scholarly journals Rat Mannose-Binding Protein A Binds CD14

2001 ◽  
Vol 69 (3) ◽  
pp. 1587-1592 ◽  
Author(s):  
Hirofumi Chiba ◽  
Hitomi Sano ◽  
Daisuke Iwaki ◽  
Seiji Murakami ◽  
Hiroaki Mitsuzawa ◽  
...  
Keyword(s):  
Lipid A ◽  
Binding Protein ◽  
Protein A ◽  
Cellular Responses ◽  
Dependent Manner ◽  
Soluble Cd14 ◽  
Concentration Dependent Manner ◽  
E Coli ◽  
Mannose Binding Protein ◽  
Mannose Binding

ABSTRACT Lipopolysaccharide (LPS) has been known to induce inflammation by interacting with CD14, which serves as a receptor for LPS. Mannose-binding protein (MBP) belongs to the collectin subgroup of the C-type lectin superfamily, along with surfactant proteins SP-A and SP-D. We have recently demonstrated that SP-A modulates LPS-induced cellular responses by interaction with CD14 (H. Sano, H. Sohma, T. Muta, S. Nomura, D. R. Voelker, and Y. Kuroki, J. Immunol. 163:387–395, 2000) and that SP-D also interacts with CD14 (H. Sano, H. Chiba, D. Iwaki, H. Sohma, D. R. Voelker, and Y. Kuroki, J. Biol. Chem. 275:22442–22451, 2000). In this study, we examined whether MBP, a collectin highly homologous to SP-A and SP-D, could bind CD14. Recombinant rat MBP-A bound recombinant human soluble CD14 in a concentration-dependent manner. Its binding was not inhibited in the presence of excess mannose or EDTA. MBP-A bound deglycosylated CD14 treated with N-glycosidase F, neuraminidase, and O-glycosidase, indicating that MBP-A interacts with the peptide portion of CD14. Since LPS was also a ligand for the collectins, we compared the characteristics of binding of MBP-A to LPS with those of binding to CD14. MBP-A bound to lipid A fromSalmonella enterica serovar Minnesota and rough LPS (S. enterica serovar Minnesota Re595 and Escherichia coli J5, Rc), but not to smooth LPS (E. coli O26:B6 and O111:B4). Unlike CD14 binding, EDTA and excess mannose attenuated the binding of MBP-A to rough LPS. From these results, we conclude that CD14 is a novel ligand for MBP-A and that MBP-A utilizes a different mechanism for CD14 recognition from that for LPS.

Introduction of Mannose Binding Protein-Type Phosphatidylinositol Recognition into Pulmonary Surfactant Protein A†

Biochemistry ◽  
1999 ◽  
Vol 38 (22) ◽  
pp. 7321-7331 ◽  
Author(s):  
Hirofumi Chiba ◽  
Hitomi Sano ◽  
Masaki Saitoh ◽  
Hitoshi Sohma ◽  
Dennis R. Voelker ◽  
...  
Keyword(s):  
Pulmonary Surfactant ◽  
Binding Protein ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Mannose Binding Protein ◽  
Mannose Binding ◽  
Pulmonary Surfactant Protein

The human ortholog of rhesus mannose-binding protein-A gene is an expressed pseudogene that localizes to Chromosome 10

1998 ◽  
Vol 9 (3) ◽  
pp. 246-249 ◽  
Author(s):  
Ning Guo ◽  
Tirsit Mogues ◽  
Stanislawa Weremowicz ◽  
Cynthia C. Morton ◽  
Kedarnath N. Sastry
Keyword(s):  
Binding Protein ◽  
Protein A ◽  
Chromosome 10 ◽  
Mannose Binding Protein ◽  
Mannose Binding ◽  
Human Ortholog

scholarly journals A human mannose-binding protein is an acute-phase reactant that shares sequence homology with other vertebrate lectins.

1988 ◽  
Vol 167 (3) ◽  
pp. 1034-1046 ◽  
Author(s):  
R A Ezekowitz ◽  
L E Day ◽  
G A Herman
Keyword(s):  
Acute Phase ◽  
Disulfide Bonds ◽  
Signal Sequence ◽  
Binding Protein ◽  
Protein A ◽  
Coelomic Fluid ◽  
Carbohydrate Binding ◽  
Cdna Clones ◽  
Mannose Binding Protein ◽  
Mannose Binding

Mannose-binding proteins have been isolated from the liver of rats and humans and subsequently been found in the serum of rats, rabbits, and humans. We report the isolation of cDNA clones isolated from a human liver cDNA library that encodes a human mannose-binding protein. The primary structure has three domains: (a) an NH2-terminal cysteine-rich segment of 19 amino acids which appears to be involved in the formation of interchain disulfide bonds that would stabilize multimeric forms of the protein; (b) a collagen-like region consisting of 19 repeats of the sequence Gly-x-y; and (c) a COOH-terminal putative carbohydrate-binding domain consisting of 148 residues. This human mannose-binding protein bears 51% overall homology (allowing three gaps) with a rat mannose-binding protein C and 48% homology (allowing seven gaps) with a rat mannose-binding protein A. Like these homologous rat proteins, the human mannose-binding protein COOH-terminal sequences are homologous to the carbohydrate recognition portion of several other lectin-like proteins including mammalian hepatic receptors, an insect-soluble hemolymph, and a sea urchin lectin found in coelomic fluid. The apoproteins of dog and human surfactant and the human lymphocyte IgE Ec receptor have not been shown to have lectin-like properties, yet by homology are members of this family of lectin-like proteins. The human mannose-binding protein is preceded by a typical hydrophobic signal sequence and its hepatic secretion is induced as part of the acute-phase response consistent with its probable role in host defense.

Oxygen modulates the differentiation of human fetal lung in vitro and its responsiveness to cAMP

1993 ◽  
Vol 264 (5) ◽  
pp. L465-L474 ◽  
Author(s):  
M. J. Acarregui ◽  
J. M. Snyder ◽  
C. R. Mendelson
Keyword(s):  
Gene Expression ◽  
Atmospheric Oxygen ◽  
Protein A ◽  
Morphological Differentiation ◽  
Fetal Lung ◽  
Morphological Development ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Human Fetal Lung

Previously, it was found that lung explants from mid-trimester human abortuses differentiate spontaneously in organ culture in serum-free defined medium in an atmosphere of 95% air-5% CO2. Dibutyryl adenosine 3',5'-cyclic monophosphate (DBcAMP) treatment of human fetal lung in culture increases the rate of morphological differentiation and enhances expression of the surfactant protein A (SP-A) gene. To begin to define the factors responsible for this accelerated in vitro differentiation, we analyzed the effects of atmospheric oxygen on the morphological and biochemical development of human fetal lung in culture and on responsiveness of the cultured tissue to DBcAMP. We found that when lung explants were maintained in an atmosphere containing 1% oxygen they failed to differentiate spontaneously and no induction of SP-A gene expression was apparent. Furthermore, at 1% oxygen, DBcAMP had no effect to stimulate morphological differentiation or SP-A gene expression. When lung tissues that had been maintained for 5 days in 1% oxygen were transferred to an environment containing 20% oxygen, there was rapid morphological development and induction of SP-A gene expression. The effects on morphological development were manifest within 24 h of transfer to the 20% oxygen environment; within 72 h, a marked stimulatory effect of DBcAMP on SP-A gene expression also was observed. Our findings further suggest that the effects of oxygen on the levels of SP-A and SP-A mRNA are concentration dependent. Interestingly, the inductive effects of DBcAMP on SP-A gene expression were apparent only at oxygen concentrations > or = 10%. Morphological differentiation of the cultured human fetal lung tissue also was influenced by oxygen in a concentration-dependent manner. These findings suggest that oxygen plays an important permissive role in the spontaneous differentiation of human fetal lung in vitro.

Isolation and characterization of the major mannose-binding protein in chicken serum

Biochemistry ◽  
1985 ◽  
Vol 24 (21) ◽  
pp. 5932-5938 ◽  
Author(s):  
Ke Yi Wang ◽  
Theresa B. Kuhlenschmidt ◽  
Y. C. Lee
Keyword(s):  
Binding Protein ◽  
Chicken Serum ◽  
Isolation And Characterization ◽  
Mannose Binding Protein ◽  
Mannose Binding

Agaricus bisporus mannose binding protein is not an agglutinating protein

2019 ◽  
Vol 519 (4) ◽  
pp. 773-776 ◽  
Author(s):  
Najwa Nabila ◽  
Vincencius F. Meidianto ◽  
Raymond R. Tjandrawinata ◽  
Heni Rachmawati ◽  
Wangsa T. Ismaya
Keyword(s):  
Agaricus Bisporus ◽  
Binding Protein ◽  
Mannose Binding Protein ◽  
Mannose Binding
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