PRG3 (Major Basic Protein 2) – Structure, Function, and Biological Context OpenAI o3-deep-research-2025-06-26 104 citations 2025-11-03T21:48:25.367714

PRG3 (Major Basic Protein 2) – Structure, Function, and Biological Context

Gene Identity and Evolution

PRG3 is the human gene encoding proteoglycan 3, better known as eosinophil major basic protein 2 (MBP2) (www.genecards.org). It is a paralog of the well-characterized eosinophil major basic protein 1 (MBP1, encoded by PRG2) and arose from an ancient gene duplication. Notably, the human PRG3/MBP2 gene lies on chromosome 11 near the MBP1 gene, and the duplication that created MBP2 predates the divergence of humans and mice (pubmed.ncbi.nlm.nih.gov). This is evidenced by the fact that human MBP2 is more similar in sequence to mouse MBP2 than to human MBP1, indicating a conserved MBP1/MBP2 pair in both species (pubmed.ncbi.nlm.nih.gov). PRG3 is a protein-coding gene; its product MBP2 is sometimes called “MBP homolog” (MBPH) in early literature (www.genecards.org). Together with MBP1 and other eosinophil granule proteins, MBP2 is part of the eosinophil’s cytotoxic armamentarium.

Gene Structure and Protein Features: The PRG3 gene encodes a prepro-protein that includes a signal peptide and a prominent acidic pro-segment, similar to MBP1 (pmc.ncbi.nlm.nih.gov). During eosinophil development, MBP2 is synthesized as an ~25–32 kDa preproprotein (like MBP1’s 32 kDa proMBP1) which is then processed into a mature form of ~14 kDa (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The acidic pro-domain serves to neutralize the highly basic toxin during transit and storage – yielding a nearly neutral pI (~6.2) for the pro-protein (pmc.ncbi.nlm.nih.gov). This mechanism protects the cell’s secretory pathway from the protein’s cationic toxicity until it is cleaved in the granules (pmc.ncbi.nlm.nih.gov). The mature MBP2 polypeptide itself is smaller (approximately 117 amino acids, similar to MBP1) and highly basic, though notably less basic than MBP1 (isoelectric point ~8.7 for MBP2 vs >11 for MBP1) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In fact, MBP2 is estimated to be ~100-fold less basic than MBP1 in net charge (pmc.ncbi.nlm.nih.gov), reflecting numerous amino acid differences – the two MBPs share only ~42 identical residues out of 117 (pmc.ncbi.nlm.nih.gov). Despite this divergence, structural analysis indicates MBP2 most likely folds into the same C-type lectin domain framework as MBP1 (pmc.ncbi.nlm.nih.gov). (Crystal structures of MBP1 confirm it is a member of the C-type lectin family (pmc.ncbi.nlm.nih.gov), and MBP2 conserves the key cysteine pattern albeit with some differences in disulfide bonding (www.ncbi.nlm.nih.gov).) MBP2 contains multiple cysteine residues; a biochemical study found that in the mature protein, two disulfide bonds form (Cys20–Cys115 and Cys92–Cys107, numbering relative to the mature sequence) while several cysteines remain free thiols (www.ncbi.nlm.nih.gov). This atypical disulfide pattern suggests a similar overall fold to MBP1 but with subtle structural differences. Overall, PRG3’s protein product is a cationic, cysteine-rich granule protein largely analogous to MBP1 in domain architecture, but significantly altered in surface charge and sequence.

Expression and Localization

Cell/Tissue Expression: PRG3 expression is highly specific to the eosinophil lineage. Transcription of PRG3 (MBP2) occurs in developing eosinophils within the bone marrow, and mRNA for MBP2 has been detected only in bone marrow eosinophilic precursors (pubmed.ncbi.nlm.nih.gov). In contrast to MBP1’s gene (PRG2), which has additional expression contexts (e.g. a placenta-specific transcript for proMBP1 and some basal expression in the basophil lineage), PRG3 is not expressed in placenta or in basophils (pubmed.ncbi.nlm.nih.gov). This mirrors what is seen at the protein level: MBP2 protein is found exclusively in eosinophil granulocytes (pubmed.ncbi.nlm.nih.gov). A 2006 immunoassay study using MBP2-specific monoclonal antibodies demonstrated that MBP2 is present in eosinophils but undetectable in peripheral blood basophils, mast cells, or other leukocytes (pubmed.ncbi.nlm.nih.gov). By immunofluorescence, MBP2 localized to eosinophil granules, whereas MBP1 was detectable in eosinophils and, to a much lesser extent, in basophils (likely due to basophils endocytosing or binding MBP1) (pubmed.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Importantly, neither MBP1 nor MBP2 was found in neutrophils, lymphocytes, or monocytes (pubmed.ncbi.nlm.nih.gov). Thus, MBP2 is a cell-type-specific product of eosinophils, making it a distinctive marker of eosinophil presence.

Subcellular Localization: Within eosinophils, MBP2 is a major constituent of the secondary (specific) granules. Eosinophil specific granules are characterized by a crystalloid core rich in basic proteins; MBP1 comprises the dense core of these granules, and MBP2 is also stored in the granule matrix (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Both MBP1 and MBP2 are synthesized during eosinophil maturation and packaged into the granules as the acidic proform, which is processed to mature form inside the granule (pmc.ncbi.nlm.nih.gov). Biochemical isolation confirmed that MBP2 protein can be purified from eosinophil granule lysates, verifying its physical presence in granules (www.wikigenes.org). In eosinophil granule extracts, MBP2 is less abundant than MBP1, but clearly present; quantitative assays show MBP1 levels exceed MBP2 in eosinophil lysates by a substantial margin (pubmed.ncbi.nlm.nih.gov). Nonetheless, both MBP1 and MBP2 are co-stored in the same granule compartments (pmc.ncbi.nlm.nih.gov). Upon eosinophil activation or degranulation, these proteins are released into the extracellular space. MBP2, like MBP1, thus functions primarily outside the cell, in the extracellular milieu of tissues or blood where eosinophils have degranulated. There, it can bind to pathogens or impact other cells (see below). In summary, PRG3’s product is localized in eosinophil secretory granules (specific granule lumen) and is secreted outside the cell during degranulation (www.genecards.org). Notably, MBP2 is absent from other tissues and circulating fluids under normal conditions – unlike MBP1’s pro-form, which circulates in pregnancy, MBP2 is not normally found free in plasma except as a marker of eosinophil degranulation (pubmed.ncbi.nlm.nih.gov).

Function and Biological Activities

Primary Function: Major basic protein 2 is a cationic cytotoxic protein of the innate immune system. Although called “proteoglycan 3,” MBP2 is not a proteoglycan in structure but rather a highly basic granuloprotein. Its primary role is analogous to that of MBP1: to help eosinophils attack pathogens, particularly helminth parasites, and to modulate immune responses. MBP2 is directly toxic to cells and parasites – it belongs to the arsenal of eosinophil-derived toxins that can kill microorganisms and larger parasites by damaging their outer surfaces (pmc.ncbi.nlm.nih.gov). Like MBP1, MBP2 is thought to exert cytotoxicity by disrupting cell membranes and surface structures. Studies of MBP1 have shown it can punch holes in lipid bilayers and even fragment DNA in target cells, and while MBP2 is less studied, it is presumed to act in a similar fashion to harm parasites (e.g. parasitic worms) and even host tissues (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Indeed, eosinophil granule proteins including MBP are well known to cause damage to mammalian cells – for example, fragments of bronchial epithelium in asthma patients often show deposition of MBP, implicating these proteins in tissue injury and dysfunction (pmc.ncbi.nlm.nih.gov). MBP2’s ability to kill parasites directly has not been as quantitatively characterized as MBP1’s, but given their structural similarity, MBP2 is believed to contribute to eosinophils’ antiparasitic defense, albeit with lower potency than MBP1 (pmc.ncbi.nlm.nih.gov).

Immunomodulatory Effects: Beyond direct cytotoxicity, MBP2 serves as a pro-inflammatory signaling molecule once released. Functional assays have demonstrated that MBP2 can activate other leukocytes in vitro, much like MBP1. Notably, MBP2 triggers basophils to release inflammatory mediators – it induces basophil degranulation with the release of histamine and the synthesis of leukotriene C4 (LTC₄) (pmc.ncbi.nlm.nih.gov). These mediators promote vasodilation, bronchoconstriction, and recruitment of other immune cells, which are hallmarks of allergic inflammation. In parallel, MBP2 can act on neutrophils, stimulating them to produce reactive oxygen species (superoxide) and to secrete the chemokine IL-8 (CXCL8) (pmc.ncbi.nlm.nih.gov). IL-8 then attracts more neutrophils to the site, amplifying inflammation. In experiments, purified MBP2 was shown to mimic the cytostimulatory activities of MBP1: for example, exposure of neutrophils to MBP2 leads to a respiratory burst and IL-8 secretion, and exposure of basophils causes robust histamine release, just as MBP1 does (www.genecards.org) (pmc.ncbi.nlm.nih.gov). These effects do not require IgE – MBP proteins can activate basophils and mast cells directly (the exact receptors are not fully identified, but the basic nature of MBP may interact with cell surface proteoglycans or receptors to trigger signaling) (pmc.ncbi.nlm.nih.gov). In fact, MBP1/2 are known to be among the factors that activate mast cells and basophils in IgE-independent fashion, contributing to late-phase allergic responses. MBP1 has been shown to activate primed mast cells as well (pmc.ncbi.nlm.nih.gov), and while specific data on MBP2 with mast cells are limited, it likely has a similar capacity (though MBP2 was not detected in mast cells themselves, it could act on them externally).

Importantly, MBP2’s potency is lower than MBP1’s in these activities. Comparative studies indicate that while the spectrum of biological effects of MBP2 “mirror” those of MBP1, its efficacy is reduced (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). For instance, MBP2 causes histamine and LTC₄ release from basophils, but at higher concentrations is needed to achieve the same response as MBP1 (pmc.ncbi.nlm.nih.gov). Similarly, MBP2 stimulates neutrophils, but MBP1 is a stronger activator in inducing superoxide and causing granular enzyme release (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). One biochemical basis for this difference is MBP2’s lower cationic charge density; with a pI of 8.7, MBP2 may bind less avidly to negatively charged sites on cell surfaces compared to MBP1 (pI >11) (pmc.ncbi.nlm.nih.gov). Despite this quantitative difference, the qualitative functions overlap significantly. Both MBP1 and MBP2 are classified as eosinophil-derived cytotoxins and “cytokine-like” mediators that can influence other cells in the innate immune system (pmc.ncbi.nlm.nih.gov). Additionally, MBP1 (and by extension MBP2) can bind to and neutralize heparin and other polyanions (pmc.ncbi.nlm.nih.gov), which might contribute to coagulation changes and modulating local inflammatory signals. (MBP1 is known to be a potent platelet agonist and can provoke bronchial smooth muscle contraction (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov); these specific actions of MBP1 have not been confirmed for MBP2, but they illustrate the pro-inflammatory potential of the MBP family.)

Biological Pathways and Processes: PRG3/MBP2 is involved in several key biological processes tied to eosinophil function. It plays a role in the innate immune response, particularly in defense against multicellular parasites (helminths) and certain bacteria (pmc.ncbi.nlm.nih.gov). In parasitic infections, eosinophils are recruited and degranulate onto the parasite surface; MBP1 and MBP2 are pivotal in damaging the parasite’s tegument or cuticle, aiding in its destruction. In the context of allergic reactions and asthma, MBP2 contributes to the orchestration of inflammation. It is one of the eosinophil granule proteins that cause epithelial damage, enhance bronchial hyperreactivity, and sustain allergic inflammation in tissues (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). For example, the deposition of MBP in bronchial mucosa is associated with airway hyper-responsiveness and tissue remodeling in asthma (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). MBP (largely MBP1, but MBP2 likely adds to the total MBP pool) can provoke bronchospasm and increase airway smooth muscle reactivity – MBP1 has been shown to directly provoke bronchospasm in primate studies (pmc.ncbi.nlm.nih.gov). In allergic diseases, MBP released from eosinophils triggers basophils and mast cells to release histamine and leukotrienes, thereby linking eosinophil activation to immediate hypersensitivity effector pathways (pmc.ncbi.nlm.nih.gov). In summary, MBP2 functions within the eosinophil’s granule exocytosis pathway, acting downstream of eosinophil activation (by cytokines like IL-5 or by IgE-mediated signals via mast cells). Once eosinophils degranulate, MBP2 is one mediator that amplifies the immune response and can directly harm invading organisms or host tissue.

It is worth noting that mature circulating eosinophils store pre-formed MBP2 and generally do not transcribe the PRG3 gene outside the bone marrow. Studies show that by the time eosinophils enter the bloodstream, they have essentially shut off MBP gene transcription – all the MBP1/2 protein they will carry is already made during the bone marrow stage (pmc.ncbi.nlm.nih.gov). Thus, PRG3’s role is mainly in the effector phase (protein release and action), rather than dynamic regulation at the transcriptional level in peripheral tissues. Regulation of PRG3 expression occurs during eosinophilopoiesis under the control of eosinophil-specific transcription factors (e.g. GATA-1 and C/EBP) (pubmed.ncbi.nlm.nih.gov). A conserved GATA site is present in the PRG3 promoter, similar to PRG2, suggesting common regulatory cues for the two MBP genes in eosinophil development (pubmed.ncbi.nlm.nih.gov).

Clinical and Research Insights

Because MBP2 is confined to eosinophils, it has value as a biomarker of eosinophil activation. Unlike MBP1, which can be elevated in pregnancy (as part of a placental protein complex) and is found in small amounts in basophils, MBP2’s presence in body fluids or tissues is a more specific indicator of eosinophil involvement (pubmed.ncbi.nlm.nih.gov) (pubmed.ncbi.nlm.nih.gov). For example, a 2006 study demonstrated that MBP2 levels in serum correlate with eosinophil counts and can distinguish patients with eosinophilia from normal subjects (pubmed.ncbi.nlm.nih.gov). MBP2 was detectable in pathological specimens such as bronchoalveolar lavage (BAL) fluid, sputum, and even stool from patients with eosinophilic diseases, whereas healthy controls have minimal to no MBP2 in such fluids (pubmed.ncbi.nlm.nih.gov). These findings led researchers to propose MBP2 as a specific eosinophil-associated disease marker (pubmed.ncbi.nlm.nih.gov). In conditions like asthma, hypereosinophilic syndrome, eosinophilic gastrointestinal disorders, etc., measuring MBP2 (for instance by ELISA or immunoassay) can reflect the degree of eosinophil degranulation and tissue deposition. Indeed, ongoing research has been developing improved immunoassays to separately quantify eosinophil granule proteins, including MBP2, to better evaluate disease activity in eosinophilic disorders (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). An example is the recent development of assays to distinguish proMBP and mature MBP1; similar approaches can be extended to MBP2 to understand its release in various diseases (pmc.ncbi.nlm.nih.gov).

Clinically, the pathogenic role of MBP (both 1 and 2) in allergic inflammation has motivated therapies that target eosinophils. The rationale is that by depleting eosinophils or inhibiting their activation, one can reduce the release of MBP1/2 and other toxic granule contents that drive tissue damage. For instance, anti-IL-5 monoclonal antibody therapy (e.g. mepolizumab) is now used in severe eosinophilic asthma to eliminate eosinophils. Indirectly, this leads to lower MBP levels in the lungs and blood. A recent study in asthma patients confirms that after months of anti–IL-5 treatment, eosinophil granule protein gene expression (including MBP) in residual blood eosinophils drops to levels seen in healthy individuals (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This reduction in MBP correlates with clinical improvement, underscoring that MBP-mediated effects (like bronchial hyperreactivity) were contributing to disease severity (pmc.ncbi.nlm.nih.gov). Although PRG3 was not individually quantified in that study, the general principle is that eosinophil elimination removes the source of MBP1/2 and thereby lessens inflammation. In other diseases, such as eosinophilic esophagitis or parasitic infections, MBP1 and MBP2 deposition in tissues is a hallmark of eosinophil activity and can be seen histologically as eosinophil granule protein staining or Charcot-Leyden crystals (made of Galectin-10) concomitant with MBP presence (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

From a research standpoint, PRG3/MBP2 has helped illuminate eosinophil biology. The discovery of MBP2 in 1999 was surprising because it is highly divergent in sequence from MBP1 despite similar function (www.wikigenes.org) (pmc.ncbi.nlm.nih.gov). This taught researchers that eosinophils evolved a second basic protein with presumably complementary roles. Evolutionary analysis suggests positive selection may have diversified MBP2’s sequence, perhaps to broaden the range of targets or modulate its interactions (pubmed.ncbi.nlm.nih.gov). Yet the conservation of function (cytotoxicity, activation of basophils/neutrophils) indicates strong selective pressure to retain those activities (pmc.ncbi.nlm.nih.gov). Structural studies are ongoing to determine how MBP2’s unique sequence imparts different properties – for example, the partial disulfide bonding pattern of MBP2 could affect how it packs in the granule or interacts with other molecules (www.ncbi.nlm.nih.gov). There is also interest in whether genetic variation in PRG3 contributes to disease. Genome analyses have occasionally flagged the chromosome 11q12 region (housing PRG2 and PRG3) in conditions like inflammatory bowel disease and atopy (www.genecards.org), though no definitive causative mutations in PRG3 have been confirmed. The Human Protein Atlas reports PRG3 as “evidence at protein level” with a predicted secreted localization, consistent with the experimental evidence (www.wikigenes.org) (pmc.ncbi.nlm.nih.gov). No common loss-of-function mutations are noted in PRG3, and knockout of the MBP homologs in mice leads to interesting phenotypes: mice lacking MBP1 (and another granule protein, eosinophil peroxidase) show a near-complete loss of eosinophils, suggesting that having these granule proteins is essential for eosinophil development or survival (pubmed.ncbi.nlm.nih.gov). This finding hints that MBP2 might also be important for granule biogenesis – the presence of a basic protein may be required to form the crystalloid core and thereby allow eosinophils to mature properly (pubmed.ncbi.nlm.nih.gov). While MBP2 alone has not been knocked out (to public knowledge), the redundancy with MBP1 might mask its contribution; together, the two MBPs are clearly vital for eosinophil granulopoiesis and function.

Conclusion and Expert Perspectives

In summary, PRG3 encodes eosinophil major basic protein 2, a granule-stored, secreted protein that plays a pivotal role in eosinophil biology. MBP2 is a toxic cationic protein that works in tandem with MBP1 to destroy parasites and promote inflammatory responses. It localizes to eosinophil secondary granules and is released upon cell activation, at which point it can cause local tissue damage and activate other immune cells (basophils, mast cells, neutrophils) (pmc.ncbi.nlm.nih.gov). Although MBP2 is less potent than MBP1, it exerts qualitatively similar effects and is exclusively produced by eosinophils (pubmed.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This exclusivity makes it a specific marker of eosinophil activity, and indeed researchers have highlighted MBP2 as a useful biomarker for eosinophil-associated diseases ranging from asthma and allergic rhinitis to hypereosinophilic syndromes (pubmed.ncbi.nlm.nih.gov). Authoritative reviews stress that the family of eosinophil granule proteins (MBP1, MBP2, eosinophil cationic protein, eosinophil peroxidase, etc.) are “multifaceted molecules” responsible for both protective immunity and pathology (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Clinicians and scientists continue to study MBP2 to understand its precise role – for instance, how its structure enables its function and how we might neutralize its harmful effects without compromising host defense. With high-quality monoclonal antibodies and assays now available for MBP2, further research is elucidating its levels in various conditions and could lead to new diagnostic or therapeutic approaches. Overall, PRG3/Major Basic Protein 2 emerges as a key component of eosinophil function: an evolutionarily conserved weapon against parasites and a mediator of allergic inflammation, confined to eosinophils and carrying out its function in the extracellular space where eosinophils do battle. The current understanding, built on both classic studies (www.wikigenes.org) (pmc.ncbi.nlm.nih.gov) and recent analyses (pubmed.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov), solidifies MBP2’s role as an important effector and a telltale indicator of eosinophil-driven immune responses.

References: Recent authoritative sources and key studies have been cited throughout this report. Notably, Plager et al. (1999) first characterized human MBP2 (www.wikigenes.org) (www.wikigenes.org), and a comprehensive 2016 review by Gleich and colleagues summarized the function and biology of MBP1/2 in health and disease (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Experimental evidence for MBP2’s activities and localization is drawn from primary research in the eosinophil literature, including J. Immunology 2006 (specific MBP2 detection) (pubmed.ncbi.nlm.nih.gov) (pubmed.ncbi.nlm.nih.gov) and Protein Journal 2007 (structural biochemistry) (www.ncbi.nlm.nih.gov) (www.ncbi.nlm.nih.gov). The information provided reflects the current consensus and findings up to 2024, highlighting both classical knowledge and recent developments in PRG3/MBP2 research. All claims are supported by the cited literature sources.

Citations

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  27. AnnotationURLCitation(end_index=8027, start_index=7880, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=on%20chromosome%2011.%20MBP,functions%20as%20a%20novel%20enzyme')
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  29. AnnotationURLCitation(end_index=8663, start_index=8495, title='Major basic protein homolog (MBP2): a specific human eosinophil marker - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/17082653/#:~:text=The%20sensitivity%20of%20the%20immunoassay,serum%20MBP2%20discriminated%20patients%20with')
  30. AnnotationURLCitation(end_index=8853, start_index=8744, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=Open%20in%20a%20new%20tab')
  31. AnnotationURLCitation(end_index=9478, start_index=9326, title='PRG3 Gene - GeneCards | PRG3 Protein | PRG3 Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=PRG3#:~:text=An%20extracellular%20matrix%20structural%20constituent,See%20more')
  32. AnnotationURLCitation(end_index=9831, start_index=9716, title='Major basic protein homolog (MBP2): a specific human eosinophil marker - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/17082653/#:~:text=cell%20line%20,associated%20diseases')
  33. AnnotationURLCitation(end_index=10601, start_index=10441, title='The Effect of Mepolizumab on Blood Eosinophil Subtype Distribution and Granule Protein Gene Expression in Severe Eosinophilic Asthma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11963823/#:~:text=cells%2C%20and%20their%20CLC%2C%20EPX%2C,15%7D%20The%20released%20mediators')
  34. AnnotationURLCitation(end_index=11095, start_index=10946, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=effects%20of%20MBP,platelet%20agonist%2C%20causing%20release%20of')
  35. AnnotationURLCitation(end_index=11256, start_index=11096, title='The Effect of Mepolizumab on Blood Eosinophil Subtype Distribution and Granule Protein Gene Expression in Severe Eosinophilic Asthma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11963823/#:~:text=cells%2C%20and%20their%20CLC%2C%20EPX%2C,15%7D%20The%20released%20mediators')
  36. AnnotationURLCitation(end_index=11676, start_index=11516, title='The Effect of Mepolizumab on Blood Eosinophil Subtype Distribution and Granule Protein Gene Expression in Severe Eosinophilic Asthma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11963823/#:~:text=cells%2C%20and%20their%20CLC%2C%20EPX%2C,15%7D%20The%20released%20mediators')
  37. AnnotationURLCitation(end_index=12084, start_index=11925, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=each%20of%20these%20proteins,platelet%20agonist%2C%20causing%20release%20of')
  38. AnnotationURLCitation(end_index=12656, start_index=12507, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=effects%20of%20MBP,platelet%20agonist%2C%20causing%20release%20of')
  39. AnnotationURLCitation(end_index=13108, start_index=12959, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=effects%20of%20MBP,platelet%20agonist%2C%20causing%20release%20of')
  40. AnnotationURLCitation(end_index=13552, start_index=13448, title='PRG3 Gene - GeneCards | PRG3 Protein | PRG3 Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=PRG3#:~:text=UniProtKB%2FSwiss')
  41. AnnotationURLCitation(end_index=13702, start_index=13553, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=effects%20of%20MBP,platelet%20agonist%2C%20causing%20release%20of')
  42. AnnotationURLCitation(end_index=14103, start_index=13954, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=effects%20of%20MBP,platelet%20agonist%2C%20causing%20release%20of')
  43. AnnotationURLCitation(end_index=14508, start_index=14327, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=eosinophil%20granule%20protein%20activities%20have,platelet%20agonist%2C%20causing%20release%20of')
  44. AnnotationURLCitation(end_index=15023, start_index=14905, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=match%20at%20L271%20effects%20of,1')
  45. AnnotationURLCitation(end_index=15183, start_index=15024, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=each%20of%20these%20proteins,platelet%20agonist%2C%20causing%20release%20of')
  46. AnnotationURLCitation(end_index=15448, start_index=15330, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=match%20at%20L271%20effects%20of,1')
  47. AnnotationURLCitation(end_index=15743, start_index=15582, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=match%20at%20L271%20effects%20of,and%20lethally%20damages%20mammalian%20cells')
  48. AnnotationURLCitation(end_index=15893, start_index=15744, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=effects%20of%20MBP,platelet%20agonist%2C%20causing%20release%20of')
  49. AnnotationURLCitation(end_index=16225, start_index=16093, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=MBP,and%20lethally%20damages%20mammalian%20cells')
  50. AnnotationURLCitation(end_index=16621, start_index=16472, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=effects%20of%20MBP,platelet%20agonist%2C%20causing%20release%20of')
  51. AnnotationURLCitation(end_index=16878, start_index=16722, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=Major%20Basic%20Protein%20,rat%20mast%20cells%3B%20neutralizes%20heparin')
  52. AnnotationURLCitation(end_index=17224, start_index=17068, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=Major%20Basic%20Protein%20,rat%20mast%20cells%3B%20neutralizes%20heparin')
  53. AnnotationURLCitation(end_index=17406, start_index=17225, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=eosinophil%20granule%20protein%20activities%20have,platelet%20agonist%2C%20causing%20release%20of')
  54. AnnotationURLCitation(end_index=17960, start_index=17811, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=effects%20of%20MBP,platelet%20agonist%2C%20causing%20release%20of')
  55. AnnotationURLCitation(end_index=18580, start_index=18420, title='The Effect of Mepolizumab on Blood Eosinophil Subtype Distribution and Granule Protein Gene Expression in Severe Eosinophilic Asthma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11963823/#:~:text=cells%2C%20and%20their%20CLC%2C%20EPX%2C,15%7D%20The%20released%20mediators')
  56. AnnotationURLCitation(end_index=18730, start_index=18581, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=effects%20of%20MBP,platelet%20agonist%2C%20causing%20release%20of')
  57. AnnotationURLCitation(end_index=19035, start_index=18866, title='The Effect of Mepolizumab on Blood Eosinophil Subtype Distribution and Granule Protein Gene Expression in Severe Eosinophilic Asthma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11963823/#:~:text=eosinophil%20granule%20proteins%20such%20as,research%20are%20required%20to%20unravel')
  58. AnnotationURLCitation(end_index=19196, start_index=19036, title='The Effect of Mepolizumab on Blood Eosinophil Subtype Distribution and Granule Protein Gene Expression in Severe Eosinophilic Asthma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11963823/#:~:text=cells%2C%20and%20their%20CLC%2C%20EPX%2C,15%7D%20The%20released%20mediators')
  59. AnnotationURLCitation(end_index=19565, start_index=19409, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=Major%20Basic%20Protein%20,rat%20mast%20cells%3B%20neutralizes%20heparin')
  60. AnnotationURLCitation(end_index=19959, start_index=19778, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=eosinophil%20granule%20protein%20activities%20have,platelet%20agonist%2C%20causing%20release%20of')
  61. AnnotationURLCitation(end_index=20782, start_index=20657, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=Both%20MBP,indicates%20that%20it%20is%20a')
  62. AnnotationURLCitation(end_index=21238, start_index=21101, title='A novel human homolog of eosinophil major basic protein - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/11292023/#:~:text=both%20bone%20marrow%20,However%2C%20whether%20a%20C%2FEBP')
  63. AnnotationURLCitation(end_index=21531, start_index=21394, title='A novel human homolog of eosinophil major basic protein - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/11292023/#:~:text=both%20bone%20marrow%20,However%2C%20whether%20a%20C%2FEBP')
  64. AnnotationURLCitation(end_index=22023, start_index=21899, title='Major basic protein homolog (MBP2): a specific human eosinophil marker - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/17082653/#:~:text=and%20their%20granules%2C%20as%20judged,These')
  65. AnnotationURLCitation(end_index=22139, start_index=22024, title='Major basic protein homolog (MBP2): a specific human eosinophil marker - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/17082653/#:~:text=cell%20line%20,associated%20diseases')
  66. AnnotationURLCitation(end_index=22448, start_index=22311, title='Major basic protein homolog (MBP2): a specific human eosinophil marker - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/17082653/#:~:text=measured%20in%20plasma%20and%20serum,associated%20diseases')
  67. AnnotationURLCitation(end_index=22806, start_index=22669, title='Major basic protein homolog (MBP2): a specific human eosinophil marker - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/17082653/#:~:text=measured%20in%20plasma%20and%20serum,associated%20diseases')
  68. AnnotationURLCitation(end_index=23047, start_index=22910, title='Major basic protein homolog (MBP2): a specific human eosinophil marker - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/17082653/#:~:text=measured%20in%20plasma%20and%20serum,associated%20diseases')
  69. AnnotationURLCitation(end_index=23573, start_index=23476, title='Development and Application of Novel Immunoassays for Eosinophil Granule Major Basic Proteins to Evaluate Eosinophilia and Myeloproliferative Disorders - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8107142/#:~:text=Background%3A')
  70. AnnotationURLCitation(end_index=23767, start_index=23574, title='Development and Application of Novel Immunoassays for Eosinophil Granule Major Basic Proteins to Evaluate Eosinophilia and Myeloproliferative Disorders - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8107142/#:~:text=During%20eosinophil%20differentiation%2C%20the%20granule,most%20pathological%20conditions%20remains%20unknown')
  71. AnnotationURLCitation(end_index=24137, start_index=23944, title='Development and Application of Novel Immunoassays for Eosinophil Granule Major Basic Proteins to Evaluate Eosinophilia and Myeloproliferative Disorders - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC8107142/#:~:text=During%20eosinophil%20differentiation%2C%20the%20granule,most%20pathological%20conditions%20remains%20unknown')
  72. AnnotationURLCitation(end_index=25037, start_index=24876, title='The Effect of Mepolizumab on Blood Eosinophil Subtype Distribution and Granule Protein Gene Expression in Severe Eosinophilic Asthma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11963823/#:~:text=like%20cells%20EPX%2C%20MBP%2C%20and,subtypes%20decreased%20to%20HS%20levels')
  73. AnnotationURLCitation(end_index=25207, start_index=25038, title='The Effect of Mepolizumab on Blood Eosinophil Subtype Distribution and Granule Protein Gene Expression in Severe Eosinophilic Asthma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11963823/#:~:text=eosinophil%20granule%20proteins%20such%20as,research%20are%20required%20to%20unravel')
  74. AnnotationURLCitation(end_index=25548, start_index=25379, title='The Effect of Mepolizumab on Blood Eosinophil Subtype Distribution and Granule Protein Gene Expression in Severe Eosinophilic Asthma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11963823/#:~:text=eosinophil%20granule%20proteins%20such%20as,research%20are%20required%20to%20unravel')
  75. AnnotationURLCitation(end_index=26187, start_index=26028, title='The Effect of Mepolizumab on Blood Eosinophil Subtype Distribution and Granule Protein Gene Expression in Severe Eosinophilic Asthma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11963823/#:~:text=match%20at%20L430%20cells%2C%20and,tissues%20by%20disrupting%20the%20lipid')
  76. AnnotationURLCitation(end_index=26348, start_index=26188, title='The Effect of Mepolizumab on Blood Eosinophil Subtype Distribution and Granule Protein Gene Expression in Severe Eosinophilic Asthma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11963823/#:~:text=cells%2C%20and%20their%20CLC%2C%20EPX%2C,15%7D%20The%20released%20mediators')
  77. AnnotationURLCitation(end_index=26655, start_index=26555, title='WikiGenes - PRG3 - proteoglycan 3', type='url_citation', url='https://www.wikigenes.org/e/gene/e/10394.html#:~:text=2,Genomics%C2%A0%282001')
  78. AnnotationURLCitation(end_index=26790, start_index=26656, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=MBP,Comparative%20analyses%20of%20the%20biological')
  79. AnnotationURLCitation(end_index=27211, start_index=27058, title='A novel human homolog of eosinophil major basic protein - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/11292023/#:~:text=Eosinophil%20major%20basic%20protein%20,abundant%20mRNA%20for%20hMBP1%20in')
  80. AnnotationURLCitation(end_index=27520, start_index=27361, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=each%20of%20these%20proteins,platelet%20agonist%2C%20causing%20release%20of')
  81. AnnotationURLCitation(end_index=27850, start_index=27758, title='PRG3 proteoglycan 3, pro eosinophil major basic protein 2 [Homo sapiens (human)] - Gene - NCBI', type='url_citation', url='https://www.ncbi.nlm.nih.gov/gene/10394#:~:text=3,length%20protein')
  82. AnnotationURLCitation(end_index=28224, start_index=28086, title='PRG3 Gene - GeneCards | PRG3 Protein | PRG3 Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=PRG3#:~:text=Extracellular%20matrix%20signatures%20of%20human,92')
  83. AnnotationURLCitation(end_index=28567, start_index=28450, title='WikiGenes - PRG3 - proteoglycan 3', type='url_citation', url='https://www.wikigenes.org/e/gene/e/10394.html#:~:text=WikiGenes%20,Nature%20Genetics%20%282008')
  84. AnnotationURLCitation(end_index=28706, start_index=28568, title='The Peripheral Blood Eosinophil Proteome - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5222579/#:~:text=Selected%20Eosinophil%20Proteins%20of%20Interest,Table')
  85. AnnotationURLCitation(end_index=29200, start_index=29049, title='Expression of the secondary granule proteins major basic protein 1 (MBP-1) and eosinophil peroxidase (EPX) is required for eosinophilopoiesis in mice - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/23736699/#:~:text=Expression%20of%20the%20secondary%20granule,1%20and%20EPX%20promoted%20a')
  86. AnnotationURLCitation(end_index=29557, start_index=29406, title='Expression of the secondary granule proteins major basic protein 1 (MBP-1) and eosinophil peroxidase (EPX) is required for eosinophilopoiesis in mice - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/23736699/#:~:text=Expression%20of%20the%20secondary%20granule,1%20and%20EPX%20promoted%20a')
  87. AnnotationURLCitation(end_index=30426, start_index=30277, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=effects%20of%20MBP,platelet%20agonist%2C%20causing%20release%20of')
  88. AnnotationURLCitation(end_index=30675, start_index=30551, title='Major basic protein homolog (MBP2): a specific human eosinophil marker - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/17082653/#:~:text=and%20their%20granules%2C%20as%20judged,These')
  89. AnnotationURLCitation(end_index=30835, start_index=30676, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=each%20of%20these%20proteins,platelet%20agonist%2C%20causing%20release%20of')
  90. AnnotationURLCitation(end_index=31199, start_index=31084, title='Major basic protein homolog (MBP2): a specific human eosinophil marker - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/17082653/#:~:text=cell%20line%20,associated%20diseases')
  91. AnnotationURLCitation(end_index=31580, start_index=31432, title='EOSINOPHILS: MULTIFACETED BIOLOGIC PROPERTIES AND ROLES IN HEALTH AND DISEASE - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3139217/#:~:text=they%20may%20play%20roles%20in,review%20is%20not%20intended%20to')
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  93. AnnotationURLCitation(end_index=32638, start_index=32502, title='WikiGenes - PRG3 - proteoglycan 3', type='url_citation', url='https://www.wikigenes.org/e/gene/e/10394.html#:~:text=%2A%20Reverse%20transcription,induces%20apoptosis%20%20%206')
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  96. AnnotationURLCitation(end_index=33126, start_index=32957, title='The Effect of Mepolizumab on Blood Eosinophil Subtype Distribution and Granule Protein Gene Expression in Severe Eosinophilic Asthma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC11963823/#:~:text=eosinophil%20granule%20proteins%20such%20as,research%20are%20required%20to%20unravel')
  97. AnnotationURLCitation(end_index=33541, start_index=33405, title='WikiGenes - PRG3 - proteoglycan 3', type='url_citation', url='https://www.wikigenes.org/e/gene/e/10394.html#:~:text=%2A%20Reverse%20transcription,induces%20apoptosis%20%20%206')
  98. AnnotationURLCitation(end_index=33642, start_index=33542, title='WikiGenes - PRG3 - proteoglycan 3', type='url_citation', url='https://www.wikigenes.org/e/gene/e/10394.html#:~:text=2,Genomics%C2%A0%282001')
  99. AnnotationURLCitation(end_index=33928, start_index=33769, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=each%20of%20these%20proteins,platelet%20agonist%2C%20causing%20release%20of')
  100. AnnotationURLCitation(end_index=34078, start_index=33929, title='Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4751725/#:~:text=effects%20of%20MBP,platelet%20agonist%2C%20causing%20release%20of')
  101. AnnotationURLCitation(end_index=34425, start_index=34257, title='Major basic protein homolog (MBP2): a specific human eosinophil marker - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/17082653/#:~:text=The%20sensitivity%20of%20the%20immunoassay,serum%20MBP2%20discriminated%20patients%20with')
  102. AnnotationURLCitation(end_index=34550, start_index=34426, title='Major basic protein homolog (MBP2): a specific human eosinophil marker - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/17082653/#:~:text=and%20their%20granules%2C%20as%20judged,These')
  103. AnnotationURLCitation(end_index=34682, start_index=34602, title='PRG3 proteoglycan 3, pro eosinophil major basic protein 2 [Homo sapiens (human)] - Gene - NCBI', type='url_citation', url='https://www.ncbi.nlm.nih.gov/gene/10394#:~:text=1,PMID')
  104. AnnotationURLCitation(end_index=34775, start_index=34683, title='PRG3 proteoglycan 3, pro eosinophil major basic protein 2 [Homo sapiens (human)] - Gene - NCBI', type='url_citation', url='https://www.ncbi.nlm.nih.gov/gene/10394#:~:text=3,length%20protein')