Gene Ontology annotation through association of InterPro records with GO terms.
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt.
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara.
Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein. Disulfide structure and carbohydrate attachment.
Purification and cDNA cloning of a novel factor produced by a human T-cell hybridoma: sequence homology with animal lectins.
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
Extracellular matrix signatures of human primary metastatic colon cancers and their metastases to liver.
Proteomic characterization of human multiple myeloma bone marrow extracellular matrix.
Circulating human pregnancy-associated plasma protein-A is disulfide-bridged to the proform of eosinophil major basic protein.
Cloning of cDNA for rat eosinophil major basic protein.
Exocytosis of ficolin-rich granule lumen proteins
Deep research on PRG2 function
Falcon deep research on PRG2/MBP-1 (2023-2024 literature; in situ nanocrystal structure, GWAS, eosinophil-epithelial interactions)
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MBP-1 is stored as dense nanocrystals in eosinophil secretory granules; IL-33 activation drives lattice expansion and crystal extrusion during degranulation.
"MBP-1 forms the **dense nanocrystalline core** of **eosinophil secretory granules (SGr)** and is stored as **nanocrystals** in resting cells."
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Soluble mature MBP-1 is cytotoxic and membrane-disruptive; proMBP-1 and intact nanocrystals are non-toxic, supporting an intracellular neutralization mechanism prior to controlled release.
"Soluble MBP-1 is described as **cytotoxic** and **membrane-disruptive**, whereas **proMBP-1** and **isolated nanocrystalline cores** of MBP-1 are reported as **nontoxic**, indicating that precursor neutralization plus crystallization are key protective strategies inside the eosinophil."
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In situ granule form lacks canonical Ca2+-dependent carbohydrate-binding residues; purified/recrystallized MBP-1 retains binding to sulfated sugars such as heparin.
"MBP-1 retains a **CTL-like carbohydrate-binding region**, but the in situ granule form lacks the canonical acidic residues for **Ca2+-dependent carbohydrate binding**, explaining loss of canonical lectin behavior. By contrast, purified/recrystallized MBP-1 can bind **sulfated sugars such as heparin**."
GWAS of genetic factors affecting white blood cell morphological parameters in Sardinians uncovers influence of chromosome 11 innate immunity gene cluster on eosinophil morphology.
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A rare Sardinian-specific PRG2 p.Ser148Pro variant modifies PRG2 amino acid contacts and protein dynamics, potentially interfering with non-toxic granule formation and altering eosinophil morphology.
"Computational analyses revealed that a rare, Sardinian-specific PRG2:p.Ser148Pro mutation modifies PRG2 amino acid contacts and protein dynamics in a manner that could possibly explain the changes observed in eosinophil morphology."
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PRG2 coding variation has large effect on eosinophil light scatter (granularity).
"The most interesting signal with large effect size on eosinophil scatter ( P -value = 8.33 x 10 −32 , beta = −1.651, se = 0.1351) falls within the innate immunity cluster on chromosome 11, and is located in the PRG2 gene."
Eosinophil-Epithelial Cell Interactions in Asthma.
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Eosinophil granule proteins (including MBP) have bidirectional injurious and modulatory effects on airway epithelial cells in asthma.
"We suggest that eosinophils and their products can have both injurious and beneficial effects on airway epithelial cells in asthma and that there are bidirectional interactions and signaling between eosinophils and airway epithelial cells in asthma."
Evidence for a Role of the Long Non-Coding RNA ITGB2-AS1 in Eosinophil Differentiation and Functions.
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MBP-1 (PRG2) is a key eosinophil granule protein whose expression depends on granulopoiesis programs; loss of lncRNA ITGB2-AS1 reduces cytoplasmic granules and MBP-1 levels.
"ITGB2-AS1 deficiency led to impaired eosinophil differentiation, as evidenced by a reduction in cytoplasmic granules and decreased expression of key eosinophil granule proteins, including eosinophil peroxidase (EPX) and major basic protein-1 (MBP-1)."
Newborns with Favourable Outcomes after Perinatal Asphyxia Have Upregulated Glucose Metabolism-Related Proteins in Plasma.
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PRG2 (bone marrow proteoglycan, P13727) detected in newborn plasma proteomics; differentially abundant between favorable vs unfavorable HIE outcomes. High-throughput observational; not informative for core molecular function but documents extracellular/plasma presence.
"The only down-regulated protein (UniProt ID, log2 fold change) affected by sHIE+ outcome was bone marrow proteoglycan (P13727, −0.72 FC)."