title: 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.
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.
authors.affiliation: 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.
authors.forename: Jürgen
authors.initials: J
authors.lastname: Kopitz
authors.affiliation: Institut für Physiologische Chemie, Tierärztliche Fakultät, Ludwig-Maximilians-Universität, Veterinärstraße 13, 80539 München, Germany.
authors.forename: Sabine
authors.initials: S
authors.lastname: Vértesy
authors.affiliation: Institut für Physiologische Chemie, Tierärztliche Fakultät, Ludwig-Maximilians-Universität, Veterinärstraße 13, 80539 München, Germany.
authors.forename: Sabine
authors.initials: S
authors.lastname: André
authors.affiliation: Funktionelle Proteomanalyse, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 580, 69120 Heidelberg, Germany.
authors.forename: Sabine
authors.initials: S
authors.lastname: Fiedler
authors.affiliation: Funktionelle Proteomanalyse, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 580, 69120 Heidelberg, Germany.
authors.forename: Martina
authors.initials: M
authors.lastname: Schnölzer
authors.affiliation: Institut für Physiologische Chemie, Tierärztliche Fakultät, Ludwig-Maximilians-Universität, Veterinärstraße 13, 80539 München, Germany.
authors.forename: Hans-Joachim
authors.initials: HJ
authors.lastname: Gabius
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002448:Cell Adhesion; D002449:Cell Aggregation; D049109:Cell Proliferation; D006224:Cricetinae; D037483:Galectin 1 / Q000378:metabolism*; D037502:Galectin 3 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D009447:Neuroblastoma / Q000473:pathology*; D011485:Protein Binding; D015202:Protein Engineering; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D037483:Galectin 1; D037502:Galectin 3; D006023:Glycoproteins; D011994:Recombinant Proteins
keywords: Adhesion; Glycoprotein; Lectin; Matrix metalloproteinase; Neuroblastoma; Proliferation