Mannose receptor determination may be a useful tool in research, because endocytosis via this animal lectin is involved in many functions of macrophage cells, in particular, the scavenger activity, the specific and unspecific defence against infective diseases, the recognition of neoplastic cells and the activation/differentiation process of the monocyte/macrophage and microglial population. To date, available tests required expensive equipment, the use of radioactive material or the availability of a specific antiserum. We describe an ELISA-like assay, based on biotinylated mannose-conjugated bovine serum albumin (BSA), which specifically binds to the cell mannose receptor. Biotin-labelled receptors can be quantified colorimetrically, utilising an avidin-alkaline phosphatase conjugate as the indicator enzyme. This new method is sensitive and reproducible, as well as simple and rapid, and can be performed with standard laboratory equipment.
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http://dx.doi.org/10.1016/s0165-022x(03)00019-8 | DOI Listing |
Cell Surf
June 2025
Departamento de Biología, División de Ciencias Naturales y Exactas, Campus Guanajuato, Universidad de Guanajuato, Noria Alta s/n, col. Noria Alta, C.P. 36050 Guanajuato, Gto, Mexico.
is one of the leading etiological agents of sporotrichosis, a cutaneous and subcutaneous mycosis worldwide distributed. This organism has been recently associated with epidemic outbreaks in Brazil. Despite the medical relevance of this species, little is known about its virulence factors, and most of the information on this subject is extrapolated from .
View Article and Find Full Text PDFJ Cell Sci
January 2025
Department of Genetics, Yale School of Medicine, USA.
Retromer mediates retrograde transport of protein cargos from endosomes to the trans-Golgi network (TGN). γ-secretase is a protease that cleaves the transmembrane domain of its target proteins. Although retromer can form a stable complex with γ-secretase, the functional consequences of this interaction are not known.
View Article and Find Full Text PDFACS Appl Mater Interfaces
January 2025
Department of Ultrasound, National Clinical Research Center for Child Health and Disorders, Ministry of Education Key Laboratory of Child Development and Disorders, Chongqing Engineering Research Center of Stem Cell Therapy, Children's Hospital of Chongqing Medical University, Chongqing 400010, China.
: Photodynamic therapy (PDT) has emerged as a promising treatment for cancer, primarily due to its ability to generate reactive oxygen species (ROS) that directly induce tumor cell death. However, the hypoxic microenvironment commonly found within tumors poses a significant challenge by inhibiting ROS production. This study aims to investigate the effect of improving tumor hypoxia on enhancing PDT.
View Article and Find Full Text PDFProtein Eng Des Sel
January 2025
Pfizer Rare Disease Research Unit, 610 Main Street, Cambridge, MA 02139, United States.
Pompe disease is a tissue glycogen disorder caused by genetic insufficiency of the GAA enzyme. GAA enzyme replacement therapies for Pompe disease have been limited by poor lysosomal trafficking of the recombinant GAA molecule through the native mannose-6-phosphate-mediated pathway. Here, we describe the successful rational engineering of a chimeric GAA enzyme that utilizes the binding affinity of a modified IGF-II moiety to its native receptor to bypass the mannose-6-phosphate-mediated lysosomal trafficking pathway, conferring a significant increase in cellular uptake of the GAA enzyme.
View Article and Find Full Text PDFAdv Sci (Weinh)
January 2025
Institute of Biomedicine and Translational Medicine, University of Tartu, Ravila 14B, Tartu, 50411, Estonia.
In triple-negative breast cancer (TNBC), pro-tumoral macrophages promote metastasis and suppress the immune response. To target these cells, a previously identified CD206 (mannose receptor)-binding peptide, mUNO was engineered to enhance its affinity and proteolytic stability. The new rationally designed peptide, MACTIDE, includes a trypsin inhibitor loop, from the Sunflower Trypsin Inhibitor-I.
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