Format

Send to

Choose Destination
Biochimie. 2014 Sep;104:90-9. doi: 10.1016/j.biochi.2014.05.010. Epub 2014 Jun 6.

Human chimera-type galectin-3: defining the critical tail length for high-affinity glycoprotein/cell surface binding and functional competition with galectin-1 in neuroblastoma cell growth regulation.

Author information

1
Abteilung für Angewandte Tumorbiologie, Zentrum Pathologie, Klinikum der Ruprecht-Karls-Universität, Im Neuenheimer Feld 224, 69120 Heidelberg, Germany. Electronic address: juergen.kopitz@med.uni-heidelberg.de.
2
Institut für Physiologische Chemie, Tierärztliche Fakultät, Ludwig-Maximilians-Universität, Veterinärstraße 13, 80539 München, Germany.
3
Funktionelle Proteomanalyse, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 580, 69120 Heidelberg, Germany.

Abstract

Many human proteins have a modular design with receptor and structural domains. Using adhesion/growth-regulatory galectin-3 as model, we describe an interdisciplinary strategy to define the functional significance of its tail established by nine non-triple helical collagen-like repeats (I-IX) and the N-terminal peptide. Genetic engineering with sophisticated mass spectrometric product analysis provided the tools for biotesting, i.e. eight protein variants with different degrees of tail truncation. Evidently,various aspects of galectin-3 activity (cis binding and cell bridging) are affected by tail shortening in a different manner. Thus, this combined approach reveals an unsuspected complexity of structure-function relationship, encouraging further application beyond this chimera-type galectin.

KEYWORDS:

Adhesion; Glycoprotein; Lectin; Matrix metalloproteinase; Neuroblastoma; Proliferation

PMID:
24909114
DOI:
10.1016/j.biochi.2014.05.010
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center