Phosphorylated human galectin-3: Facile large-scale preparation of active lectin and detection of structural changes by CD spectroscopy

Kübler, Dieter, Hung, Chien-Wen, Dam, Tarun K., Kopitz, Jürgen, André, Sabine, Kaltner, Herbert, Lohr, Michaela, Manning, Joachim C., He, Lizhong, Wang, Hui, Middelberg, Anton, Brewer, C. Fred, Reed, Jennifer, Lehmann, Wolf-Dieter and Gabius, Hans-Joachim (2008) Phosphorylated human galectin-3: Facile large-scale preparation of active lectin and detection of structural changes by CD spectroscopy. Biochimica et Biophysica Acta (BBA) - General Subjects, 1780 4: 716-722. doi:10.1016/j.bbagen.2008.01.018


Author Kübler, Dieter
Hung, Chien-Wen
Dam, Tarun K.
Kopitz, Jürgen
André, Sabine
Kaltner, Herbert
Lohr, Michaela
Manning, Joachim C.
He, Lizhong
Wang, Hui
Middelberg, Anton
Brewer, C. Fred
Reed, Jennifer
Lehmann, Wolf-Dieter
Gabius, Hans-Joachim
Title Phosphorylated human galectin-3: Facile large-scale preparation of active lectin and detection of structural changes by CD spectroscopy
Journal name Biochimica et Biophysica Acta (BBA) - General Subjects   Check publisher's open access policy
ISSN 0304-4165
1872-8006
Publication date 2008-04
Sub-type Article (original research)
DOI 10.1016/j.bbagen.2008.01.018
Volume 1780
Issue 4
Start page 716
End page 722
Total pages 7
Place of publication New York, NY, U. S. A.
Publisher Elsevier BV
Collection year 2009
Language eng
Subject C1
860899 Human Pharmaceutical Products not elsewhere classified
100302 Bioprocessing, Bioproduction and Bioproducts
100799 Nanotechnology not elsewhere classified
0601 Biochemistry and Cell Biology
030403 Characterisation of Biological Macromolecules
100709 Nanomedicine
Formatted abstract
Galectin-3 has a unique modular design. Its short N-terminal stretch can be phosphorylated, relevant for nuclear export and anti-anoikis/apoptosis activity. Enzymatic modification by casein kinase 1 at constant ATP concentration yielded mg quantities of mono- and diphosphorylated derivatives at Ser5/Ser11 in a 2:1 ratio. Their carbohydrate-inhibitable binding to asialofetuin, cell surfaces of three tumor lines, rabbit erythrocytes leading to haemagglutination and cytoplasmic sites in fixed tissue sections was not markedly altered relative to phosphate-free galectin-3. Spectroscopically, phosphorylation induced alterations in the far UV CD, indicative of an increase in ordered structure. This is accompanied by changes in the environment of aromatic amino acids signified by shifts in the near UV CD.
© 2008 Elsevier B.V. All rights reserved.
Keyword Apoptosis
Histochemistry
Lectin
Serine phosphorylation
Titania chromatography
Q-Index Code C1
Q-Index Status Confirmed Code

 
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Created: Thu, 16 Apr 2009, 16:16:13 EST by Amanda Lee on behalf of School of Chemical Engineering