Josiah Ochieng

Learn More
The primary structure of galectin-3, a approximately 30 kDa galactoside-binding protein (aka CBP-35, mL-34, hL-31, L-29, Mac-2, and epsilon BP), reveals two structural domains: an amino-terminal domain consists of a Pro-Gly-rich motif, and a globular carboxyl-terminal domain containing a carbohydrate-binding site. In this study, we report that the(More)
Galectin-3 is an important intracellular and extracellular lectin which is presumed to interact with extracellular matrix proteins and cell surface glycoproteins in normal and pathophysiological conditions. The exact physiological role of the protein is presently not known. We have previously demonstrated that recombinant human galectin-3 is a novel(More)
Binding of Trypanosoma cruzi trypomastigotes to laminin is enhanced by galectin-3, a beta-galactoside binding lectin. The galectin-3 enhanced binding of trypanosomes to laminin is inhibited by lactose. Co-immunoprecipitations indicate that galectin-3 binds to the 45, 32 and 30 kDa trypanosome surface proteins. Binding of galectin-3 to the 45, 32 and 30 kDa(More)
Galectin-3 has been suspected of modulating cell to extracellular matrix interactions in a novel fashion ever since it was first described. However, the rapid accumulation of research data in just the last 8 years alone has completely changed our perspective of this multifunctional protein. Its chimeric nature (consists of carbohydrate recognition and(More)
The control of cellular adhesion to extracellular matrix proteins is poorly understood. In the present analyses, we set out to test the hypothesis that high galectin-3 concentration on the cell surface downregulates cellular adhesion to the extracellular matrix proteins. Various tumor cell lines were briefly incubated without or with galectin-3 and then(More)
In the following experiments, we sought to understand the triggering mechanism which propels galectin-3 to be secreted into the extracellular compartment from its intracellular stores in breast carcinoma cells. We also wanted to analyze in greater details the role of galectin-3 in cellular adhesion and spreading. To do this, we made use of two pairs of(More)
Cystatins, the classical inhibitors of C1 cysteine proteinases, have been extensively studied and reviewed in the literature. Over the last 20 years, however, proteins containing cystatin domains but lacking protease inhibitory activities have been identified, and most likely more will be described in the near future. These proteins together with family 1,(More)
In this report, we have analyzed the adhesive interactions of a breast carcinoma cell line, BT-549, and its galectin-3-transfected subclone 11-9-1-4 with laminin, collagen IV and fibronectin. We determined that 11-9-1-4 cells adhered much more rapidly (within 1 h of plating) to laminin- and collagen IV-coated wells than the galectin-3 null expressing BT-549(More)
Galectin-3 is a beta-galactoside binding lectin whose precise physiological role is not yet defined. In the present studies, we questioned whether galectin-3 plays a role in the adhesion of breast carcinoma cells to elastin. The impetus for this analysis was the initial observation that the cellular receptor for elastin, the 67 kDa elastin/laminin protein(More)
The human galectin-3 is a galactoside-binding protein of 31 kDa which functions as a receptor for glycoproteins containing poly N-acetyllactosamine side chains and as a substrate for matrix metalloproteinases-2 and -9. We studied its expression by flow cytoflourimetry, Western, Northern and Southern analyses, in five cultured human breast carcinoma cell(More)