (DPPC) liposomes. 1,2-Dipalmitoylphosphatidylcholine 91-95 surfactant protein A1 Homo sapiens 50-54 10526225-6 1999 With palmitoyloleoylphosphatidylcholine (POPC), the complex formation proceeds at half the rate, compared to DPPC, leading to a lower final equilibrium level of SP-A lipid interaction. 1,2-Dipalmitoylphosphatidylcholine 109-113 surfactant protein A1 Homo sapiens 161-165 10353843-3 1999 SP-A binds to dipalmitoyl phosphatidylcholine (DPPC) and galactosylceramide (GalCer) and MBP-A binds to phosphatidylinositol (PI). 1,2-Dipalmitoylphosphatidylcholine 14-45 surfactant protein A1 Homo sapiens 0-4 10465757-2 1999 At pH 7.4, TR-SP-A expanded the pi-A isotherms of film of dipalmitoylphosphatidylcholine (DPPC). 1,2-Dipalmitoylphosphatidylcholine 58-88 surfactant protein A1 Homo sapiens 14-18 10465757-2 1999 At pH 7.4, TR-SP-A expanded the pi-A isotherms of film of dipalmitoylphosphatidylcholine (DPPC). 1,2-Dipalmitoylphosphatidylcholine 90-94 surfactant protein A1 Homo sapiens 14-18 10465757-4 1999 At pH 4.5, TR-SP-A expanded DPPC monolayers to a slightly lower extent than at pH 7.4. 1,2-Dipalmitoylphosphatidylcholine 28-32 surfactant protein A1 Homo sapiens 14-18 10465757-6 1999 Films of DPPC/dipalmitoylphosphatidylglycerol (DPPG) 7:3 mol/mol were somewhat expanded by TR-SP-A at pH 7.4. 1,2-Dipalmitoylphosphatidylcholine 9-13 surfactant protein A1 Homo sapiens 94-98 10353843-3 1999 SP-A binds to dipalmitoyl phosphatidylcholine (DPPC) and galactosylceramide (GalCer) and MBP-A binds to phosphatidylinositol (PI). 1,2-Dipalmitoylphosphatidylcholine 47-51 surfactant protein A1 Homo sapiens 0-4 8280055-6 1993 In addition, we demonstrated a shielding of the tryptophan fluorescence from quenching by acrylamide on interaction of porcine SP-A with DPPC, DPPG or LPC. 1,2-Dipalmitoylphosphatidylcholine 137-141 surfactant protein A1 Homo sapiens 127-131 8652605-1 1996 Pulmonary surfactant protein A (SP-A) augments the uptake of phospholipid liposomes containing dipalmitoylphosphatidylcholine (DPPC) by alveolar type II cells. 1,2-Dipalmitoylphosphatidylcholine 95-125 surfactant protein A1 Homo sapiens 0-30 8652605-1 1996 Pulmonary surfactant protein A (SP-A) augments the uptake of phospholipid liposomes containing dipalmitoylphosphatidylcholine (DPPC) by alveolar type II cells. 1,2-Dipalmitoylphosphatidylcholine 95-125 surfactant protein A1 Homo sapiens 32-36 8652605-1 1996 Pulmonary surfactant protein A (SP-A) augments the uptake of phospholipid liposomes containing dipalmitoylphosphatidylcholine (DPPC) by alveolar type II cells. 1,2-Dipalmitoylphosphatidylcholine 127-131 surfactant protein A1 Homo sapiens 0-30 8652605-1 1996 Pulmonary surfactant protein A (SP-A) augments the uptake of phospholipid liposomes containing dipalmitoylphosphatidylcholine (DPPC) by alveolar type II cells. 1,2-Dipalmitoylphosphatidylcholine 127-131 surfactant protein A1 Homo sapiens 32-36 8652605-4 1996 SP-A increased the amount of liposomes containing radiolabeled DPPC associated with type II cell plasma membrane by 4-fold compared to the control without SP-A when analyzed by sucrose density gradient centrifugation. 1,2-Dipalmitoylphosphatidylcholine 63-67 surfactant protein A1 Homo sapiens 0-4 8652605-7 1996 When type II cell plasma membrane and liposomes containing [14C]DPPC and [3H]triolein were coincubated with or without SP-A, analysis on sucrose density gradients revealed that the profiles of [14C]DPPC and [3H]triolein in each fraction were almost identical with or without SP-A, indicating that SP-A mediates the binding of liposomes to plasma membrane but not transfer of DPPC. 1,2-Dipalmitoylphosphatidylcholine 198-202 surfactant protein A1 Homo sapiens 119-123 8652605-7 1996 When type II cell plasma membrane and liposomes containing [14C]DPPC and [3H]triolein were coincubated with or without SP-A, analysis on sucrose density gradients revealed that the profiles of [14C]DPPC and [3H]triolein in each fraction were almost identical with or without SP-A, indicating that SP-A mediates the binding of liposomes to plasma membrane but not transfer of DPPC. 1,2-Dipalmitoylphosphatidylcholine 198-202 surfactant protein A1 Homo sapiens 119-123 7525589-9 1994 Antibody 1D6 completely blocked the binding of SP-A to dipalmitoylphosphatidylcholine and galactosylceramide and liposome aggregation. 1,2-Dipalmitoylphosphatidylcholine 55-85 surfactant protein A1 Homo sapiens 47-51 9548588-0 1998 Interaction of pulmonary surfactant protein A with dipalmitoylphosphatidylcholine and cholesterol at the air/water interface. 1,2-Dipalmitoylphosphatidylcholine 51-81 surfactant protein A1 Homo sapiens 15-45 9548588-1 1998 Interaction of pulmonary surfactant protein A (SP-A) with pure and binary mixed dipalmitoylphosphatidylcholine (DPPC) and cholesterol (3.5 wt%) at the air/saline, 1.5 mM CaCl2 interface was investigated using a rhomboid surface balance at 37 degrees C. Surface tension-area isotherms were measured to access the surface active properties of the monolayers. 1,2-Dipalmitoylphosphatidylcholine 80-110 surfactant protein A1 Homo sapiens 47-51 9548588-1 1998 Interaction of pulmonary surfactant protein A (SP-A) with pure and binary mixed dipalmitoylphosphatidylcholine (DPPC) and cholesterol (3.5 wt%) at the air/saline, 1.5 mM CaCl2 interface was investigated using a rhomboid surface balance at 37 degrees C. Surface tension-area isotherms were measured to access the surface active properties of the monolayers. 1,2-Dipalmitoylphosphatidylcholine 112-116 surfactant protein A1 Homo sapiens 47-51 9548588-3 1998 The results showed that SP-A can interact with the polar head groups of DPPC monolayers and aggregate DPPC molecules. 1,2-Dipalmitoylphosphatidylcholine 72-76 surfactant protein A1 Homo sapiens 24-28 9548588-3 1998 The results showed that SP-A can interact with the polar head groups of DPPC monolayers and aggregate DPPC molecules. 1,2-Dipalmitoylphosphatidylcholine 102-106 surfactant protein A1 Homo sapiens 24-28 9548588-4 1998 SP-A decreased the surface area reduction required for DPPC monolayers to achieve near zero surface tension from 30 to 25% of the area at equilibrium. 1,2-Dipalmitoylphosphatidylcholine 55-59 surfactant protein A1 Homo sapiens 0-4 9548588-8 1998 Although SP-A could not promote the squeeze-out of cholesterol from homogeneous mixed monolayers, it facilitated that of cholesterol domains especially when SP-A had first interacted with DPPC. 1,2-Dipalmitoylphosphatidylcholine 188-192 surfactant protein A1 Homo sapiens 9-13 9548588-9 1998 These results indicate that pulmonary surfactant protein A facilitates the squeeze-out of cholesterol domains from mixed monolayers by condensing DPPC and limiting lateral interactions of DPPC with cholesterol domains. 1,2-Dipalmitoylphosphatidylcholine 146-150 surfactant protein A1 Homo sapiens 28-58 9548588-9 1998 These results indicate that pulmonary surfactant protein A facilitates the squeeze-out of cholesterol domains from mixed monolayers by condensing DPPC and limiting lateral interactions of DPPC with cholesterol domains. 1,2-Dipalmitoylphosphatidylcholine 188-192 surfactant protein A1 Homo sapiens 28-58 8652605-8 1996 SP-A increased the association of liposomes containing DPPC with the membrane by 2-fold more than that containing 1-palmitoyl-2-linoleoyl-phosphatidylcholine (PLPC). 1,2-Dipalmitoylphosphatidylcholine 55-59 surfactant protein A1 Homo sapiens 0-4 8652605-9 1996 SP-A induced aggregation of phospholipid liposomes containing PLPC as well as those containing DPPC, but the final turbidity of DPPC liposomes aggregated by SP-A was only by 15% greater than that of PLPC liposomes. 1,2-Dipalmitoylphosphatidylcholine 95-99 surfactant protein A1 Homo sapiens 0-4 8652605-9 1996 SP-A induced aggregation of phospholipid liposomes containing PLPC as well as those containing DPPC, but the final turbidity of DPPC liposomes aggregated by SP-A was only by 15% greater than that of PLPC liposomes. 1,2-Dipalmitoylphosphatidylcholine 128-132 surfactant protein A1 Homo sapiens 157-161 8280055-8 1993 In the case of human SP-A, shielding was only observed on interaction with DPPC. 1,2-Dipalmitoylphosphatidylcholine 75-79 surfactant protein A1 Homo sapiens 21-25 8280055-9 1993 From the intrinsic fluorescence measurements as well as from the quenching experiments, we concluded that the interaction of some phospholipid vesicles with SP-A produces a conformational change on the protein molecule and that the interaction of SP-A with DPPC is stronger than with other phospholipids. 1,2-Dipalmitoylphosphatidylcholine 257-261 surfactant protein A1 Homo sapiens 247-251 8280055-11 1993 Physiological ionic strength was found to be required for the interaction of SP-A with negatively charged vesicles of either DPPG or DPPC/DPPG (7:3, w/w). 1,2-Dipalmitoylphosphatidylcholine 133-137 surfactant protein A1 Homo sapiens 77-81 8280055-13 1993 The increase in intrinsic fluorescence of SP-A in the presence of DPPC vesicles was much stronger when the vesicles were in the gel state than when they were in the liquid-crystalline state. 1,2-Dipalmitoylphosphatidylcholine 66-70 surfactant protein A1 Homo sapiens 42-46 8368329-2 1993 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. 1,2-Dipalmitoylphosphatidylcholine 49-79 surfactant protein A1 Homo sapiens 0-4 8368329-2 1993 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. 1,2-Dipalmitoylphosphatidylcholine 81-85 surfactant protein A1 Homo sapiens 0-4 8368329-2 1993 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. 1,2-Dipalmitoylphosphatidylcholine 188-192 surfactant protein A1 Homo sapiens 0-4 8368329-2 1993 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. 1,2-Dipalmitoylphosphatidylcholine 188-192 surfactant protein A1 Homo sapiens 0-4 8368329-3 1993 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. 1,2-Dipalmitoylphosphatidylcholine 111-115 surfactant protein A1 Homo sapiens 184-188 8368329-7 1993 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. 1,2-Dipalmitoylphosphatidylcholine 71-75 surfactant protein A1 Homo sapiens 143-147 8368329-7 1993 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. 1,2-Dipalmitoylphosphatidylcholine 71-75 surfactant protein A1 Homo sapiens 143-147 1306239-6 1992 We revealed that SP-A binds specifically to dipalmitoylphosphatidylcholine and galactose-ceramide and asialo GM2, while SP-D binds specifically to phosphatidylinositol and glucose-ceramide. 1,2-Dipalmitoylphosphatidylcholine 44-74 surfactant protein A1 Homo sapiens 17-21