Marsich Eleonora, Mozetic Pamela, Ortolani Fulvia, Contin Magali, Marchini Maurizio, Vetere Amedeo, Pacor Sabrina, Semeraro Sabrina, Vittur Franco, Paoletti Sergio
Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, Trieste, Italy.
Matrix Biol. 2008 Jul;27(6):513-25. doi: 10.1016/j.matbio.2008.04.003. Epub 2008 May 8.
Galectin-1 is a 14 kDa beta-galactoside binding protein, capable of forming lattice-like structures with glycans of cellular glycoconjugates and inducing intracellular signaling. The expression of Galectin-1 in porcine cartilage is described in this work for the first time. Immunocytochemical methods revealed distinct distribution patterns for both articular and growth plate cartilage. In articular cartilage, the highest reactivity for Galectin-1 was found in all chondrocytes at the superficial zone and in most of those at the lower layer of the middle zone. In the growth plate, marked reactivity was seen in chondrocytes at the proliferative zone and reached a maximum level for the column-forming cells at the hypertrophic zone. In addition, different Galectin-1 distribution patterns were observed at the subcellular level. With regards to the metabolic effects of Galectin-1, the results in vitro seem to indicate an inhibitory effect of Galectin-1 on articular chondrocyte anabolism (i.e. inhibition of cell proliferation and anabolic gene expression) and a stimulation of catabolic processes (i.e. induction of matrix degradation and hypertrophy marker expression). These data represent a starting point for the understanding the molecular mechanisms underlining ECM-Galectin-1 interaction and the subsequent signaling-cell transduction processes involving cartilage formation and maturation.
