Major Basic Protein Homolog (MBP2): A Specific Human Eosinophil Marker

Plager, Douglas A.; Loegering, David A.; Checkel, James L.; Tang, Junger; Kephart, Gail M.; Caffes, Patricia L.; Adolphson, Cheryl R.; Ohnuki, Lyo E.; Gleich, Gerald J.

doi:10.1016/j.jaci.2005.12.954

Cited by 7 publications

(5 citation statements)

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“…MBP is one of the most abundant proteins produced by eosinophils, and is found as 2 different homologues (MBP1 and MBP2). MBP1 is also produced at much lower levels in basophils; however, MBP2 is eosinophil specific (1,2). ECP and EDN are both ribonucleases and both function to protect the host from infections, mainly, it is thought, through pore formation in pathogens (3)(4)(5).…”

Section: Granule Proteinsmentioning

confidence: 99%

Role of Eosinophils in Inflammatory Bowel and Gastrointestinal Diseases

Woodruff

Masterson

Fillon

et al. 2011

J. pediatr. gastroenterol. nutr.

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Inflammatory bowel diseases (IBD) are characterized by the invasion of leukocytes into the intestinal mucosa. However, a mixed inflammatory picture is observed that includes neutrophils, lymphocytes, monocytes, and eosinophils. To this day, the role of eosinophils in health and in disease remains unclear. Investigations into their function stem primarily from allergic diseases, asthma, and parasitic infections. This makes it even more difficult to discern a role for the fascinating eosinophil in IBDs because, unlike the lung or the skin, eosinophils reside in normal intestinal mucosa and increase in disease states; consequently, an intricate system must regulate their migration and numbers. These granulocytes are equipped with the machinery to participate in gastrointestinal (GI) inflammation and in the susceptible microenvironment, they may initiate or perpetuate an inflammatory response. A significant body of literature characterizes eosinophils present in the GI microenvironment where they have the potential to interact with other resident cells, thus promoting intestinal remodeling, mucus production, epithelial barrier, cytokine production, angiogenesis, and neuropeptide release. A number of lines of evidence support both potential beneficial and deleterious roles of eosinophils in the gut. Although studies from the gut and other mucosal organs suggest eosinophils affect mucosal GI inflammation, definitive roles for eosinophils in IBDs await discovery.

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Section: Granule Proteinsmentioning

confidence: 99%

Role of Eosinophils in Inflammatory Bowel and Gastrointestinal Diseases

Woodruff

Masterson

Fillon

et al. 2011

J. pediatr. gastroenterol. nutr.

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“…As R2 peptide particularly reduced infiltration of eosinophils ( Figure 1B), we examined the effect of R2 peptide on EMBP, a constituent of eosinophil secondary granules that is elevated in biological fluids from patients with asthma and other eosinophil-associated diseases (Srelts et al, 1998;Plager et al, 2006). R2 peptide pretreatment reduced the increased EMBP expression in BAL cells (Figure 2A left panel) or lung tissues (Figure 2A right panel) of OVA-mice.…”

Section: Effect Of R2 Peptide On Expressions Of Embp Muc5ac or Vcam-1mentioning

confidence: 99%

Anti‐inflammatory effects of the R2 peptide, an inhibitor of transglutaminase 2, in a mouse model of allergic asthma, induced by ovalbumin

Kim

Park

Hong

et al. 2010

British J Pharmacology

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BACKGROUND AND PURPOSETransglutaminase 2 (TGase 2) expression is increased in inflammatory diseases, and TGase 2 inhibitors block these increases. We examined whether the R2 peptide inhibited the expression of TGase 2 in a mouse model of inflammatory allergic asthma. EXPERIMENTAL APPROACHC57BL/6 mice were sensitized and challenged by ovalbumin (OVA) to induce asthma. OVA-specific serum IgE and leukotrienes (LTs) levels were measured by enzyme-linked immunosorbent assay. Recruitment of inflammatory cells into bronchoalveolar lavage (BAL) fluid or lung tissues and goblet cell hyperplasia were assessed histologically. Airway hyperresponsiveness was determined in a barometric plethysmographic chamber. Expression of TGase 2, eosinophil major basic protein (EMBP), the adhesion molecule vascular cell adhesion molecule-1, Muc5ac and phospholipase A2 (PLA2) protein were determined by Western blot. Expression of mRNAs of Muc5ac, cytokines, matrix metalloproteinases (MMPs) and tissue inhibitors of MMPs (TIMPs) were measured by reverse transcriptase-polymerase chain reaction and nuclear factor-kB (NF-kB) by electrophoretic mobility shift assay. KEY RESULTSR2 peptide reduced OVA-specific IgE levels; the number of total inflammatory cells, macrophages, neutrophils, lymphocytes and eosinophils in BAL fluid and the number of goblet cells. Airway hyperresponsiveness, TGase 2 and EMBP levels, mRNA levels of interleukin (IL)-4, IL-5, IL-6, IL-8, IL-13, RANTES, tumour necrosis factor-a, and MMP2/9, Muc5ac, NF-kB activity, PLA2 activity and expressions, and LT levels in BAL cells and lung tissues were all reduced by R2 peptide. R2 peptide also restored expression of TIMP1/2. CONCLUSION AND IMPLICATIONSR2 peptide reduced allergic responses by regulating NF-kB/TGase 2 activity in a mouse model of allergic asthma. This peptide may be useful in the treatment of allergic asthma. AbbreviationsBAL, bronchoalveolar lavage; ELISA, enzyme-linked immunosorbent assay; EMBP, eosinophil major basic protein; EMSA, electrophoretic mobility shift assay; MMP, matrix metalloproteinase; NF-kB, nuclear factor-kappa B; OVA, ovalbumin; PAS, periodic acid-Schiff; PBS, phosphate buffered saline; PLA2, phospholipase A2; RT-PCR, reverse transcriptase-polymerase chain reaction; TGase 2, transglutaminase 2; TIMP, tissue inhibitor of matrix metalloproteinase BJP British Journal of Pharmacology

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“…Previous studies have shown that cationic proteins or peptides such as polyarginine (R9) are involved in formation of RNA nanoparticles (Dana Maria Copolovici, 2014; Wang et al , 2021). Given that serum contains various cationic proteins derived from basophil and eosinophils (Plager et al , 2006), we next tested whether the cationic proteins in serum are responsible for miRNA phase separation. As shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

A novel pathway of functional microRNA uptake and mitochondria delivery

Liu

et al. 2022

Preprint

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Extracellular miRNAs serve as signal molecules in the recipient cells. Uptake of extracellular miRNAs by the recipient cells and their intracellular transport, however, remains elusive. Here we show RNA phase separation as a novel pathway of miRNA uptake. In the presence of serum, synthetic miRNAs rapidly self-assembly into ~110nm discrete nanoparticles which enable miRNAs' entry into different cells. Depleting serum cationic proteins prevents the formation of such nanoparticles and thus blocks miRNA uptake. Different from lipofectamine-mediated miRNA transfection in which the majority of miRNAs are in lysosomes of transfected cells, nanoparticles-mediated miRNA uptake predominantly delivers miRNAs into mitochondria in a polyribonucleotide nucleotidyltransferase 1-dependent manner. Functional assays further show that the internalized miR-21 via miRNA phase separation enhances mitochondrial translation of Cytochrome b, leading to increase in ATP and ROS reduction in HEK293T cells. Our findings reveal a previously unrecognized mechanism for uptaking and delivering functional extracellular miRNAs into mitochondria.

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Major Basic Protein Homolog (MBP2): A Specific Human Eosinophil Marker

Cited by 7 publications

References 0 publications

Role of Eosinophils in Inflammatory Bowel and Gastrointestinal Diseases

Role of Eosinophils in Inflammatory Bowel and Gastrointestinal Diseases

Anti‐inflammatory effects of the R2 peptide, an inhibitor of transglutaminase 2, in a mouse model of allergic asthma, induced by ovalbumin

A novel pathway of functional microRNA uptake and mitochondria delivery

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