scholarly journals Acquisition of LURE-Binding Activity at the Pollen Tube Tip of Torenia fournieri

2013 ◽  
Vol 6 (4) ◽  
pp. 1074-1090 ◽  
Author(s):  
Satohiro Okuda ◽  
Takamasa Suzuki ◽  
Masahiro M. Kanaoka ◽  
Hitoshi Mori ◽  
Narie Sasaki ◽  
...  
Keyword(s):  
Pollen Tube ◽  
Binding Activity ◽  
Torenia Fournieri

scholarly journals Guidance in Vitro of the Pollen Tube to the Naked Embryo Sac of Torenia fournieri

1998 ◽  
Vol 10 (12) ◽  
pp. 2019-2031 ◽  
Author(s):  
Tetsuya Higashiyama ◽  
Haruko Kuroiwa ◽  
Shigeyuki Kawano ◽  
Tsuneyoshi Kuroiwa
Keyword(s):  
Pollen Tube ◽  
Embryo Sac ◽  
Torenia Fournieri

Guidance in vitro of the Pollen Tube to the Naked Embryo Sac of Torenia fournieri

1998 ◽  
Vol 10 (12) ◽  
pp. 2019 ◽  
Author(s):  
Tetsuya Higashiyama ◽  
Haruko Kuroiwa ◽  
Shigeyuki Kawano ◽  
Tsuneyoshi Kuroiwa
Keyword(s):  
Pollen Tube ◽  
Embryo Sac ◽  
Torenia Fournieri

scholarly journals Species Preferentiality of the Pollen Tube Attractant Derived from the Synergid Cell of Torenia fournieri

2006 ◽  
Vol 142 (2) ◽  
pp. 481-491 ◽  
Author(s):  
Tetsuya Higashiyama ◽  
Rie Inatsugi ◽  
Sachio Sakamoto ◽  
Narie Sasaki ◽  
Toshiyuki Mori ◽  
...  
Keyword(s):  
Pollen Tube ◽  
Torenia Fournieri ◽  
Synergid Cell

Isolation of two populations of sperm cells from the pollen tube of Torenia fournieri

2006 ◽  
Vol 25 (11) ◽  
pp. 1138-1142 ◽  
Author(s):  
Su Hong Chen ◽  
Jing Ping Liao ◽  
An Xiu Kuang ◽  
Hui Qiao Tian
Keyword(s):  
Pollen Tube ◽  
Sperm Cells ◽  
Torenia Fournieri ◽  
Two Populations

scholarly journals Pollen Tube Growth in Cross Combinations between Torenia fournieri and Fourteen Related Species

2007 ◽  
Vol 57 (2) ◽  
pp. 117-122 ◽  
Author(s):  
Shinji Kikuchi ◽  
Hiroki Kino ◽  
Hiroyuki Tanaka ◽  
Hisashi Tsujimoto
Keyword(s):  
Pollen Tube ◽  
Related Species ◽  
Pollen Tube Growth ◽  
Tube Growth ◽  
Torenia Fournieri

Genomic analysis of C-type lectins

2002 ◽  
Vol 69 ◽  
pp. 59-72 ◽  
Author(s):  
Kurt Drickamer ◽  
Andrew J. Fadden
Keyword(s):  
Biological Effects ◽  
Cell Signalling ◽  
Genomic Analysis ◽  
Binding Activity ◽  
Immunoglobulin Superfamily ◽  
Carbohydrate Binding ◽  
Carbohydrate Recognition ◽  
Calcium Dependent ◽  
Binding Domains ◽  
Carbohydrate Recognition Domains

Many biological effects of complex carbohydrates are mediated by lectins that contain discrete carbohydrate-recognition domains. At least seven structurally distinct families of carbohydrate-recognition domains are found in lectins that are involved in intracellular trafficking, cell adhesion, cell–cell signalling, glycoprotein turnover and innate immunity. Genome-wide analysis of potential carbohydrate-binding domains is now possible. Two classes of intracellular lectins involved in glycoprotein trafficking are present in yeast, model invertebrates and vertebrates, and two other classes are present in vertebrates only. At the cell surface, calcium-dependent (C-type) lectins and galectins are found in model invertebrates and vertebrates, but not in yeast; immunoglobulin superfamily (I-type) lectins are only found in vertebrates. The evolutionary appearance of different classes of sugar-binding protein modules parallels a development towards more complex oligosaccharides that provide increased opportunities for specific recognition phenomena. An overall picture of the lectins present in humans can now be proposed. Based on our knowledge of the structures of several of the C-type carbohydrate-recognition domains, it is possible to suggest ligand-binding activity that may be associated with novel C-type lectin-like domains identified in a systematic screen of the human genome. Further analysis of the sequences of proteins containing these domains can be used as a basis for proposing potential biological functions.

Limited Proteolysis of Vitronectin by Plasmin Destroys Heparin Binding Activity

1991 ◽  
Vol 66 (03) ◽  
pp. 310-314 ◽  
Author(s):  
David C Sane ◽  
Tammy L Moser ◽  
Charles S Greenberg
Keyword(s):  
Limited Proteolysis ◽  
Plasminogen Activator Inhibitor ◽  
Binding Activity ◽  
Binding Domain ◽  
Heparin Binding ◽  
Inhibitor Type ◽  
Activator Inhibitor Type ◽  
Activator Inhibitor ◽  
Pai 1

SummaryVitronectin (VN) stabilizes plasminogen activator inhibitor type 1 (PAI-1) activity and prevents the fibrin(ogen)-induced acceleration of plasminogen activation by t-PA. These antifibrinolytic activities as well as other functions are mediated by the glycosaminoglycan (GAG) binding domain of VN. Since the GAG binding region is rich in arginyl and lysyl residues, it is a potential target for enzymes such as plasmin. In this paper, the dose and time-dependent proteolysis of VN by plasmin is demonstrated. The addition of urokinase or streptokinase (200 units/ml) to plasma also produced proteolysis of VN. With minimal proteolysis, the 75 kDa band was degraded to a 62-65 kDa form of VN. This minimal proteolysis destroyed the binding of [3H]-heparin to VN and reversed the neutralization of heparin by VN.Thus, the plasmin-mediated proteolysis of the GAG binding activity of VN could destroy the antifibrinolytic activity of VN during physiologic conditions and during thrombolytic therapy. Furthermore, other functions of VN in complement and coagulation systems that are mediated by the GAG binding domain may be destroyed by plasmin proteolysis.

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