A5060325837- Galectins and Cancer Biology
- Signaling Pathways in Disease
- Glycosylation and Glycoproteins Research
- Toxin Mechanisms and Immunotoxins
- Peptidase Inhibition and Analysis
- Macrophage Migration Inhibitory Factor
- T-cell and Retrovirus Studies
- Neuroscience and Neural Engineering
- Immune Cell Function and Interaction
- Fungal Infections and Studies
- Monoclonal and Polyclonal Antibodies Research
- Aluminum Alloys Composites Properties
- Neuroinflammation and Neurodegeneration Mechanisms
- Helicobacter pylori-related gastroenterology studies
- Amoebic Infections and Treatments
- Hormonal Regulation and Hypertension
- Protein Tyrosine Phosphatases
- Dermatology and Skin Diseases
- Lymphoma Diagnosis and Treatment
- Alzheimer's disease research and treatments
- Hormonal and reproductive studies
- Asthma and respiratory diseases
- Studies on Chitinases and Chitosanases
- Radiomics and Machine Learning in Medical Imaging
- Parasitic Infections and Diagnostics
University of California, Davis
2013-2025
Rutgers, The State University of New Jersey
2024
California Institute for Regenerative Medicine
2020-2023
Institute of Biomedical Science
2014
Institute of Biomedical Sciences, Academia Sinica
2012-2013
Academia Sinica
2013
UC Davis Comprehensive Cancer Center
2012
University of California Davis Medical Center
2010-2012
University of Kragujevac
2012
bioMérieux (United States)
2011
Galectin-3 is a member (if large family of beta-galactoside-binding animal lectins. It has been shown that the expression galectin-3 upregulated in proliferating cells, suggesting possible role for this lectin regulation cell growth. Previously, we have T cells infected with human T-cell leukemia virus type I express high levels galectin-3, contrast to uninfected which do not detectable amounts protein. In study, examined growth properties transfected cDNA, and thus constitutively...
Abstract Galectin-3 is a β-galactoside-binding protein implicated in diverse biological processes. We found that galectin-3 induced human monocyte migration vitro dose-dependent manner, and it was chemotactic at high concentrations (1.0 μM) but chemokinetic low (10–100 nM). Galectin-3-induced inhibited by its specific mAb blocked lactose C-terminal domain fragment of the protein, indicating both N-terminal domains are involved this activity. Pertussis toxin (PTX) almost completely...
Abstract Galectins are a family of mammalian β-galactoside-binding proteins that positively and negatively regulate T cell death. Extracellular galectin-1 directly induces death cells thymocytes, while intracellular galectin-3 blocks In contrast to the antiapoptotic function galectin-3, we demonstrate extracellular human thymocytes cells. However, events in galectin-3- galectin-1-induced differ number ways. Thymocyte subsets different susceptibility two galectins: whereas kills...
Galectin-3 is a member of large family animal lectins. This protein expressed abundantly by macrophages, but its function in this cell type not well understood. We have studied the effect galectin-3 gene targeting on phagocytosis, major macrophages. Compared with wild-type galectin-3-deficient (gal3-/-) cells exhibited reduced phagocytosis IgG-opsonized erythrocytes and apoptotic thymocytes vitro. In addition, gal3-/- mice showed attenuated phagocytic clearance peritoneal macrophages vivo....
Galectin-3 is a member of large family animal lectins. This protein expressed abundantly by macrophages, but its function in this cell type not well understood. We have studied the effect galectin-3 gene targeting on phagocytosis, major macrophages. Compared with wild-type galectin-3–deficient (gal3–/–) cells exhibited reduced phagocytosis IgG-opsonized erythrocytes and apoptotic thymocytes vitro. In addition, gal3–/– mice showed attenuated phagocytic clearance peritoneal macrophages vivo....
Properties of IgE-binding Lectinpressed recombinant human eBP in Escherichia coli and generated a polypeptide by collagenase digestion that contains only the carboxyl-terminal domain (eBP-C) performed detailed analyses various functional properties both tBP-C. EXPERIMENTAL PROCEDURESMaterials-The E. expression vector pKK233-2 was from Pharmacia LKB Biotechnology Inc.Restriction enzymes were obtained New England Biolabs or U. S. Biochemical Corp. Collagenase (Achromobacter iophagus)...
Abstract Lectins play a critical role in host protection against infection. The galectin family of lectins recognizes saccharide ligands on variety microbial pathogens, including viruses, bacteria, and parasites. Galectin-3, expressed by macrophages, dendritic cells, epithelial binds bacterial parasitic pathogens Leishmania major, Trypanosoma cruzi, Neisseria gonorrhoeae. However, there have been no reports galectins having direct effects viability. We found that galectin-3 bound only to...
Galectin-7 is normally expressed in all types of stratified epithelia, but significantly down-regulated squamous cell carcinomas. This protein was recently found to be highly inducible by p53 a colon carcinoma line, DLD-1, and designated as PIG1 (for p53-inducedgene 1). We studied transfectants HeLa DLD-1 cells ectopically expressing this that they were more susceptible apoptosis than control transfectants. observed induced mechanistically distinct stimuli, suggesting galectin-7 acts on...
We have investigated the function of endogenous galectin-3 in T cells. Galectin-3-deficient (gal3 −/− ) CD4 + cells secreted more IFN-γ and IL-4 than gal3 +/+ after T-cell receptor (TCR) engagement. Galectin-3 was recruited to cytoplasmic side immunological synapse (IS) activated In stimulated on supported lipid bilayers, primarily located at peripheral supramolecular activation cluster (pSMAC). Gal3 formed central SMAC bilayers less effectively adhered antigen-presenting firmly cells,...
Abstract Galectin-3 is a β-galactoside-binding lectin that plays an important role in inflammatory diseases. It also interacts with the surface carbohydrates of many pathogens, including LPS. However, its infection not fully understood. Data presented herein demonstrate for first time galectin-3 negative regulator LPS-induced inflammation. constitutively produced by macrophages and directly binds to Galectin-3-deficient had markedly elevated signaling cytokine production compared wild-type...
Disorders of wound healing characterized by impaired or delayed re-epithelialization are a serious medical problem. These conditions affect many tissues, painful, and difficult to treat. In this study, using cornea as model, we demonstrate for the first time importance carbohydrate-binding proteins galectins-3 -7 in wounds. two different models corneal healing, wounds was significantly slower galectin-3-deficient (gal3<sup>−/−</sup>) mice compared with wild-type (gal3<sup>+/+</sup>) mice....
Galectins are a family of β-galactoside-binding animal lectins. In particular, widely studied member galectin-3, previously designated as ϵBP, CBP35, Mac-2, L-29 and L-34, has been associated with assorted processes such cell growth, tumor transformation metastasis. Galectin-3 is expressed in various tissues organs but significantly absent normal hepatocytes. However, evaluation patient liver biopsies for galectin-3 expression resulted the finding that hepatocellular carcinoma (HCC)...
Galectins are a family of β-galactoside-binding animal lectins with conserved carbohydrate recognition domains (CRDs). Here we report the identification and characterization new galectin, galectin-12, which contains two that homologous to galectin CRD. The N-terminal domain all sequence elements predicted form β-sheets found in other galectins, as well carbohydrate-interacting residues. C-terminal shows considerable divergence from consensus sequence, many these residues not present....