Journal articles: 'Anti-SRP'

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Suzuki, Shigeaki. "Anti-SRP myopathy." Rinsho Shinkeigaku 51, no. 11 (2011): 961–63. http://dx.doi.org/10.5692/clinicalneurol.51.961.

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Dandasena, Tarini, Vaibhav Ingle, Abhishek Singhai, and Saurabh Saigal. "Anti-SRP-positive necrotising myopathy concurrent with breast malignancy." BMJ Case Reports 16, no. 12 (December 2023): e254702. http://dx.doi.org/10.1136/bcr-2023-254702.

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Anti-signal recognition particle (anti-SRP)-positive necrotising myopathy causes severe progressive proximal weakness with a propensity to involve pharyngeal, laryngeal and respiratory muscles. It is one of the aggressive inflammatory myopathies. First-line treatment is with high-dose steroids followed by other immunosuppressants, but this conventional therapy is often ineffective. Second-line treatment involves use of either rituximab or intravenous immunonoglobulin (IVIG). Anti-SRP-positive necrotising myopathy is frequently treated as refractory myositis due to its poor responsiveness to steroid monotherapy and conventional immunosuppressive therapies. Therefore, anti-SRP-positive necrotising myopathy differs from immune-mediated myopathy. Although anti-SRP autoantibody is found in only 4–6% of patients with idiopathic inflammatory myopathy, the actual proportion of patients with refractory anti-SRP-positive necrotising myopathy is unknown. We describe a patient with multiple comorbidities who had subacute-onset anti-SRP-positive immune-mediated necrotising myopathy (IMNM). After failing steroids, methotrexate and IVIG therapy, she made a considerable recovery with rituximab. She was later diagnosed to have breast malignancy. Malignancy-associated anti-SRP-positive IMNM is rarely reported.

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Allenbach, Yves, Louiza Arouche-Delaperche, Corinna Preusse, Helena Radbruch, Gillian Butler-Browne, Nicolas Champtiaux, Kuberaka Mariampillai, et al. "Necrosis in anti-SRP+ and anti-HMGCR+myopathies." Neurology 90, no. 6 (January 12, 2018): e507-e517. http://dx.doi.org/10.1212/wnl.0000000000004923.

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ObjectiveTo characterize muscle fiber necrosis in immune-mediated necrotizing myopathies (IMNM) with anti–signal recognition particle (SRP) or anti–3-hydroxy-3-methylglutarylcoenzyme A reductase (HMGCR) antibodies and to explore its underlying molecular immune mechanisms.MethodsMuscle biopsies from patients with IMNM were analyzed and compared to biopsies from control patients with myositis. In addition to immunostaining and reverse transcription PCR on muscle samples, in vitro immunostaining on primary muscle cells was performed.ResultsCreatine kinase levels and muscle regeneration correlated with the proportion of necrotic fibers (r = 0.6, p < 0.001). CD68+iNOS+ macrophages and a Th-1 immune environment were chiefly involved in ongoing myophagocytosis of necrotic fibers. T-cell densities correlated with necrosis but no signs of cytotoxicity were detected. Activation of the classical pathway of the complement cascade, accompanied by deposition of sarcolemmal immunoglobulins, featured involvement of humoral immunity. Presence of SRP and HMGCR proteins on altered myofibers was reproduced on myotubes exposed to purified patient-derived autoantibodies. Finally, a correlation between sarcolemmal complement deposits and fiber necrosis was observed (r = 0.4 and p = 0.004). Based on these observations, we propose to update the pathologic criteria of IMNM.ConclusionThese data further corroborate the pathogenic role of anti-SRP and anti-HMGCR autoantibodies in IMNM, highlighting humoral mechanisms as key players in immunity and myofiber necrosis.

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Suzuki, Shigeaki. "Anti-SRP myopathy: different entity from myositis." Rinsho Shinkeigaku 52, no. 11 (2012): 1148–50. http://dx.doi.org/10.5692/clinicalneurol.52.1148.

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Zhuo, De-Bing, and Hui Cao. "Fast Sound Source Localization Based on SRP-PHAT Using Density Peaks Clustering." Applied Sciences 11, no. 1 (January 5, 2021): 445. http://dx.doi.org/10.3390/app11010445.

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Sound source localization has been increasingly used recently. Among the existing techniques of sound source localization, the steered response power–phase transform (SRP-PHAT) exhibits considerable advantages regarding anti-noise and anti-reverberation. When applied in real-time situations, however, the heavy computational load makes it impossible to localize the sound source in a reasonable time since SRP-PHAT employs a grid search scheme. To solve the problem, an improved procedure called ODB-SRP-PHAT, i.e., steered response power and phase transformation with an offline database (ODB), was proposed by the authors. The basic idea of ODB-SRP-PHAT is to determine the possible sound source positions using SRP-PHAT and density peak clustering before real-time localization and store the identified positions in an ODB. Then, at the online positioning stage, only the power values of the positions in the ODB will be calculated. When used in real-time monitoring, e.g., locating the speaker in a video conference, the computational load of ODB-SRP-PHAT is significantly smaller than that of SRP-PHAT. Simulations and experiments under a real environment verified the high localization accuracy with a small computational load of ODB-SRP-PHAT. In addition, the advantages of anti-noise and anti-reverberation remained. The suggested procedure displayed good applicability in a real environment.

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Martínez-Rodríguez, Pablo, María Escribano-Iglesias, Ángel-P. Crisolino-Pozas, Noelia Cubino-Boveda, Miriam López-Parra, Miguel Marcos, and Antonio-J. Chamorro. "Plasma Exchange in Anti-Signal Recognition Particle Myopathy: A Systematic Review and Combined Analysis of Patient Individual Data." Journal of Personalized Medicine 14, no. 5 (April 27, 2024): 461. http://dx.doi.org/10.3390/jpm14050461.

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Anti-signal recognition particle myopathy (anti-SRP myopathy) is a rare subtype of immune-mediated inflammatory myopathy characterized by muscle weakness and anti-SRP autoantibodies. Although plasma exchange (PE) is used in severe cases, its role remains unclear. A systematic review was conducted following PRISMA guidelines, identifying 23 patients with anti-SRP myopathy treated with PE. Data on demographics, clinical features, laboratory findings, treatments, and outcomes were analyzed combining individual patient data if available. Sixteen (69.6%) patients were male, with muscle weakness as the predominant symptom in 100% of cases. After PE, most patients showed improvement in symptoms, and the proportion of patients with muscle weakness was reduced (p = 0.001). Relapse occurred in 17.4% of the cases. The incidence of adverse events was low (8.7%). Despite limitations, including a small sample size and heterogeneous data, our systematic review suggests that PE may be effective in inducing remission and controlling symptoms in anti-SRP myopathy, particularly in severe cases. Since evidence on PE in anti-SRP myopathy is limited, further research, including prospective multicenter studies, is warranted to understand better its efficacy and safety and establish its role in treatment algorithms.

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Shinde, Ujwala A., and Shivkumar S. Kanojiya. "Serratiopeptidase Niosomal Gel with Potential in Topical Delivery." Journal of Pharmaceutics 2014 (March 20, 2014): 1–9. http://dx.doi.org/10.1155/2014/382959.

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The objective of present study was to develop nonionic surfactant vesicles of proteolytic enzyme serratiopeptidase (SRP) by adapting reverse phase evaporation (REV) technique and to evaluate the viability of SRP niosomal gel in treating the topical inflammation. The feasibility of SRP niosomes by REV method using Span 40 and cholesterol has been successfully demonstrated in this investigation. The entrapment efficiency was found to be influenced by the molar ratio of Span 40 : cholesterol and concentration of SRP in noisome. The developed niosomes were characterized for morphology, particle size, and in vitro release. Niosomal gel was prepared by dispersing xanthan gum into optimized batch of SRP niosomes. Ex vivo permeation and in vivo anti-inflammatory efficacy of gel formulation were evaluated topically. SRP niosomes obtained were round in nanosize range. At Span 40 : cholesterol molar ratio 1 : 1 entrapment efficiency was maximum, that is, 54.82% ± 2.08, and showed consistent release pattern. Furthermore ex vivo skin permeation revealed that there was fourfold increase in a steady state flux when SRP was formulated in niosomes and a significant increase in the permeation of SRP, from SRP niosomal gel containing permeation enhancer. In vivo efficacy studies indicated that SRP niosomal gel had a comparable topical anti-inflammatory activity to that of dicolfenac gel.

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Bergua, Cécile, Hélène Chiavelli, Yves Allenbach, Louiza Arouche-Delaperche, Christophe Arnoult, Gwladys Bourdenet, Laetitia Jean, et al. "In vivo pathogenicity of IgG from patients with anti-SRP or anti-HMGCR autoantibodies in immune-mediated necrotising myopathy." Annals of the Rheumatic Diseases 78, no. 1 (October 11, 2018): 131–39. http://dx.doi.org/10.1136/annrheumdis-2018-213518.

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ObjectivesIn autoimmunity, autoantibodies (aAb) may be simple biomarkers of disease or true pathogenic effectors. A form of idiopathic inflammatory myopathy associated with anti-signal recognition particle (SRP) or anti-3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR) aAb has been individualised and is referred to as immune-mediated necrotising myopathy (IMNM). The level of aAb correlates with IMNM activity and disease may respond to immunosuppression, suggesting that they are pathogenic. We aimed to evaluate the pathogenicity of IgG from patients with anti-SRP or anti-HMGCR aAb in vivo by developing the first mouse model of IMNM.MethodsIgG from patients suffering from anti-SRP or anti-HMGCR associated IMNM were passively transferred to wild-type, Rag2-/- or complement C3-/- mice. Muscle deficiency was evaluated by muscle strength on electrostimulation and grip test. Histological analyses were performed after haematoxylin/eosin staining or by immunofluorescence or immunohistochemistry analysis. Antibody levels were quantified by addressable laser bead assay (ALBIA).ResultsPassive transfer of IgG from patients suffering from IMNM to C57BL/6 or Rag2-/- mice provoked muscle deficiency. Pathogenicity of aAb was reduced in C3-/- mice while increased by supplementation with human complement. Breakage of tolerance by active immunisation with SRP or HMGCR provoked disease.ConclusionThis study demonstrates that patient-derived anti-SRP+ and anti-HMGCR+ IgG are pathogenic towards muscle in vivo through a complement-mediated mechanism, definitively establishing the autoimmune character of IMNM. These data support the use of plasma exchanges and argue for evaluating complement-targeting therapies in IMNM.

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Eura, N., T. Shiota, M. Ozaki, N. Iguchi, Y. Uchihara, H. Nanaura, K. Fukushima, et al. "P.11Clinicopathological difference between anti-SRP and anti-HMGCR myopathy." Neuromuscular Disorders 29 (October 2019): S44. http://dx.doi.org/10.1016/j.nmd.2019.06.040.

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Botos, Balázs, Melinda Nagy-Vincze, and Katalin Dankó. "Anti-SRP-pozitív myositises betegeink klinikai sajátosságai és terápiára adott válaszuk." Orvosi Hetilap 158, no. 35 (September 2017): 1382–89. http://dx.doi.org/10.1556/650.2017.30827.

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Abstract: Introduction: Idiopathic inflammatory myopathies are a group of clinically heterogeneous diseases, which have been classified by myositis specific antibodies recently. The anti-SRP positive subset of this group is characterized by more severe clinical prognosis than other myositis specific antibody positive types. Aim: Our goal was to compare 16 anti-SRP positive patients in the Division of Clinical Immunology, Department of Internal Medicine, University of Debrecen with 16 antibody negative ones. Method: Muscle strength validated in both groups by the manual muscle test proved to be significantly decreased both before and after therapy (χ2 = 0.006 and 0.019) in the anti-SRP positive group. Results: Muscle-specific inflammatory laboratory parameters showed significant difference only in case of LDH-levels after therapy. Both groups showed good clinical response to first line steroid treatment, yet the significantly higher rate of second line administration suggests worse therapeutic response of the antibody positive group. Conclusion: Based on these facts we determined poor clinical prognosis and therapeutic response of the anti-SRP positive group. Orv Hetil. 2017; 158(35): 1382–1389.

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SCHIAPPACASSE POYANCO, GIANNI. "Miopatías Necrotizantes Autoinmunes: Reconocimiento como nuevo subgrupo de Miopatía Inflamatoria Idiopática." Revista Chilena de Reumatología 35, no. 2 (July 24, 2023): 44–54. http://dx.doi.org/10.58450/rcr.v35i2.45.

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Miopatía Necrotizante Autoinmune (MNA) fue reconocida como nuevo subgrupo de miositis luego de observar en biopsias musculares la presencia de necrosis con escaso o ausente infiltrado inflamatorio, sumado a la expresión de dos anticuerpos específicos de miositis (Anticuerpo anti Partícula de Reconocimiento de Señal, anti-SRP; y Anticuerpo anti Hidroxi-3-metilglutaril-CoA reductasa, anti-HM- GCR), ambos fuertemente asociados al hallazgo histológico descrito y a fenotipos clínicos característicos a cada anticuerpo, los cuales comparten importantes similitudes representadas por severa debilidad muscular proximal, gran elevación de creatinkinasa (CK), escasa manifestación de síntomas y signos extramusculares, y resistencia al uso de inmunosupresión habitual. Si bien en primera instancia los criterios de clasificación propuestos estaban basados en la histología, la observación de necrosis en otros subgrupos de miositis, sumado a la homogeneidad del comportamiento clínico de pacientes que expresaban anticuerpos anti-SRP o anti-HMGCR independiente de la histología presentada, llevó en el año 2016 al Grupo de Trabajo del Centro Europeo Neuromuscular (ENMC) a establecer criterios diagnósticos de MNA basados en el comportamiento clínico (debilidad muscular proximal con CK total elevada) más la presencia del anticuerpo respectivo (anti-SRP o anti-HMGCR), reservando la necesidad de realizar biopsia muscular en el caso que la serología resulte negativa, siendo así reconocidas tres entidades distintas de MNA: Miopatía anti-SRP, Miopatía anti-HMGCR y Miopatía Necroti- zante seronegativa. La presente revisión expresa el actual conocimiento de MNA y sus subtipos, refiriéndose a aspectos históricos, clínicos, histológicos, inmuno- patológicos, y de pronóstico y tratamiento.

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Rodríguez-Muguruza, S., I. Lozano-Ramos, A. Hernández-Gallego, I. Ojanguren, A. Riveros-Frutos, S. Holgado, L. Mateo, et al. "AB0642 Are Anti-Srp Autoantibodies Specific for Myositis?" Annals of the Rheumatic Diseases 73, Suppl 2 (June 2014): 1017.4–1018. http://dx.doi.org/10.1136/annrheumdis-2014-eular.3621.

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Pruna, L., F. Maurier, and P. Kaminsky. "L’étrange destin des polymyosites à anticorps anti-SRP." La Revue de Médecine Interne 30 (June 2009): S97. http://dx.doi.org/10.1016/j.revmed.2009.03.190.

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Farah, Kchaou, Nadia Bouattour, Khadija Moalla, Salma Sakka, Sawsan Daoud, Nouha Farhat, Mariem Damak, and Chokri Mhiri. "Immune-mediated necrotizing myopathy with anti-SRP autoantibodies." Journal of the Neurological Sciences 455 (December 2023): 122524. http://dx.doi.org/10.1016/j.jns.2023.122524.

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MOLL, Ralf G. "Protein–protein, protein–RNA and protein–lipid interactions of signal-recognition particle components in the hyperthermoacidophilic archaeon Acidianus ambivalens." Biochemical Journal 374, no. 1 (August 15, 2003): 247–54. http://dx.doi.org/10.1042/bj20030475.

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The signal-recognition particle (SRP) of one of the most acidophilic and hyperthermophilic archaeal cells, Acidianus ambivalens, and its putative receptor component, FtsY (prokaryotic SRP receptor), were investigated in detail. A. ambivalens Ffh (fifty-four-homologous protein) was shown to be a soluble protein with strong affinity to membranes. In its membrane-residing form, Ffh was extracted from plasma membranes with chaotropic agents like urea, but not with agents diminishing electrostatic interactions. Using unilamellar tetraether phospholipid vesicles, both Ffh and FtsY associate independently from each other in the absence of other factors, suggesting an equilibrium of soluble and membrane-bound protein forms under in vivo conditions. The Ffh protein precipitated from cytosolic cell supernatants with anti-Ffh antibodies, together with an 7 S-alike SRP–RNA, suggesting a stable core ribonucleoprotein composed of both components under native conditions. The SRP RNA of A. ambivalens depicted a size of about 309 nucleotides like the SRP RNA of the related organism Sulfolobus acidocaldarius. A stable heterodimeric complex composed of Ffh and FtsY was absent in cytosolic super-natants, indicating a transiently formed complex during archaeal SRP targeting. The FtsY protein precipitated in cytosolic super-natants with anti-FtsY antisera as a homomeric protein lacking accessory protein components. However, under in vitro conditions, recombinantly generated Ffh and FtsY associate in a nucleotide-independent manner, supporting a structural receptor model with two interacting apoproteins.

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Li, James P., Kae Yol Lee, Ta-Min Chang, and William Y. Chey. "MEK inhibits secretin release and pancreatic secretion: roles of secretin-releasing peptide and somatostatin." American Journal of Physiology-Gastrointestinal and Liver Physiology 280, no. 5 (May 1, 2001): G890—G896. http://dx.doi.org/10.1152/ajpgi.2001.280.5.g890.

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We investigated the mechanism of action of methionine enkephalin (MEK) on HCl-stimulated secretin release and pancreatic exocrine secretion. Anesthetized rats with pancreatobiliary cannulas and isolated upper small intestinal loops were perfused intraduodenally with 0.01 N HCl while bile and pancreatic juice were diverted. The effect of intravenous MEK on acid-stimulated secretin release and pancreatic exocrine secretion was then studied with or without coinfusion of naloxone, an anti-somatostatin (SS) serum, or normal rabbit serum. Duodenal acid perfusate, which contains secretin-releasing peptide (SRP) activity, was collected from donor rats with or without pretreatment with MEK, MEK + naloxone, or MEK + anti-SS serum, concentrated by ultrafiltration, and neutralized. The concentrated acid perfusate (CAP), which contains SRP bioactivity, was infused intraduodenally into recipient rats. MEK increased plasma SS concentration and inhibited secretin release and pancreatic fluid and bicarbonate secretion dose-dependently. The inhibition was partially reversed by naloxone and anti-SS serum but not by normal rabbit serum. In recipient rats, CAP increased plasma secretin level and pancreatic secretion. CAP SRP bioactivity decreased when it was collected from MEK-treated donor rats; this was partially reversed by coinfusion with naloxone or anti-SS serum. These results suggest that in the rat, MEK inhibition of acid-stimulated pancreatic secretion and secretin release involves suppression of SRP activity release. Thus the MEK inhibitory effect appears to be mediated in part by endogenous SS.

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Picard, Cécile, Thierry Vincent, Jean-Christophe Lega, Sophie Hue, Françoise Fortenfant, Daniela Lakomy, René-Louis Humbel, et al. "Heterogeneous clinical spectrum of anti-SRP myositis and importance of the methods of detection of anti-SRP autoantibodies: a multicentric study." Immunologic Research 64, no. 3 (January 7, 2016): 677–86. http://dx.doi.org/10.1007/s12026-015-8774-6.

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Watanabe, Yurika, Akinori Uruha, Shigeaki Suzuki, Jin Nakahara, Kohei Hamanaka, Kazuko Takayama, Norihiro Suzuki, and Ichizo Nishino. "Clinical features and prognosis in anti-SRP and anti-HMGCR necrotising myopathy." Journal of Neurology, Neurosurgery & Psychiatry 87, no. 10 (May 4, 2016): 1038–44. http://dx.doi.org/10.1136/jnnp-2016-313166.

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Abbasov, F. A., G. V. Zemtsova, P. A. Popov, K. I. Chekhonatskaya, D. V. Kukhno, M. M. Severova, M. V. Shmyreva, A. A. Kindarova, and D. Yu Schekochikhin. "Anti-SRP antibody-associated necrotizing myopathy: 2 clinical cases." Neuromuscular Diseases 13, no. 2 (June 16, 2023): 72–82. http://dx.doi.org/10.17650/2222-8721-2023-13-2-72-82.

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Necrotizing myopathies are a subtype of autoimmune myopathies characterized by muscle fiber necrosis with minimal infiltration by inflammatory cells on muscle biopsy. This group of myopathies is defined by flaccid palsies due to prima‑ ry skeletal muscle damage as well as extramuscular manifestations such as fever, rash, arthritis, Raynaud’s syndrome and interstitial lung disease. The presence of anti-SRP antibodies is associated with rapidly progressive refractory myositis predominantly affecting limb muscles and axial muscles.Objective of the work is to analyze the course of severe, refractory to several lines of immunosuppressive therapies anti-SRP associated necrotizing myopathy and to highlight an adequate treatment regime.Necrotizing myopathy was suspected in patients aged 39 and 56 years with rapidly progressive flaccid tetraparesis on the basis of clinical and anamnestic data, the results of needle electromyography and muscle magnetic resonance imaging, as well as the analysis of myositis-specific and myositis-associated autoantibodies. In both cases, a rapid development of atrophies, marked muscle weakness in the limbs, without involvement of the bulbar musculature, was observed. To achieve effective control of the disease progression, several lines of therapy were required: glucocorticosteroids, intravenous immunoglobulins, methotrexate and rituximab. Our observations are consistent with those in the literature.Our observations illustrate the clinical course of severe myopathy associated with anti-SRP antibodies. Early initiation of aggressive immunosuppression is crucial to control the disease progression. Treatment and rehabilitation allow achieving significant improvement of the patient’s condition.

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Rehman, Attique ur, Marryam Riaz, Moeez Ansari, Saqib Naeem Sidiqui, Adeel Ijaz Rana, and Yousaf Athar. "Comparison of Clinical Attachment Level Gain Using Scaling Root Planing Versus Adjunctive Azithromycin on Chronic Periodontitis." Pakistan Journal of Medical and Health Sciences 15, no. 8 (August 26, 2021): 2054–56. http://dx.doi.org/10.53350/pjmhs211582054.

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Objective: The objective of the study was to compare the mean clinical attachment gain in patients of chronic periodontitis after scaling and root alone versus Azithromycin as an adjunct to scaling and root. Study Design Comparative study Place and Duration: Conducted at Operative Dentistry Department, Azra Naheed Dental College, Lahore for a duration of 4 months from December 2019 to March 2020. Methodology: Total Sixty patients fulfilling the selection criteria were randomly allocated to SRP and SRP+Az groups. In both groups, conventional scaling and root planing was done. In the SRP group placebo capsules were prescribed, while in the SRP+Az group, Azithromycin (500mg) once daily was prescribed for 3 days. Clinical attachment level (CAL) was measured initially and after 5 weeks. Data was analyzed in SPSS version 19.0 using independent sample t-test. Results: Both groups showed gain in CAL compared to baseline. However, SRP+Az group showed significantly more gain in CAL in comparison to SRP group (P value < 0.05). Conclusion: Use of Azithromycin adjunctive to SRP is an effective treatment modality in chronic periodontitis patients. Keywords: Anti‐Bacterial Agents, Azithromycin, Chronic periodontitis, Clinical attachment level, Periodontal Debridement, Scaling and root planing,

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Verwaerde, Claudie, C. Auriault, Martine Damonneville, J. M. Grzych, R. Pierce, and A. Capron. "IgG response of rats and humans to the released products of schistosomula of Schistosoma mansoni." Parasitology 90, no. 3 (June 1985): 509–18. http://dx.doi.org/10.1017/s0031182000055505.

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The participation of products released from Schistosoma mansoni schistosomula (SRP-A) in the IgG antibody response of infected Brown-Norway rats and infected humans has been studied using immunoprecipitation with various antigenic preparations and in in vitro cytotoxicity assays. A large number of SRP-A molecules with a wide range of molecular weights was recognized by infected rat and human sera. Anti-SRP-A antibodies appeared in rat sera from day 28 after infection. In infected humans, a variable pattern of SRP-A recognition was observed between individuals. IgG antibodies obtained by immunization of rats with SRP-A without addition of adjuvants reacted with 3 major schistosomula surface proteins with molecular weights of 38, 32 and 21 kDa. These latter molecules were also revealed strongly by infected rat sera. Moreover, these antibodies were able to kill schistosomula in vitro in the presence of complement or eosinophils.

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Wendling, Daniel, Xavier Guillot, Marie Godfrin-Valnet, and Clément Prati. "Usefulness of anti-SRP antibody testing in inflammatory myopathies." Joint Bone Spine 81, no. 6 (December 2014): 548–49. http://dx.doi.org/10.1016/j.jbspin.2014.03.013.

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Maurousset, Aude, Philippe Corcia, Bertrand De Toffol, Jean-Michel Vallat, Anne-Marie Guennoc, and Julien Biberon. "Présentation SLA-like d’une myopathie nécrosante à anti-SRP." Revue Neurologique 171 (April 2015): A158. http://dx.doi.org/10.1016/j.neurol.2015.01.362.

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Suzuki, S., Y. Hayashi, M. Kuwana, R. Tsuburaya, N. Suzuki, and I. Nishino. "Anti-SRP Myopathy: Disease Progression and Neurological Outcome (PD6.010)." Neurology 78, Meeting Abstracts 1 (April 22, 2012): PD6.010. http://dx.doi.org/10.1212/wnl.78.1_meetingabstracts.pd6.010.

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Bleunven, Christophe, Susan Treves, Xia Jinyu, Elisa Leo, Michel Ronjat, Michel De Waard, Georg Kern, Bernhard E. Flucher, and Francesco Zorzato. "SRP-27 is a novel component of the supramolecular signalling complex involved in skeletal muscle excitation–contraction coupling." Biochemical Journal 411, no. 2 (March 27, 2008): 343–49. http://dx.doi.org/10.1042/bj20070906.

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SRP-27 (sarcoplasmic reticulum protein of 27 kDa) is a newly identified integral membrane protein constituent of the skeletal muscle SR (sarcoplasmic reticulum). We identified its primary structure from cDNA clones isolated from a mouse skeletal muscle cDNA library. ESTs (expressed sequence tags) of SRP-27 were found mainly in cDNA libraries from excitable tissues of mouse. Western blot analysis confirmed the expression of SRP-27 in skeletal muscle and, to a lower extent, in heart and brain. Mild trypsin proteolysis combined with primary-structure prediction analysis suggested that SRP-27 has four transmembrane-spanning alpha helices and its C-terminal domain faces the cytoplasmic side of the endo(sarco)plasmic reticulum. The expression of SRP-27 is higher in fast twitch skeletal muscles compared to slow twitch muscles and peaks during the first month of post-natal development. High-resolution immunohistochemistry and Western blot analysis of subcellular fractions indicated that SRP-27 is distributed in both longitudinal tubules and terminal cisternae of the SR, as well as in the perinuclear membrane systems and the nuclear envelope of myotubes and adult fibres. SRP-27 co-sediments with the RyR (ryanodine receptor) macromolecular complex in high-salt sucrose-gradient centrifugation, and is pulled-down by anti-RyR as well as by maurocalcin, a well characterized RyR modulator. Our results indicate that SRP-27 is part of a SR supramolecular complex, suggesting the involvement of SRP-27 in the structural organization or function of the molecular machinery underlying excitation–contraction coupling.

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Soares, Izadora Fonseca Zaiden, Victoria Fernandez Comprido, Bianca Raquel Ruoh Harn Scovoli Hsu, and Alzira Alves de Siqueira Carvalho. "Immune-mediated necrotising myopathy in asymptomatic patients with high creatine kinase." BMJ Case Reports 13, no. 10 (October 2020): e235457. http://dx.doi.org/10.1136/bcr-2020-235457.

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Subacute symmetrical proximal muscle weakness and persistent elevated creatine kinase levels are typical of immune-mediated necrotising myopathy (IMNM). These conditions are accompanied by copious myofibre necrosis, degeneration and regeneration with minimal to no inflammation on muscle biopsy. We report two cases (case 1 and case 2) of asymptomatic IMNM from different families with hyperCKaemia associated with positive anti-signal recognition particle (SRP) and anti-3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR) antibodies, respectively, and we also reviewed the literature. There are only a few previous descriptions of patients with asymptomatic IMNM.The disease onset could be insidious and lead to delayed diagnosis and treatment. We recommend testing for the anti-HMGCR and anti-SRP antibodies in patients with idiopathic hyperCKaemia because they could show no symptoms of this disorder.

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Ocaña Pérez, E., M. Romero Jurado, A. M. Peña Casas, and A. Martínez Cañamero. "Presencia de anticuerpos anti-SRP y anti-M2 en paciente con polimiositis severa." Revista Clínica Española 213, no. 9 (December 2013): e91-e93. http://dx.doi.org/10.1016/j.rce.2013.07.013.

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Sugie, Kazuma, Yasuyo Tonomura, and Satoshi Ueno. "Characterization of Dermatomyositis with Coexistence of Anti-Jo-1 and Anti-SRP Antibodies." Internal Medicine 51, no. 7 (2012): 799–802. http://dx.doi.org/10.2169/internalmedicine.51.6566.

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Guo, Yunlong, Meihong Liu, Xin Liu, Mingzhu Zheng, Xiuying Xu, Xiaokang Liu, Jiyu Gong, Huimin Liu, and Jingsheng Liu. "Metagenomic and Untargeted Metabolomic Analysis of the Effect of Sporisorium reilianum Polysaccharide on Improving Obesity." Foods 12, no. 8 (April 7, 2023): 1578. http://dx.doi.org/10.3390/foods12081578.

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Gut microbiota plays an important role in the pathophysiology of obesity. Fungal polysaccharide can improve obesity, but the potential mechanism needs further study. This experiment studied the potential mechanism of polysaccharides from Sporisorium reilianum (SRP) to improve obesity in male Sprague Dawley (SD) rats fed with a high-fat diet (HFD) using metagenomics and untargeted metabolomics. After 8 weeks of SRP (100, 200, and 400 mg/kg/day) intervention, we analyzed the related index of obesity, gut microbiota, and untargeted metabolomics of rats. The obesity and serum lipid levels of rats treated with SRP were reduced, and lipid accumulation in the liver and adipocyte hypertrophy was improved, especially in rats treated with a high dose of SRP. SRP improved the composition and function of gut microbiota in rats fed with a high-fat diet, and decreased the ratio of Firmicutes to Bacteroides at the phylum level. At the genus level, the abundance of Lactobacillus increased and that of Bacteroides decreased. At the species level, the abundance of Lactobacillus crispatus, Lactobacillus helveticus, and Lactobacillus acidophilus increased, while the abundance of Lactobacillus reuteri and Staphylococcus xylosus decreased. The function of gut microbiota mainly regulated lipid metabolism and amino acid metabolism. The untargeted metabolomics indicated that 36 metabolites were related to the anti-obesity effect of SRP. Furthermore, linoleic acid metabolism, phenylalanine, tyrosine, and tryptophan biosynthesis, and the phenylalanine metabolism pathway played a role in improving obesity in those treated with SRP. The study results suggest that SRP significantly alleviated obesity via gut-microbiota-related metabolic pathways, and SRP could be used for the prevention and treatment of obesity.

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Mehta, Puja, Rachel Dorsey-Campbell, Pooja Dassan, Catherine Nelson-Piercy, and Stuart Viegas. "Difficult case: rituximab in anti-SRP antibody myositis in pregnancy." Practical Neurology 19, no. 5 (April 12, 2019): 444–46. http://dx.doi.org/10.1136/practneurol-2018-002168.

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A 30-year-old nulliparous woman presented at 15-week gestation with severe skeletal and respiratory muscle weakness, having been diagnosed with anti-signal recognition particle antibody myositis 3 years before. Remission had previously been induced with rituximab (after failure of standard therapies). She had continued oral prednisolone and rituximab every 6 months but had stopped this when planning pregnancy. At 16-weeks gestation, she restarted corticosteroids and rituximab, with clinical and biochemical recovery and no complications. Rituximab should ideally be given in the first trimester; treatment later in pregnancy increases the risk of neonatal B-cell depletion and cytopenias. The fetal risk from drug therapy must be weighed against the risk to mother and fetus from untreated disease. This report highlights the importance of preconception counselling for disease control and patient education regarding medication safety and early referral to obstetric medicine clinics, to facilitate complex clinical decision-making.

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Pinal-Fernandez, Iago, Maria Casal-Dominguez, John A. Carrino, Arash H. Lahouti, Pari Basharat, Jemima Albayda, Julie J. Paik, et al. "Thigh muscle MRI in immune-mediated necrotising myopathy: extensive oedema, early muscle damage and role of anti-SRP autoantibodies as a marker of severity." Annals of the Rheumatic Diseases 76, no. 4 (September 20, 2016): 681–87. http://dx.doi.org/10.1136/annrheumdis-2016-210198.

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ObjectivesThe aims of this study were to define the pattern of muscle involvement in patients with immune-mediated necrotising myopathy (IMNM) relative to those with other inflammatory myopathies and to compare patients with IMNM with different autoantibodies.MethodsAll Johns Hopkins Myositis Longitudinal Cohort subjects with a thigh MRI (tMRI) who fulfilled criteria for IMNM, dermatomyositis (DM), polymyositis (PM), inclusion body myositis (IBM) or clinically amyopathic DM (CADM) were included in the study. Muscles were assessed for intramuscular and fascial oedema, atrophy and fatty replacement. Disease subgroups were compared using univariate and multivariate analyses. Patients with IMNM with anti-signal recognition particle (SRP) autoantibodies were compared with those with IMNM with anti-HMG-CoA reductase (HMGCR) autoantibodies.ResultsThe study included 666 subjects (101 IMNM, 176 PM, 219 DM, 17 CADM and 153 IBM). Compared with DM or PM, IMNM was characterised by a higher proportion of thigh muscles with oedema, atrophy and fatty replacement (p<0.01). Patients with IMNM with anti-SRP had more atrophy (19%, p=0.003) and fatty replacement (18%, p=0.04) than those with anti-HMGCR. In IMNM, muscle abnormalities were especially common in the lateral rotator and gluteal groups. Fascial involvement was most widespread in DM. Fatty replacement of muscle tissue began early during the course of disease in IMNM and the other groups. An optimal combination of tMRI features had only a 55% positive predictive value for diagnosing IMNM.ConclusionsCompared with patients with DM or PM, IMNM is characterised by more widespread muscle involvement. Anti-SRP-positive patients have more severe muscle involvement than anti-HMGCR-positive patients.

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Tanaka, Mariko, Naoki Gamou, Hirohiko Shizukawa, Emiko Tsuda, and Shun Shimohama. "Myopericarditis in a case of anti-signal recognition particle (anti-SRP) antibody-positive myopathy." Rinsho Shinkeigaku 56, no. 12 (2016): 862–65. http://dx.doi.org/10.5692/clinicalneurol.cn-000916.

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THORNTON, A. B., D. U. THOMSON, G. H. LONERAGAN, J. T. FOX, D. T. BURKHARDT, D. A. EMERY, and T. G. NAGARAJA. "Effects of a Siderophore Receptor and Porin Proteins–Based Vaccination on Fecal Shedding of Escherichia coli O157:H7 in Experimentally Inoculated Cattle." Journal of Food Protection 72, no. 4 (April 1, 2009): 866–69. http://dx.doi.org/10.4315/0362-028x-72.4.866.

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The efficacy of a vaccine containing outer membrane siderophore receptor and porin (SRP) proteins for reducing fecal prevalence and shedding of Escherichia coli O157:H7 was evaluated in cattle inoculated with E. coli O157:H7. Thirty calves were randomly assigned to one of two groups, and on days 1 and 21 these calves were given subcutaneous injections of either a placebo (control) or the vaccine. Blood was collected weekly to monitor the serum anti-SRP antibody titers. Two weeks after the second vaccination, calves were orally inoculated with a mixture of five strains of nalidixic acid–resistant (NalR) E. coli O157:H7. Fecal samples and rectoanal mucosal swabs were collected daily for the first 5 days and then three times each week for the following 4 weeks to determine the presence and enumerate the fecal concentration of NalR E. coli O157:H7. At necropsy on day 35, gut contents and tissue swabs were collected to determine the presence and concentration of NalR E. coli O157:H7. Vaccinated cattle had significantly higher anti-SRP antibody titers than did control cattle, with a significant treatment × week interaction (P < 0.01). Vaccination of cattle with the SRP protein tended to decrease fecal concentration (1.9 versus 1.6 log CFU/g) of NalR E. coli O157:H7 (P = 0.10). The number of calves that were fecal culture positive for E. coli O157:H7 was lower (P = 0.05) in the vaccinated group than in the control group. The E. coli O157:H7 SRP vaccine tended to reduce fecal prevalence and concentration of E. coli O157:H7 in cattle orally inoculated with NalR E. coli O157: H7 and may be a useful prehavest intervention strategy. Future research must be conducted on natural prevalence in feedlot operations to further evaluate the efficacy of this novel vaccine.

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Panthi, Vijay Kumar, Saurav Kumar Jha, Raghvendra Chaubey, and Rudra Pangeni. "Formulation and development of Serratiopeptidase enteric coated tablets and analytical method validation by UV Spectroscopy." International Journal of Analytical Chemistry 2021 (October 19, 2021): 1–13. http://dx.doi.org/10.1155/2021/9749474.

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Serratiopeptidase (SRP) is a proteolytic enzyme that emerged as one of the most potent anti-inflammatory and analgesic drugs. The purpose of the present study was to formulate and evaluate enteric-coated tablets for SRP and investigate their stability using a simple and validated analytical method by ultraviolet (UV) spectroscopy. The colloidal silicon dioxide (2.50%), sodium starch glycolate (3.44%), and crospovidone (2.50%) were used as appropriate excipients for the development of core part of tablets. To protect the prepared tablets from acidic environment in the stomach, white shellac, castor oil, HPMC phthalate 40, and ethyl cellulose were used. The seal coating and enteric coating attained were 2.75% and 6.74%, respectively. SRP was found to be linear at 265 nm in the concentration range of 25–150 µg/mL. The results revealed that our developed method was linear (R2 = 0.999), precise (RSD % = 0.133), and accurate (% recovery = 99.96–103.34). The formulated SRP tablets were found to be stable under accelerated conditions as well as under room temperature for 6 months (assay %: >97.5%). The in vitro drug release study demonstrated that enteric-coated tablets were able to restrict SRP release in both acidic environments: 0.1 N HCl and simulated gastric fluid (pH 1.2). Moreover, at 60 minutes, the formulated SRP tablets revealed 13.0% and 8.98% higher drug release in phosphate buffer (pH 6.8) and simulated intestinal fluid (pH 6.8), respectively, compared to the marketed tablet formulation. This study concludes that enteric-coated tablets of SRP with higher drug release in the intestine can be prepared and examined for their stability using validated analytical technique of UV spectroscopy.

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Harinesan, Nimalan, and Stephen W. Reddel. "072 Signal recognition particle antibody associated necrotizing myositis with ‘burnt-out’ paravertebral muscle atrophy." Journal of Neurology, Neurosurgery & Psychiatry 90, e7 (July 2019): A22.3—A23. http://dx.doi.org/10.1136/jnnp-2019-anzan.60.

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IntroductionNecrotizing autoimmune myositis (NAM) is an increasingly recognised myositis.1 While diagnosis is primarily from muscle pathology, antibodies to signal recognition particle (SRP) or 3-hydroxy-3-methylglutaryl–coenzyme A reductase (HMGCR) are also associated.CaseA 67 year old woman presented with proximal weakness and elevated creatine kinase (CK) levels following a complicated AMI, CABG and commencement of atorvastatin. Muscle biopsy confirmed necrotizing myositis and SRP (not HMGCoAR) antibodies were positive. Recovery and rehabilitation was slow and her CK did not normalise for 12 months. She was treated with immunotherapy including intravenous immunoglobulin, oral and intravenous corticosteroids, azathioprine, and mycophenolate.Residual hip, abdominal and truncal weakness remained, affecting her gait and posture. CK levels during this period remained normal. MRI demonstrated extensive paravertebral muscle loss with fatty replacement without oedema. Small myopathic units without active features were present on EMG.ConclusionThis case illustrates several important aspects of NAM, which remains a rare disorder. Recovery can be incomplete in up to 40%, especially if control is delayed.2 In our opinion, normalisation of CK is an important target and may be necessary for full recovery, and rising CK may predict relapse.3 We suggest MRI and EMG of weak muscles may assist in distinguishing persisting myositis from ‘burnt-out’ disease, clarifying whether immunotherapy should be increased or not. However relapse on weaning immunosuppression remains frequent. While SRP antibodies in patients who had also taken statins has been previously reported, the quick sequential onset in this case suggests possible causality.ReferencesMammen AL. Autoimmune Myopathies. Contin Lifelong Learn Neurol. 2016;22(6):1852–1870.Watanabe Y, Uruha A, Suzuki S, et al. Clinical features and prognosis in anti-SRP and anti-HMGCR necrotising myopathy. J Neurol Neurosurg Psychiatry 2016;87(10):1038–1044.Ramanathan S, Langguth D, Hardy TA, et al. Clinical course and treatment of anti-HMGCR antibody–associated necrotizing autoimmune myopathy. Neurol Neuroimmunol Neuroinflammation 2015;2:e96.

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Maity, Tuhin Subhra, Howard M. Fried, and Kevin M. Weeks. "Anti-cooperative assembly of the SRP19 and SRP68/72 components of the signal recognition particle." Biochemical Journal 415, no. 3 (October 15, 2008): 429–37. http://dx.doi.org/10.1042/bj20080569.

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The mammalian SRP (signal recognition particle) represents an important model for the assembly and role of inter-domain interactions in complex RNPs (ribonucleoproteins). In the present study we analysed the interdependent interactions between the SRP19, SRP68 and SRP72 proteins and the SRP RNA. SRP72 binds the SRP RNA largely via non-specific electrostatic interactions and enhances the affinity of SRP68 for the RNA. SRP19 and SRP68 both bind directly and specifically to the same two RNA helices, but on opposite faces and at opposite ends. SRP19 binds at the apices of helices 6 and 8, whereas the SRP68/72 heterodimer binds at the three-way junction involving RNA helices 5, 6 and 8. Even though both SRP19 and SRP68/72 stabilize a similar parallel orientation for RNA helices 6 and 8, these two proteins bind to the RNA with moderate anti-cooperativity. Long-range anti-cooperative binding by SRP19 and SRP68/72 appears to arise from stabilization of distinct conformations in the stiff intervening RNA scaffold. Assembly of large RNPs is generally thought to involve either co-operative or energetically neutral interactions among components. By contrast, our findings emphasize that antagonistic interactions can play significant roles in assembly of multi-subunit RNPs.

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Mecoli, Christopher A., Arash H. Lahouti, Robert A. Brodsky, Andrew L. Mammen, and Lisa Christopher-Stine. "High-dose cyclophosphamide without stem cell rescue in immune-mediated necrotizing myopathies." Neurology - Neuroimmunology Neuroinflammation 4, no. 5 (July 11, 2017): e381. http://dx.doi.org/10.1212/nxi.0000000000000381.

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Objective:To describe the experience managing treatment-refractory immune-mediated necrotizing myopathies (IMNM) with high-dose cyclophosphamide (HiCy) therapy.Methods:Five patients with severe refractory IMNM who were treated with HiCy without stem cell rescue were identified. Their medical records were reviewed to assess demographic, clinical, and histologic characteristics as well as response to therapy.Results:Three patients with anti–signal recognition particle (SRP) and 2 patients with anti-HMG-CoA reductase autoantibodies were included. The mean follow-up time after HiCy therapy was 37 ± 28 months. Two patients demonstrated substantial response, evidenced by improved muscle strength and decreased muscle enzymes after HiCy therapy; both of these patients were anti-SRP positive. Four patients experienced febrile neutropenia after HiCy therapy, one of which required a prolonged intensive care unit stay for infectious complications, from which they eventually recovered.Conclusions:These data suggest that HiCy therapy without stem cell rescue may be considered as an alternative for the treatment of refractory IMNM.

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Resseguier, A. S., C. Le Quang, C. Makarawiez, V. Rieu, P. Philippe, and M. Ruivard. "Myopathie nécrosante auto-immune associée aux anticorps anti SRP et grossesse." La Revue de Médecine Interne 34 (June 2013): A126. http://dx.doi.org/10.1016/j.revmed.2013.03.097.

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Hashimoto, M., A. Iwata, S. Tsuji, and J. Shimizu. "P2.48 Evaluation of the ELISA method for anti-SRP antibody detection." Neuromuscular Disorders 20, no. 9-10 (October 2010): 633. http://dx.doi.org/10.1016/j.nmd.2010.07.120.

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Karsenty, J., J. C. Lega, N. Fabien, A. Hot, J. F. Cordier, C. Lecomte, J. Ninet, and I. Durieu. "Spectre clinique des connectivites avec anticorps anti-Signal Recognition Particle (SRP)." La Revue de Médecine Interne 33 (December 2012): A73. http://dx.doi.org/10.1016/j.revmed.2012.10.098.

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Guerin-Moreau, M., L. Martin, and N. Cordel. "Les anticorps anti-SRP constituent-ils un facteur pronostique des dermatomyosites ?" Annales de Dermatologie et de Vénéréologie 141, no. 12 (December 2014): S420—S421. http://dx.doi.org/10.1016/j.annder.2014.09.433.

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Kessentini, N., S. Mrabet, E. Farhat, F. Hentati, and M. Zouari. "Myosite à anticorps anti-SRP : une forme frontière des myopathies héréditaires." Revue Neurologique 169 (April 2013): A44—A45. http://dx.doi.org/10.1016/j.neurol.2013.01.098.

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Tokuzumi, M., T. Fujisawa, E. Shu, H. Kanoh, C. Saigo, T. Miyazaki, Y. Hamaguchi, and M. Seishima. "Anti-SRP Antibody-positive Myopathy with Universal Alopecia and Multiple Vitiligo." Acta Dermato Venereologica 95, no. 4 (2015): 497–98. http://dx.doi.org/10.2340/00015555-1985.

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Knauß, S., Y. Allenbach, C. Preuße, N. Fischer, V. Matyash, H. Goebel, O. Benveniste, and W. Stenzel. "PD1 and PDL2 axis confers T cell exhaustion in anti-SRP+ and anti-HMGCR+ myopathies." Neuromuscular Disorders 27 (October 2017): S156—S157. http://dx.doi.org/10.1016/j.nmd.2017.06.230.

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Eura, N., K. Sugie, M. Ozaki, T. Shiota, Y. Uchihara, H. Nanaura, K. Fukushima, et al. "Clinicopathological evaluation of anti-SRP versus anti-HMGCR myopathy: What are the similarities and differences?" Journal of the Neurological Sciences 381 (October 2017): 273–74. http://dx.doi.org/10.1016/j.jns.2017.08.780.

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Kurashige, Takashi, Tomomi Murao, Naoko Mine, Tomohito Sugiura, Yukiko Inazuka, Kazuya Kuraoka, Tetsuya Takahashi, Hirofumi Maruyama, and Tsuyoshi Torii. "Anti-HMGCR Antibody-Positive Myopathy Shows Bcl-2-Positive Inflammation and Lymphocytic Accumulations." Journal of Neuropathology & Experimental Neurology 79, no. 4 (February 25, 2020): 448–57. http://dx.doi.org/10.1093/jnen/nlaa006.

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Abstract Anti-3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR) and antisignal recognition particle (SRP) antibodies are frequently associated with immune-mediated necrotizing myopathy (IMNM). However, the difference in clinical manifestations between anti-HMGCR and anti-SRP antibodies is unclear. HMGCR is an essential enzyme for cholesterol biosynthesis and is inhibited by statins that regulate apoptosis of Bcl-2-positive and beta chemokine receptor 4 (CCR4)-positive lymphoma cells. In this study, we aimed to clarify Bcl-2 and CCR4 expressions of lymphocytes in anti-HMGCR antibody-positive IMNM and explore the difference between anti-HMGCR antibody-positive myopathy and other inflammatory myopathies. We retrospectively examined Bcl-2- and CCR4-positive lymphocyte infiltrations in muscle and skin biopsy specimens from 19 anti-HMGCR antibody-positive patients and 75 other idiopathic inflammatory myopathies (IIMs) patients. A higher incidence of Bcl-2- and CCR4-positive lymphocytes was detected in the muscle and skin of anti-HMGCR antibody-positive IMNM patients (p < 0.001). In 5 patients with anti-HMGCR antibodies, Bcl-2-positive lymphocytes formed lymphocytic accumulations, which were not observed in other IIMs. Low-density lipoprotein cholesterol levels were not increased except for patients with Bcl-2-positive lymphocytic accumulations (p = 0.010). Bcl-2 and CCR4 lymphocyte infiltrations could be a pathological characteristic of anti-HMGCR antibody-positive IMNM.

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Yadav, Vikas, Satyam Sharma, Ashutosh Kumar, Sanjiv Singh, and V. Ravichandiran. "Serratiopeptidase Attenuates Lipopolysaccharide-Induced Vascular Inflammation by Inhibiting the Expression of Monocyte Chemoattractant Protein-1." Current Issues in Molecular Biology 45, no. 3 (March 8, 2023): 2201–12. http://dx.doi.org/10.3390/cimb45030142.

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Lipopolysaccharide (LPS) has potent pro-inflammatory properties and acts on many cell types including vascular endothelial cells. The secretion of the cytokines MCP-1 (CCL2), interleukins, and the elevation of oxidative stress by LPS-activated vascular endothelial cells contribute substantially to the pathogenesis of vascular inflammation. However, the mechanism involving LPS-induced MCP-1, interleukins, and oxidative stress together is not well demonstrated. Serratiopeptidase (SRP) has been widely used for its anti-inflammatory effects. In this research study, our intention is to establish a potential drug candidate for vascular inflammation in cardiovascular disorder conditions. We used BALB/c mice because this is the most successful model of vascular inflammation, suggested and validated by previous research findings. Our present investigation examined the involvement of SRP in vascular inflammation caused by lipopolysaccharides (LPSs) in a BALB/c mice model. We analyzed the inflammation and changes in the aorta by H&E staining. SOD, MDA, and GPx levels were determined as per the instructions of the kit protocols. ELISA was used to measure the levels of interleukins, whereas immunohistochemistry was carried out for the evaluation of MCP-1 expression. SRP treatment significantly suppressed vascular inflammation in BALB/c mice. Mechanistic studies demonstrated that SRP significantly inhibited the LPS-induced production of proinflammatory cytokines such as IL-2, IL-1, IL-6, and TNF-α in aortic tissue. Furthermore, it also inhibited LPS-induced oxidative stress in the aortas of mice, whereas the expression and activity of monocyte chemoattractant protein-1 (MCP-1) decreased after SRP treatment. In conclusion, SRP has the ability to reduce LPS-induced vascular inflammation and damage by modulating MCP-1.

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WILEMAN, B. W., D. U. THOMSON, K. C. OLSON, J. R. JAEGER, L. A. PACHECO, J. BOLTE, D. T. BURKHARDT, D. A. EMERY, and D. STRAUB. "Escherichia coli O157:H7 Shedding in Vaccinated Beef Calves Born to Cows Vaccinated Prepartum with Escherichia coli O157:H7 SRP Vaccine." Journal of Food Protection 74, no. 10 (October 1, 2011): 1599–604. http://dx.doi.org/10.4315/0362-028x.jfp-11-034.

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Extensive research, intervention equipment, money, and media coverage have been directed at controlling Escherichia coli O157:H7 in beef cattle. However, much of the focus has been on controlling this pathogen postcolonization. This study was conducted to examine the performance, health, and shedding characteristics of beef calves that were vaccinated with an E. coli O157:H7 SRP bacterial extract. These calves had been born to cows vaccinated prepartum with the same vaccine. Cows and calves were assigned randomly to one of four treatments: (i) neither cows nor calves vaccinated with E. coli O157:H7 SRP (CON), (ii) cows vaccinated with E. coli O157:H7 SRP prepartum but calves not vaccinated (COWVAC), (iii) calves vaccinated with E. coli O157:H7 SRP but born to cows not vaccinated (CALFVAC), (iv) cows vaccinated with E. coli O157:H7 SRP prepartum and calves also vaccinated (BOTH). Calves born to vaccinated cows had significantly higher titers of anti–E. coli O157:H7 SRP antibodies (SRPAb) in circulation at branding time (P < 0.001). Upon entry to the feedlot, overall fecal E. coli O157:H7 prevalence was 23% among calves, with 25% in the CON treatment group, 19% in the CALFVAC group, 32% in the COWVAC group, and 15% in the BOTH group (P > 0.05). Fecal shedding of E. coli O157 on arrival to the feedlot was not correlated with fecal shedding at slaughter (Spearman's rho = −20.02; P = 0.91). No significant effects of cow or calf E. coli O157:H7 SRP vaccination treatment were found on feedlot calf health or performance (P > 0.05), prevalence of lung lesions or liver abscess (P > 0.05), or morbidity, retreatment, or mortality numbers (P > 0.05). The findings of this study indicate that the timing of vaccination of calves against E. coli O157:H7 may be an important consideration for maximizing the field efficacy of this vaccine.

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Arouche-Delaperche, L., Y. Allenbach, D. Amelin, W. Stenzel, G. Butler-Browne, and O. Benveniste. "Muscle atrophy and regeneration impairment of anti-SRP and anti-HMGCR Abs in necrotizing autoimmune myopathies." Neuromuscular Disorders 26 (October 2016): S143. http://dx.doi.org/10.1016/j.nmd.2016.06.209.

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Sghiri, Rim, Zahid Shakoor, Mohammed Ahmed, Nuha Nasser Alrajhi, and Adel Almogren. "Myositis-specific and Myositis-associated Autoantibodies in Saudi Patients." Journal of Nature and Science of Medicine 7, no. 2 (April 2024): 103–7. http://dx.doi.org/10.4103/jnsm.jnsm_219_23.

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Abstract Background and Objectives: Data about myositis-specific autoantibodies (MSAs) and myositis-associated autoantibodies (MAAs) in Saudi patients are limited, and most studies have focused on anti-Jo1. This study aimed at reporting the MSAs and MAAs in Saudi population and their significance. Methods: This was a retrospective analysis of 190 Saudi patients investigated for idiopathic inflammatory myopathies (IIMs) between January 2019 and January 2023. Data for MSAs and MAAs were collected from medical records of patients. MSAs and MAAs were detected by line immunoblot. Results: Among the 190 sera tested, 47 yielded positive results for MSAs. There were 19 (40.4%) patients with IIMs, 20 (42.6%) with interstitial lung disease (ILD), and 8 (17%) with connective tissue diseases. Anti-signal recognition particle (SRP) was the most common MSA and was positive among 16 (34%) patients. Anti-PL-12 was the most frequent anti-synthetase antibody (21.3%) followed by anti-PL-7 (19.1%). Anti-Jo1 was associated with Raynaud’s phenomenon (odds ratio [OR] = 9, 95% confidence interval [CI] = 1.3–60, P = 0.037) and with ILD (OR = 29, 95% CI = 2.4–351, P = 0.008) in patients with IIMs whereas anti-PL-7 was associated with ILD in the rest of the patients (OR = 6, 95% CI = 1.1–33, P = 0.021). MAAs were positive in 24 (51.1%) patients with anti-Ro52 as the most frequently detected antibody (29.8%). Conclusion: We confirm the association of MSAs with IIMs and ILD in the Saudi population. Anti-SRP and anti-PL-12 were the most common MSAs. These observations should be validated by large-scale studies.

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Journal articles on the topic 'Anti-SRP'

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