Genomic and molecular characterization of bovine surfactant protein D (SP-D)1

2004 ◽  
Vol 41 (4) ◽  
pp. 369-376 ◽  
Author(s):  
M GJERSTORFF ◽  
J MADSEN ◽  
C BENDIXEN ◽  
U HOLMSKOV ◽  
S HANSEN
Keyword(s):  
Molecular Characterization ◽  
Surfactant Protein ◽  
Surfactant Protein D

scholarly journals Identification and Characterization of a Novel Interaction between Pulmonary Surfactant Protein D and Decorin

2003 ◽  
Vol 278 (28) ◽  
pp. 25678-25687 ◽  
Author(s):  
Jeya Nadesalingam ◽  
Andrés López Bernal ◽  
Alister W. Dodds ◽  
Antony C. Willis ◽  
David J. Mahoney ◽  
...  
Keyword(s):  
Pulmonary Surfactant ◽  
Surfactant Protein ◽  
Surfactant Protein D ◽  
Identification And Characterization ◽  
Pulmonary Surfactant Protein

Bovine conglutinin (BC) mRNA expressed in liver: cloning and characterization of the BC cDNA reveals strong homology to surfactant protein-D

Gene ◽  
1994 ◽  
Vol 141 (2) ◽  
pp. 277-281 ◽  
Author(s):  
Louis S Liou ◽  
Rajeswari Sastry ◽  
Kevan L Hartshorn ◽  
Young Moo Lee ◽  
Thomas B Okarma ◽  
...  
Keyword(s):  
Surfactant Protein ◽  
Surfactant Protein D ◽  
Strong Homology

Characterization of pulmonary surfactant protein D: its copurification with lipids

1991 ◽  
Vol 1086 (2) ◽  
pp. 185-190 ◽  
Author(s):  
Yoshio Kuroki ◽  
Masanori Shiratori ◽  
Yoshinori Ogasawara ◽  
Akihiro Tsuzuki ◽  
Toyoaki Akino
Keyword(s):  
Pulmonary Surfactant ◽  
Surfactant Protein ◽  
Surfactant Protein D ◽  
Pulmonary Surfactant Protein

scholarly journals Structural characterization of human and bovine lung surfactant protein D

1999 ◽  
Vol 343 (3) ◽  
pp. 645-652 ◽  
Author(s):  
Rikke LETH-LARSEN ◽  
Uffe HOLMSKOV ◽  
Peter HØJRUP
Keyword(s):  
Lung Surfactant ◽  
Surfactant Protein ◽  
Glycosylation Site ◽  
Surfactant Protein D ◽  
Post Translational Modifications ◽  
Single Polypeptide Chain ◽  
Lysine Residues ◽  
Lung Surfactant Protein ◽  
Single Polypeptide

Human and bovine surfactant proteins D (SP-D) were purified from late amniotic fluid and bronchioalveolar lavage on the basis of its Ca2+-dependent affinity for maltose. The molecular mass of a trimeric subunit was determined by matrix-assisted laser desorption ionization MS to lie in the range 115-125 kDa for human SP-D and 110-123 kDa for bovine SP-D. A single polypeptide chain was determined at 37-41 and 36-40 kDa for the human and bovine species respectively. The major parts of the primary structures of both SP-D molecules were determined by a combination of MS and Edman degradation. The heterogeneity in SP-D was caused mainly by a high number of post-translational modifications in the collagen-like region. Proline and lysine residues were partly hydroxylated and lysine residues were further O-glycosylated with the disaccharide galactose-glucose. A partly occupied N-linked glycosylation site was characterized in human SP-D. The carbohydrate was determined as a complex type bi-antennary structure, with a small content of mono-antennary and tri-antennary structures. No sialic acid residues were present on the glycan, but some had an attached fucose and/or an N-acetylglucosamine residue linked to the core. Bovine SP-D was determined as having a similar structure.

scholarly journals Distinctive anti-influenza properties of recombinant collectin 43

2002 ◽  
Vol 366 (1) ◽  
pp. 87-96 ◽  
Author(s):  
Kevan L. HARTSHORN ◽  
Uffe HOLMSKOV ◽  
Soren HANSEN ◽  
Pengnian ZHANG ◽  
Joseph MESCHI ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Influenza A ◽  
Antimicrobial Properties ◽  
Surfactant Protein ◽  
Surfactant Protein D ◽  
Bacterial Aggregation ◽  
Structural And Functional Properties ◽  
Antiviral Activities ◽  
Innate Defence

Collectins play important roles in innate defence against viral, fungal and bacterial pathogens. CL-43, a bovine serum collectin, which appears to have evolutionarily evolved from surfactant protein D (SP-D), shows unique structural and functional properties. In the present study, we describe the initial characterization of a recombinant CL-43 expressed in mammalian cells. Like natural CL-43, the recombinant is secreted as trimeric forms that show a preference for mannose and N-acetyl mannosamine. The natural and recombinant proteins have significantly higher haemagglutination-inhibiting activity against influenza A virus (IAV) than recombinant trimeric forms of SP-D. In contrast with the more highly multimerized forms of SP-D, namely conglutinin or mannose-binding lectin, CL-43 did not induce viral or bacterial aggregation and did not enhance IAV-induced neutrophil H2O2 generation. Like SP-D, CL-43 also strongly enhanced neutrophil uptake of IAV. However, the mechanism of this enhanced internalization is different from that of SP-D in that it did not require viral aggregation. These studies establish that the trimeric structure of CL-43 is specified by its primary sequence and indicate that this naturally occurring trimeric collectin has unique antiviral activities. These findings could facilitate the development of recombinant collectins with novel antimicrobial properties.

1446: Molecular Characterization of Cyclooxygenase-2 in a Stimulated Prostate Stroma Cells

2006 ◽  
Vol 175 (4S) ◽  
pp. 467-467
Author(s):  
Victor K. Lin ◽  
Shih-Ya Wang ◽  
Claus G. Roehrbom
Keyword(s):  
Molecular Characterization ◽  
Cyclooxygenase 2 ◽  
Prostate Stroma
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