A5029311750- Galectins and Cancer Biology
- S100 Proteins and Annexins
- Protease and Inhibitor Mechanisms
- Cell Adhesion Molecules Research
- Extracellular vesicles in disease
- Bone health and treatments
- Glycosylation and Glycoproteins Research
- Signaling Pathways in Disease
- TGF-β signaling in diseases
- Cancer Cells and Metastasis
- Vitamin D Research Studies
- Bone and Dental Protein Studies
- Peptidase Inhibition and Analysis
- Parathyroid Disorders and Treatments
- Blood Coagulation and Thrombosis Mechanisms
- Radiopharmaceutical Chemistry and Applications
- RNA modifications and cancer
- Thyroid Disorders and Treatments
- RNA Interference and Gene Delivery
- Protein Tyrosine Phosphatases
- Carcinogens and Genotoxicity Assessment
- Trypanosoma species research and implications
- Connexins and lens biology
- Pancreatitis Pathology and Treatment
- Cancer-related Molecular Pathways
Meharry Medical College
2016-2025
Xavier University of Louisiana
2013
Tulane University
2013
Vanderbilt University
2004-2012
Institute of Cytochemistry and Molecular Pharmacology
2005
Nashville Oncology Associates
1997
Weatherford College
1996
Prevent Cancer Foundation
1990-1994
Wayne State University
1991-1993
Fox Chase Cancer Center
1992
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 Pro-Gly-rich motif, globular carboxyl-terminal containing carbohydrate-binding site. In this study, we report that the galectin-3 contains cleavage site for members matrix metalloproteinase family enzymes: 72 (gelatinase A, MMP-2) 92 B, MMP-9) proteinases. major gelatinases in is at...
Exosomes are nano-vesicles secreted by a wide range of mammalian cell types. These vesicles abundant in serum and other extracellular fluids contain large repertoire proteins, mRNA microRNA. have been implicated to communication, the transfer infectious agents, neurodegenerative diseases as well tumor progression. However, precise mechanisms which they internalized and/or remain poorly understood. In order follow their release uptake breast cells real time, cell-derived exosomes were tagged...
Exosomes are small, 40–130 nm secreted extracellular vesicles that recently have become the subject of intense focus as agents intercellular communication, disease biomarkers and potential vehicles for drug delivery. It is currently unknown whether a cell produces different populations exosomes with distinct cargo separable functions. To address this question, high‐resolution methods needed. Using commercial flow cytometer directly labelled fluorescent antibodies, we show feasibility using...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTStructure-function relationship of a recombinant human galactoside-binding proteinJosiah Ochieng, David Platt, Larry Tait, Victor Hogan, Tirza Raz, Pnina Carmi, and Avraham RazCite this: Biochemistry 1993, 32, 16, 4455–4460Publication Date (Print):April 27, 1993Publication History Published online1 May 2002Published inissue 27 April 1993https://pubs.acs.org/doi/10.1021/bi00067a038https://doi.org/10.1021/bi00067a038research-articleACS...
Galectin-3 is a beta-galactoside binding lectin whose precise physiological role not yet defined. In the present studies, we questioned whether galectin-3 plays in adhesion of breast carcinoma cells to elastin. The impetus for this analysis was initial observation that cellular receptor elastin, 67 kDa elastin/laminin protein may have galectin-like properties (Mecham et al. [1989] J. Biol. Chem. 264:16652–16657). We therefore analyzed microtiter wells coated with elastin under conditions...
Human galectin-3 binds to the surface of Trypanosoma cruzi trypomastigotes and human coronary artery smooth muscle (CASM) cells. CASM cells express on their secrete it. Exogenous increased binding T. Trypanosome was enhanced when either or were preincubated with galectin-3. Cells stably transfected antisense show a dramatic decrease in expression very little adhesion The addition these restores initial capacity bind trypanosomes. Thus, host is required for exogenous enhances this process,...
Background/Aim: Previous studies have demonstrated that breast cancer cells secrete exosomes into the tumor microenvironment, promoting progression. However, paracrine influence of noncancerous epithelial on growth triple-negative (TNBC) has largely been overlooked. We hypothesize from are secreted stimulating TNBC growth. Materials and Methods: Exosome-containing media were prepared using isolated patient-derived xenografts (PDX) or MCF-10A used to treat MCF-7 cells. characterized ELISA....
The present studies were undertaken to address the innovative role of fetuin-A in growth and invasion potential a triple negative breast cancer (TNBC) cell line, MDA-MB-468. Basal like TNBC that express high levels ectopic have poorer prognosis for patients compared those low protein. We overexpressed MDA-MB-468 then determined invasive overexpressing cells vs controls transfected with empty vector. also adhesion presence only serum free medium complete medium. Our data suggest...
Binding of Trypanosoma cruzi trypomastigotes to laminin is enhanced by galectin‐3, a β‐galactoside binding lectin. The galectin‐3 trypanosomes inhibited lactose. Co‐immunoprecipitations indicate that binds the 45, 32 and 30 kDa trypanosome surface proteins. proteins Polyclonal monoclonal antibodies immunoprecipitated major 64 protein. T. antibody mucin recognized 45 interact with in order enhance adhesion laminin.
Fetuin-A is a serum glycoprotein in the cystatin family associated with regulation of soft tissue calcification. We tested role systemic fetuin tumor cell growth and metastasis by injecting Lewis lung carcinoma (LLC) cells into fetuin-A null their wild-type (WT) littermate control C57BL/6 mice via tail vein, s.c., intrasplenic routes. In experimental assay, lungs WT were filled metastatic nodules, whereas mutant virtually free colonies at end 2 weeks. Lung colonization responded to levels...
Our goal in this study was to define the mechanisms by which fetuin‐A mediates adhesion of tumor cells. The data show that absence fetuin‐A, detached cells secrete exosomes contain most known exosomal associated proteins but lack capacity mediate cellular adhesion. In presence exosomes, contain, addition other proteins, plasminogen and histones. These cell spreading. Plasminogen is a participant novel mechanism. suggest these play role progression.