scholarly journals Keratocan and Lumican Regulate Neutrophil Infiltration and Corneal Clarity in Lipopolysaccharide-induced Keratitis by Direct Interaction with CXCL1

2007 ◽  
Vol 282 (49) ◽  
pp. 35502-35509 ◽  
Author(s):  
Eric C. Carlson ◽  
Michelle Lin ◽  
Chia-Yang Liu ◽  
Winston W-Y. Kao ◽  
Victor L. Perez ◽  
...  
Keyword(s):  
Inflammatory Response ◽  
Viral Vectors ◽  
Fluorescent Protein ◽  
Critical Role ◽  
Corneal Thickness ◽  
Neutrophil Migration ◽  
Direct Interaction ◽  
Neutrophil Infiltration ◽  
Wild Type ◽  
Core Proteins

Keratocan and lumican are keratan-sulfate proteoglycans (KSPG), which have a critical role in maintaining corneal clarity. To determine whether these KSPGs have a role in corneal inflammation, we examined Kera–/– and Lum–/– mice in a model of lipopolysaccharide (LPS)-induced keratitis in which wild-type mice develop increased corneal thickness and haze due to neutrophil infiltration to the corneal stroma. Corneal thickness increases caused by LPS mice were significantly lower in Kera–/– and Lum–/– than wild-type mice. Further, LPS-injected Lum–/– mice had elevated corneal haze levels compared with that of Kera–/– and wild-type. At 24 h post-injection, total enhanced green fluorescent protein-positive bone marrow-derived inflammatory cells in chimeric mice was significantly lower in Kera–/– mice and Lum–/– mice compared with wild-type mice. Neutrophil infiltration was inhibited in Kera–/– and Lum–/– mice at 6 and 24 h post-stimulation, with Lum–/– corneas having the most profound defect in neutrophil migration. Reconstitution of keratocan and lumican expression in corneas of Kera–/– and Lum–/– mice using adeno-keratocan and adeno-lumican viral vectors, respectively, resulted in normal neutrophil infiltration in response to LPS. Immunoprecipitation/Western blot analysis showed that lumican and keratocan core proteins bind the CXC chemokine KC during a corneal inflammatory response, indicating that corneal KSPGs mediate neutrophil recruitment to the cornea by regulating chemokine gradient formation. Together, these data support a significant role for lumican and keratocan in a corneal inflammatory response with respect to edema, corneal clarity, and cellular infiltration.

scholarly journals Mesenchymal Stem Cells Ameliorate Hepatic Ischemia/Reperfusion Injury via Inhibition of Neutrophil Recruitment

2018 ◽  
Vol 2018 ◽  
pp. 1-10 ◽  
Author(s):  
Shihui Li ◽  
Xu Zheng ◽  
Hui Li ◽  
Jun Zheng ◽  
Xiaolong Chen ◽  
...  
Keyword(s):  
Stem Cells ◽  
Mesenchymal Stem Cells ◽  
Inflammatory Response ◽  
Reperfusion Injury ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Neutrophil Migration ◽  
Neutrophil Infiltration ◽  
Hepatic Ischemia ◽  
The Impact

Ischemia/reperfusion injury (IRI) remains a major problem in organ transplantation, which represents the main cause of graft dysfunction posttransplantation. Hepatic IRI is characterized by an excessive inflammatory response within the liver. Mesenchymal stem cells (MSCs) have been shown to be immunomodulatory cells and have the therapeutic action on IRI in several organs. However, the mechanism of regulatory effect of MSCs on IRI remains unclear. In the present study, we examined the impact of MSCs on hepatic inflammatory response such as neutrophil influx and liver damage in a rat model of 70% hepatic IRI. Treatment with MSCs protected rat against hepatic IRI, with significantly decreased serum levels of liver enzymes, attenuated hepatic neutrophil infiltration, reduced expression of apoptosis-associated proteins, and ameliorated liver pathological injury. MSCs also significantly enhanced the intracellular activation of p38 MAPK phosphorylation, which led to decreased expression of CXCR2 on the surface of neutrophils. In addition, MSCs significantly diminished neutrophil chemoattractant CXCL2 production by inhibiting NF-κB p65 phosphorylation in macrophages. These results demonstrate that MSCs significantly ameliorate hepatic IRI predominantly through its inhibitory effect on hepatic neutrophil migration and infiltration.

A critical role of placental growth factor in the induction of inflammation and edema formation

Blood ◽  
2003 ◽  
Vol 101 (2) ◽  
pp. 560-567 ◽  
Author(s):  
Hajimu Oura ◽  
Jennifer Bertoncini ◽  
Paula Velasco ◽  
Lawrence F. Brown ◽  
Peter Carmeliet ◽  
...  
Keyword(s):  
Growth Factor ◽  
Inflammatory Response ◽  
Critical Role ◽  
Placental Growth Factor ◽  
Delayed Type Hypersensitivity ◽  
Epidermal Keratinocytes ◽  
Wild Type ◽  
Edema Formation ◽  
Cutaneous Inflammation ◽  
Endothelial Growth Factor

Angiogenesis is a prominent feature of a number of inflammatory human diseases, including rheumatoid arthritis, psoriasis, and cutaneous delayed-type hypersensitivity (DTH) reactions. Up-regulation of placental growth factor (PlGF), a member of the vascular endothelial growth factor (VEGF) family, has been found in several conditions associated with pathologic angiogenesis; however, its distinct role in the control of angiogenesis has remained unclear. To directly investigate the biologic function of PlGF in cutaneous inflammation and angiogenesis, DTH reactions were investigated in the ear skin of wild-type mice, of PlGF-deficient mice, and of transgenic mice with targeted overexpression of human PlGF-2 in epidermal keratinocytes, driven by a keratin 14 promoter expression construct. Chronic transgenic delivery of PlGF-2 to murine epidermis resulted in a significantly increased inflammatory response, associated with more pronounced vascular enlargement, edema, and inflammatory cell infiltration than seen in wild-type mice. Conversely, PlGF deficiency resulted in a diminished and abbreviated inflammatory response, together with a reduction of inflammatory angiogenesis and edema formation. VEGF expression was up-regulated at a comparable level in the inflamed skin of all genotypes. These findings reveal that placental growth factor plays a critical role in the control of cutaneous inflammation, and they suggest inhibition of PlGF bioactivity as a potential new approach for anti-inflammatory therapy.

scholarly journals Direct interaction of eag domains and cyclic nucleotide–binding homology domains regulate deactivation gating in hERG channels

2013 ◽  
Vol 142 (4) ◽  
pp. 351-366 ◽  
Author(s):  
Elena C. Gianulis ◽  
Qiangni Liu ◽  
Matthew C. Trudeau
Keyword(s):  
Cyclic Nucleotide ◽  
Fluorescent Protein ◽  
Critical Role ◽  
Specific Interaction ◽  
Resonance Energy ◽  
Direct Interaction ◽  
Nucleotide Binding ◽  
Cyclic Nucleotide Binding ◽  
Partial Restoration ◽  
Herg Channels

Human ether-á-go-go (eag)-related gene (hERG) potassium channels play a critical role in cardiac repolarization and are characterized by unusually slow closing (deactivation) kinetics. The N-terminal “eag” domain and a C-terminal C-linker/cyclic nucleotide–binding homology domain (CNBHD) are required for regulation of slow deactivation. The region between the S4 and S5 transmembrane domains (S4–S5 linker) is also implicated in this process, but the mechanism for regulation of slow deactivation is unclear. Here, using an eag domain–deleted channel (hERG Δeag) fused to Citrine fluorescent protein, we found that most channels bearing individual alanine mutations in the S4–S5 linker were directly regulated by recombinant eag domains fused to a cyan fluorescent protein (N-eag-CFP) and had robust Förster resonance energy transfer (FRET). Additionally, a channel bearing a group of eight alanine residues in the S4–S5 linker was not measurably regulated by N-eag-CFP domains, but robust FRET was measured. These findings demonstrate that the eag domain associated with all of the S4–S5 linker mutant channels. In contrast, channels that also lacked the CNBHD (hERG Δeag ΔCNBHD-Citrine) were not measurably regulated by N-eag-CFP nor was FRET detected, suggesting that the C-linker/CNBHD was required for eag domains to directly associate with the channel. In a FRET hybridization assay, N-eag-CFP had robust FRET with a C-linker/CNBHD-Citrine, suggesting a direct and specific interaction between the eag domain and the C-linker/CNBHD. Lastly, coexpression of a hERG subunit lacking the CNBHD and the distal C-terminal region (hERG ΔpCT-Citrine) with hERG Δeag-CFP subunits had FRET and partial restoration of slow deactivation. Collectively, these findings reveal that the C-linker/CNBHD, but not the S4–S5 linker, was necessary for the eag domain to associate with the channel, that the eag domain and the C-linker/CNBHD were sufficient for a direct interaction, and that an intersubunit interaction between the eag domain and the C-linker/CNBHD regulated slow deactivation in hERG channels at the plasma membrane.

scholarly journals Tanshinone IIA Protects against Dextran Sulfate Sodium- (DSS-) Induced Colitis in Mice by Modulation of Neutrophil Infiltration and Activation

2016 ◽  
Vol 2016 ◽  
pp. 1-10 ◽  
Author(s):  
Xiaowei Liu ◽  
Haiyue He ◽  
Tingting Huang ◽  
Zhen Lei ◽  
Fuquan Liu ◽  
...  
Keyword(s):  
Dextran Sulfate ◽  
Dextran Sulfate Sodium ◽  
Intestinal Inflammation ◽  
Therapeutic Potential ◽  
Activity Index ◽  
Critical Role ◽  
Neutrophil Migration ◽  
Neutrophil Infiltration ◽  
Tanshinone Iia

Neutrophils play a critical role in the initiation and maintenance of intestinal inflammation. However, conventional neutrophil-targeted therapies can impair normal host defense. Tanshinone IIA has been recently revealed to act directly on neutrophils. Hence, we aimed at investigating whether Tanshinone IIA can protect against experimental colitis through modulation of neutrophils. We induced colitis in C57BL/6 mice by giving 3% dextran sulfate sodium (DSS) orally, and meanwhile, we treated mice daily with Tanshinone IIA intraperitoneally. The severity of colitis was evaluated by calculating disease activity index (DAI) and histological parameters. Neutrophil infiltration and activation in the colons of mice were measured. Moreover, whether Tanshinone IIA has direct effects on neutrophil migration and activation was determined in vitro. Our data showed that Tanshinone IIA significantly ameliorated the severity of DSS-induced colitis in mice, evidenced by the reduced DAI and improved colonic inflammation. In addition, Tanshinone IIA decreased neutrophil infiltration of intestinal mucosa and activation and reduced colonic inflammatory cytokines in DSS-treated mice. Furthermore, Tanshinone IIA was demonstrated to significantly suppress neutrophil migration and activation. These results provide compelling evidence that Tanshinone IIA has a therapeutic potential for alleviating inflammatory colitis in mice, which is possibly mediated by the immunomodulation of neutrophils.

scholarly journals TLR agonists regulate alloresponses and uncover a critical role for donor APCs in allogeneic bone marrow rejection

Blood ◽  
2008 ◽  
Vol 112 (8) ◽  
pp. 3508-3516 ◽  
Author(s):  
Patricia A. Taylor ◽  
Michael J. Ehrhardt ◽  
Christopher J. Lees ◽  
Angela Panoskaltsis-Mortari ◽  
Arthur M. Krieg ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Dna Sequences ◽  
Fluorescent Protein ◽  
Critical Role ◽  
Allogeneic Bone ◽  
Wild Type ◽  
Cpg Odns ◽  
Rejection Response ◽  
B Lineage ◽  
Green Fluorescent

Abstract Cytosine-phosphorothioate-guanine oligodeoxynucleotides (CpG ODNs) are synthetic ODNs with unmethylated DNA sequences that mimic viral and bacterial DNA and protect against infectious agents and tumor challenge. We show that CpG ODNs markedly accelerated graft-versus-host disease (GVHD) lethality by Toll-like receptor 9 (TLR9) ligation of host antigen-presenting cells (APCs), dependent upon host IFNγ but independent of host IL-12, IL-6, or natural killer (NK) cells. Imaging studies showed significantly more green fluorescent protein–positive (GFP+) effector T cells in lymphoid and nonlymphoid organs. In engraftment studies, CpG ODNs promoted allogeneic donor bone marrow (BM) rejection independent of host IFNγ, IL-12, or IL-6. During the course of these studies, we uncovered a previously unknown and critical role of donor BM APCs in modulating the rejection response. CpG ODNs promoted BM rejection by ligation of donor BM, but not host, TLR9. CpG ODNs did not impair engraftment of TLR9−/− BM unless wild-type myeloid (CD11b+) but not B-lineage (CD19+) BM cells were added to the donor inoculum. The importance of donor BM APCs in modulating the strength of the host antidonor rejection response was underscored by the finding that B7-1/B7-2−/− BM was less likely than wild-type BM to be rejected. Collectively, these data offer new insight into the mechanism of alloresponses regulating GVHD and BM rejection.

scholarly journals Peptidyl arginine deiminase-4-deficient mice are protected against kidney and liver injury after renal ischemia and reperfusion

2016 ◽  
Vol 311 (2) ◽  
pp. F437-F449 ◽  
Author(s):  
May Rabadi ◽  
Mihwa Kim ◽  
Vivette D'Agati ◽  
H. Thomas Lee
Keyword(s):  
Inflammatory Response ◽  
Nuclear Translocation ◽  
Neutrophil Infiltration ◽  
Arginine Deiminase ◽  
Ischemia And Reperfusion ◽  
Wild Type ◽  
Tubular Necrosis ◽  
Renal Tubular ◽  
Deficient Mice ◽  
Renal Tubular Necrosis

We previously demonstrated that renal peptidyl arginine deiminase-4 (PAD4) is induced after renal ischemia and reperfusion (I/R) injury and exacerbates acute kidney injury (AKI) by increasing the renal tubular inflammatory response. Here, we tested whether genetic ablation of PAD4 attenuates renal injury and inflammation after I/R in mice. After renal I/R, PAD4 wild-type mice develop severe AKI with large increases in plasma creatinine, neutrophil infiltration, as well as significant renal tubular necrosis, apoptosis, and proinflammatory cytokine generation. In contrast, PAD4-deficient mice are protected against ischemic AKI with reduced real tubular neutrophil infiltration, renal tubular necrosis, and apoptosis. In addition, hepatic injury and inflammation observed in PAD4 wild-type mice after renal I/R are significantly attenuated in PAD4-deficient mice. We also show that increased renal tubular PAD4 expression after renal I/R is associated with translocation of PAD4 from the nucleus to the cytosol. Consistent with PAD4 cytosolic translocation, we show increased renal tubular cytosolic peptidyl-citrullination after ischemic AKI. Mechanistically, recombinant PAD4 treatment increased nuclear translocation of NF-κB in cultured human as well as murine proximal tubule cells that is inhibited by a PAD4 inhibitor (2-chloroamidine). Taken together, our studies further support the hypothesis that renal tubular PAD4 plays a critical role in renal I/R injury by increasing the renal tubular inflammatory response and neutrophil infiltration after renal I/R perhaps by interacting with the proinflammatory transcription factor NF-κB in the cytosol and promoting its nuclear translocation.

Regulation of Systemic and Local Neutrophil Responses by G-CSF during Pulmonary Pseudomonas aeruginosa Infection.

Blood ◽  
2004 ◽  
Vol 104 (11) ◽  
pp. 1460-1460
Author(s):  
Alyssa D. Gregory ◽  
Lisa A. Hogue ◽  
Thomas W. Ferkol ◽  
Daniel C. Link
Keyword(s):  
Bone Marrow ◽  
Pseudomonas Aeruginosa ◽  
Post Infection ◽  
Neutrophil Migration ◽  
Annexin V ◽  
Severe Infection ◽  
Neutrophil Infiltration ◽  
Wild Type ◽  
Neutrophil Number ◽  
Neutrophil Response

Abstract Granulocyte colony-stimulating factor (G-CSF) expression is often induced during infection, resulting in high concentrations of G-CSF in inflammatory exudates and in the blood. This increased expression suggests that G-CSF may regulate both local and systemic neutrophil responses. Previous studies of G-CSF or G-CSF receptor deficient (G-CSFR−/−) mice challenged with different infectious agents have provided conflicting results concerning the importance of G-CSF in the regulation of stress granulopoiesis. In the present study, we use a physiologically-relevant infectious model in which Pseudomonas aeruginosa coupled to agarose beads is injected intratracheally into wild type or G-CSFR−/− mice inbred onto a C57BL/6 background. This model produces a smoldering P. aeruginosa infection in the lungs, simulating the infection observed in many patients with cystic fibrosis. Importantly, the concentration of G-CSF in the blood and bronchoalveolar lavage fluid (BALF) is significantly elevated in this model. We show that G-CSFR−/− mice display decreased survival in response to P. aeruginosa infection. Extensive pulmonary necrosis was present in G-CSFR−/− mice, and quantitative bacteriology showed decreased clearance of P. aerguinosa from the lungs. Despite this evidence for severe infection, histological studies showed that neutrophil infiltration into the lungs of G-CSFR−/− mice was markedly decreased. To characterize this defect further, we examined the systemic neutrophil response. In wild type mice, neutrophil number in the blood increased from 0.8 ± 0.1 x 10−6/ml at baseline to 2.5 ± 0.3 x 10−6/ml at 48 hours post-infection (all data represent the mean ± SEM). In contrast, G-CSFR−/− mice were neutropenic at baseline (0.1 ± 0.02 x 10−6/ml) and little increase in blood neutrophils was noted at 48 hours post-infection (0.5 ± 0.1 x 10−6/ml). In both groups of mice, a modest decrease in bone marrow neutrophils was observed during infection. These data suggest that the systemic neutrophil response in this model is dependent upon G-CSF signals and is primarily mediated by increased neutrophil release from the bone marrow rather than increased neutrophil production. We next examined the local neutrophil response. Despite normal (mip-2) or increased (KC) expression of the major chemokines regulating neutrophil migration in mice, the number of neutrophils present in the BALF of G-CSFR−/− mice following infection was markedly reduced compared to wild type [number of neutrophils per ml of BALF at 48 hours post-infection ± SEM: 3.5 ± 0.7 x 106 (wild type); 0.7 ± 0.4 x 106 (G-CSFR−/−); p<.05]. Since neutrophil number in a tissue is dependent upon both their emigration and subsequent clearance, we measured the percentage of apoptotic neutrophils in the BALF. Interestingly, the percentage of apoptotic (Annexin V-positive) neutrophils was significantly increased in G-CSFR−/− mice, suggesting that G-CSF signals may play an important role in regulating neutrophil survival at the inflammatory site. Collectively these data provide new evidence that G-CSF signals play important but specific roles in the regulation of the systemic and local neutrophil response following infection.

scholarly journals The V Antigen of Pseudomonas aeruginosa Is Required for Assembly of the Functional PopB/PopD Translocation Pore in Host Cell Membranes

2004 ◽  
Vol 72 (8) ◽  
pp. 4741-4750 ◽  
Author(s):  
Julien Goure ◽  
Alexandrine Pastor ◽  
Eric Faudry ◽  
Jacqueline Chabert ◽  
Andréa Dessen ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Host Cell ◽  
Cell Membranes ◽  
Fluorescent Protein ◽  
Direct Interaction ◽  
Wild Type ◽  
Gene Deletions ◽  
Infected Rbcs ◽  
Green Fluorescent ◽  
Host Cell Membranes

ABSTRACT Pseudomonas aeruginosa efficiently intoxicates eukaryotic cells through the activity of the type III secretion-translocation system (TTSS). Gene deletions within the translocation operon pcrGVH-popBD abolish pore-forming activity of P. aeruginosa strains with macrophages and TTSS-dependent hemolysis. Here we investigated the requirements for PcrV, PopB, and PopD in pore formation by analyzing specific mutants using red blood cells (RBCs) and fibroblasts expressing green fluorescent protein fused to actin. Simultaneous secretion of three proteins, PopB, PopD, and PcrV, was required to achieve wild-type hemolysis and effector translocation. Deletion of pcrV in a cytotoxic strain did not affect secretion of PopB and PopD but abolished hemolytic activity and translocation of effectors into fibroblasts. Notably, the PcrV-deficient mutant was not capable of inserting PopD into host cell membranes, whereas PopB and PopD, but not PcrV, were readily found within membranes of wild-type-infected RBCs. Immunoprecipitation experiments performed by using a liposome model of pore assembly revealed a direct interaction between PopD and PopB but not between PopD and PcrV. Consequently, PcrV is necessary for the functional assembly of the PopB/D translocon complex but does not interact directly with pore-forming Pop proteins.

scholarly journals Murine bubblegum orthologue is a microsomal very long-chain acyl-CoA synthetase

2004 ◽  
Vol 377 (1) ◽  
pp. 85-93 ◽  
Author(s):  
Peter FRAISL ◽  
Sonja FORSS-PETTER ◽  
Mihaela ZIGMAN ◽  
Johannes BERGER
Keyword(s):  
Fluorescent Protein ◽  
Neurodegenerative Disorder ◽  
Direct Interaction ◽  
Confocal Laser ◽  
Synthetase Activity ◽  
Wild Type ◽  
Protein Fusion ◽  
Chain Acyl ◽  
Green Fluorescent ◽  
Long Chain

It has been suggested that a gene termed bubblegum (Bgm), encoding an acyl-CoA synthetase, could be involved in the pathogenesis of the inherited neurodegenerative disorder X-ALD (X-linked adrenoleukodystrophy). The precise function of the ALDP (ALD protein) still remains unclear. Aldp deficiency in mammals and Bgm deficiency in Drosophila led to accumulation of VLCFAs (very long-chain fatty acids). As a first step towards studying this interaction in wild-type versus Aldp-deficient mice, we analysed the expression pattern of the murine orthologue of the Bgm gene. In contrast with the ubiquitously expressed Ald gene, Bgm expression is restricted to the tissues that are affected by X-ALD such as brain, testis and adrenals. During mouse brain development, Bgm mRNA was first detected by Northern-blot analysis on embryonic day 18 and increased steadily towards adulthood, whereas the highest level of Ald mRNA was found on embryonic day 12 and decreased gradually during differentiation. Protein fractionation and confocal laser imaging of Bgm–green fluorescent protein fusion proteins revealed a microsomal localization that was different from peroxisomes (where Aldp is detected), endoplasmic reticulum and Golgi. Mouse Bgm showed acyl-CoA synthetase activity towards a VLCFA substrate in addition to LCFAs, and this activity was enriched in the microsomal compartment. Speculating that Bgm expression could be regulated by Ald deficiency, we compared the abundance of Bgm mRNA in wild-type and Ald knockout mice but observed no difference. Although mouse Bgm is capable of activating VLCFA, we conclude that a direct interaction between the mouse Bgm and the Aldp seems unlikely.

scholarly journals Gemin4

2000 ◽  
Vol 148 (6) ◽  
pp. 1177-1186 ◽  
Author(s):  
Bernard Charroux ◽  
Livio Pellizzoni ◽  
Robert A. Perkinson ◽  
Jeongsik Yong ◽  
Andrej Shevchenko ◽  
...  
Keyword(s):  
Motor Neurons ◽  
Muscular Atrophy ◽  
Critical Role ◽  
Direct Interaction ◽  
Nuclear Bodies ◽  
Dead Box ◽  
Core Proteins ◽  
Smn Complex ◽  
Smn Protein

The survival of motor neurons (SMN) protein, the product of the neurodegenerative disease spinal muscular atrophy (SMA) gene, is localized both in the cytoplasm and in discrete nuclear bodies called gems. In both compartments SMN is part of a large complex that contains several proteins including Gemin2 (formerly SIP1) and the DEAD box protein Gemin3. In the cytoplasm, the SMN complex is associated with snRNP Sm core proteins and plays a critical role in spliceosomal snRNP assembly. In the nucleus, SMN is required for pre-mRNA splicing by serving in the regeneration of spliceosomes. These functions are likely impaired in cells of SMA patients because they have reduced levels of functional SMN. Here, we report the identification by nanoelectrospray mass spectrometry of a novel component of the SMN complex that we name Gemin4. Gemin4 is associated in vivo with the SMN complex through a direct interaction with Gemin3. The tight interaction of Gemin4 with Gemin3 suggests that it could serve as a cofactor of this DEAD box protein. Gemin4 also interacts directly with several of the Sm core proteins. Monoclonal antibodies against Gemin4 efficiently immunoprecipitate the spliceosomal U snRNAs U1 and U5 from Xenopus oocytes cytoplasm. Immunolocalization experiments show that Gemin4 is colocalized with SMN in the cytoplasm and in gems. Interestingly, Gemin4 is also detected in the nucleoli, suggesting that the SMN complex may also function in preribosomal RNA processing or ribosome assembly.

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