Hevea latex lectin binding protein in C-serum as an anti-latex coagulating factor and its role in a proposed new model for latex coagulation

2008 ◽  
Vol 69 (3) ◽  
pp. 656-662 ◽  
Author(s):  
Rapepun Wititsuwannakul ◽  
Piyaporn Pasitkul ◽  
Pattavuth Jewtragoon ◽  
Dhirayos Wititsuwannakul
Keyword(s):  
Binding Protein ◽  
Lectin Binding ◽  
New Model ◽  
Latex Coagulation

Ultrastructure of human C4-binding protein: proposition for a new model

1985 ◽  
Vol 15 (9) ◽  
pp. 941-945 ◽  
Author(s):  
Marie-Bernadette Villiers ◽  
Nicole M. Thielens ◽  
Christian L. Villiers ◽  
Maurice G. Colomb
Keyword(s):  
Binding Protein ◽  
New Model

scholarly journals Studies on the carbohydrate-binding characteristics of human pulmonary surfactant-associated protein A and comparison with two other collectins: mannan-binding protein and conglutinin

1993 ◽  
Vol 293 (3) ◽  
pp. 873-878 ◽  
Author(s):  
J S Haurum ◽  
S Thiel ◽  
H P Haagsman ◽  
S B Laursen ◽  
B Larsen ◽  
...  
Keyword(s):  
Binding Protein ◽  
Lectin Binding ◽  
Protein A ◽  
Exchange Chromatography ◽  
Carbohydrate Binding ◽  
Phagocytic Cells ◽  
Binding Characteristics ◽  
Carbohydrate Recognition Domains ◽  
Normal Human ◽  
Alveolar Proteinosis

The surfactant-associated protein A (SP-A) belongs to the collectin family, a group of C-type lectins encompassing also surfactant-associated protein D, mannan-binding protein (MBP) and conglutinin. These proteins all have carbohydrate-recognition domains joined to collagen stalks. It seems likely that SP-A, like MBP and conglutinin, may mediate anti-microbial activity through binding to carbohydrates on the microorganisms and collectin receptors on phagocytic cells. We have studied the influence of carbohydrates on the binding of SP-A, MBP and conglutinin to mannan in an enzyme-linked lectin-binding assay. All sugars were of D-configuration, except fucose of which both L- and D-configurations were tested. The order of inhibiting potency on the binding of SP-A was: N-acetylmannosamine > L-fucose, maltose > glucose > mannose. The following sugars were non-inhibitory: galactose, D-fucose, glucosamine, mannosamine, galactosamine, N-acetylglucosamine, and N-acetylgalactosamine. The best inhibitor of MBP was N-acetylglucosamine. Otherwise MBP showed a selectivity similar to that of SP-A. Conglutinin binding was inhibited by all the sugars examined except N-acetylgalactosamine. For conglutinin, as for MBP, the best inhibitor was N-acetylglucosamine. Normal human SP-A, alveolar-proteinosis SP-A purified by ion-exchange chromatography, and alveolar-proteinosis SP-A purified by n-butanol extraction showed no difference in sugar selectivity. The influence of pH and of the calcium concentration was also examined. Organic solvent-extracted SP-A from patients suffering from alveolar proteinosis and normal SP-A showed different sensitivity profiles.

scholarly journals Expression of the Ym2 Lectin-binding Protein Is Dependent on Interleukin (IL)-4 and IL-13 Signal Transduction

2001 ◽  
Vol 276 (45) ◽  
pp. 41969-41976 ◽  
Author(s):  
Dianne C. Webb ◽  
Andrew N. J. McKenzie ◽  
Paul S. Foster
Keyword(s):  
Signal Transduction ◽  
Binding Protein ◽  
Lectin Binding
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