Gender differences in N-glycosylation of plasma proteins in children with type 1 diabetes mellitus

Glikozilacija kao jedna od najčešćih i najsloženijih posttranslacijska modifikacija ima izniman utjecaj na konačnu funkciju modificiranog proteina, ali isto tako i sama je pod velikim utjecajem prisutnih fizioloških faktora. Šećerna bolest tipa 1 stanje je autoimunog narušavanja β - stanica Langerhansovih otočića ili samih molekula inzulina, čiji osnovni uzrok nije razjašnjen. U potrazi za objašnjenjem pozadine ove bolesti, odnosno u nastojanju pronalaska novih biomarkera koji bi na nju mogli ukazati, analiza glikozilacije ponudila se kao perspektivan pristup s obzirom na već ustanovljenu povezanost glikozilacije s različitim bolestima i patološkim stanjima, među kojima i s bolestima autoimune prirode. U istraživanju su sudjelovala 153 pacijenta u dobi između 2 i 19 godina, oboljela od šećerne bolesti tipa 1, kojima je pomoću HILIC-UPLC metode napravljen glikanski profil plazme. Dobiveni podaci obrađeni su i statistički uspoređeni prema spolu pomoću Mann-Whitney testa za nezavisne uzorke. U prvom dijelu istraživanja promatrane su pojedinačne glikanske skupine gdje je ustanovljena statistički značajna razlika za GP9, GP11, GP15 i GP17. Naknadno su ispitanici podijeljeni na dvije skupine, jednu mlađu od 10 godina i jednu stariju od 11 za ženske i 12 za muške ispitanike. Razlike među spolovima utvrđene su za GP6, GP9, GP11, GP17 i GP23 kod mlađe skupine, dok kod starije skupine nije ustanovljena statistički značajna razlika. U drugom dijelu istraživana usporedbom zastupljenosti pojedinih glikanskih osobina u profilima pacijenata nije ustanovljena statistički značajna razlika niti u jednoj kategoriji, kako kod mlađe tako ni kod starije skupine ispitanika. Dobivenim rezultatima potvrđena je prisutnost spolnih razlika u glikanskim profilima plazme pacijenata oboljelih od šećerne bolesti tipa 1, što ukazuje da razlike treba uzeti u obzir prilikom razvoja novih biomarkera i dijagnostičkih testova, odnosno eventualnih novih pristupa u terapiji.Glycosylation, as one of the most common and complex posttranslational modifications, has a profound effect on the final function of a modified protein but is also itself greatly affected by the physiological factors. Diabetes mellitus type 1 is a state where normal function of the beta cells of the pancreatic islets or the insulin molecules is compromised by an autoimmune response, even though the underlying cause is not yet known. In an effort to elucidate the cause of this disease and also to find new biomarkers that could possibly point to its development and presence, glycan analysis presented itself as a promising approach given the fact that glycosylation had already been connected to different diseases, some of which are also autoimmune. Plasma samples of 153 type 1 diabetes patients, aged between 2 and 19 years, were analyzed using a HILIC-UPLC method in a way that glycan profiles were created for every patient. Obtained data was then sorted and statistically analyzed by comparing glycosylation according to gender, using the Mann-Whitney test for independent samples. Individual glycan peaks were compared first, and analysis showed statistically significant difference between genders for GP9, GP11, GP15 and GP17. After sorting patients into two groups, one with patients younger than 10 years and another with patients older than 11 for females and 12 for males, differences were analyzed again. A younger group showed statistically significant difference in GP6, GP9, GP11, GP17 and GP23, but the older group didn't show any. Prevalences of several glycan characteristics in glycan profiles were also compared between genders, but statistically significant difference was not found for any of the analyzed characteristics in a younger group as well as in the older one. Results obtained in this study show that there is a gender difference between glycan profiles of type 1 diabetes patients. Those differences should be accounted for in development of new glycan-based diagnostic tests or therapeutics

Fucosylated AGP glycopeptides as biomarkers of HNF1A-Maturity onset diabetes of the young

Aims: We previously demonstrated that antennary fucosylated N-glycans on plasma proteins are regulated by HNF1A and can identify cases of Maturity-Onset Diabetes of the Young caused by HNF1A variants (HNF1A-MODY). Based on literature data, we further postulated that N-glycans with best diagnostic value mostly originate from alpha-1-acid glycoprotein (AGP). In this study we analyzed fucosylation of AGP in subjects with HNF1A-MODY and other types of diabetes aiming to evaluate its diagnostic potential. Methods: A recently developed LC-MS method for AGP N-glycopeptide analysis was utilized in two independent cohorts: a) 466 subjects with different diabetes subtypes to test the fucosylation differences, b) 98 selected individuals to test the discriminative potential for pathogenic HNF1A variants. Results: Our results showed significant reduction in AGP fucosylation associated to HNF1A-MODY when compared to other diabetes subtypes. Additionally, ROC curve analysis confirmed significant discriminatory potential of individual fucosylated AGP glycopeptides, where the best performing glycopeptide had an AUC of 0.94 (95% CI 0.90–0.99). Conclusions: A glycopeptide based diagnostic tool would be beneficial for patient stratification by providing information about the functionality of HNF1A. It could assist the interpretation of DNA sequencing results and be a useful addition to the differential diagnostic process.publishedVersio

High-throughput N-glycosylation analysis of alpha-1-acid glycoprotein in the identification of diabetes mellitus biomarkers

N-glikozilacija, proces enzimski posredovanog vezanja šećernih struktura na asparaginske ostatke proteina, istraživana je u brojnim bolestima, u mnogima od kojih su promjene i potvrđene. Pronalazak specifičnih promjena N-glikozilacije nudi mogućnost razvoja predikcijskih, dijagnostičkih i prognostičkih alata potrebnih u sprječavanju i liječenju različitih bolesti. Studije ukupne N-glikozilacije proteina plazme provedene u istraživanju predispozicije za šećernu bolest tipa 2, kao i istraživanju šećerne bolesti zrele dobi kod mladih osoba (MODY), identificirale su promjene u glikozilaciji za koje se vjeruje da potječu s alfa-1-kiseloga glikoproteina (AGP). S ciljem detaljnijeg istraživanja ovih promjena, razvijena je metoda za visokoprotočnu analizu N-glikozilacije AGP-a koja uključuje obogaćenje ovog proteina te analizu njegovih glikopeptida metodom tekućinske kromatografije spregnute sa spektometrijom masa (LC-MS). Inicijalnom analizom 14 zdravih ispitanika utvrđena je temporalna stabilnost Nglikoma AGP-a, kao općeniti preduvjet za dijagnostičku upotrebu. Novorazvijenom metodom zatim je analizirana glikozilacija AGP-a 108 ispitanika koji se razlikuju po svojoj predispoziciji za razvoj šećerne bolesti tipa 2 te je utvrđena povezanost porasta grananja i smanjenja sijalinizacije glikana AGP-a s povećanim rizikom od razvoja šećerne bolesti tipa 2. Nadalje, kod 466 pacijenata oboljelih od različitih tipova šećerne bolesti (HNF1A-, HNF4AMODY, šećerna bolesti tipa 1 i tipa 2) analizom fukozilacije AGP-a ustanovljeno je njezino smanjenje koje je pokazano specifično za HNF1A-MODY. Nadalje, analizom uzoraka 98 pacijenata oboljelih od šećerne bolesti ranog nastupa bez autoimunosne podloge, pokazano je da je smanjena fukozilacija prisutna samo kod pacijenata s oštećujućim HNF1A mutacijama – sržnim uzrokom bolesti. Također, pokazana je visoka uspješnost identifikacije HNF1A-MODY pacijenata na temelju individualnih glikopeptida AGP-a. Prikupljene spoznaje upućuju na mogućnost upotrebe glikozilacije AGP-a kao predikcijskog biljega za šećernu bolest tipa 2, kao i biljega identifikacije pacijenata oboljelih od HNF1A-MODY-a što bi dalo velik doprinos pravovremenom prepoznavanju rizika kao i diferencijalnoj dijagnostici šećerne bolesti.N-glycosylation, the process of enzymatically mediated binding of sugar structures to proteins' asparagine residues, has been investigated in a number of diseases, in many of which the changes have been confirmed. The discovery of specific N-glycosylation changes offers a possibility for development of prediction, diagnostic and prognostic tools needed in the prevention and treatment of various diseases. Studies of total plasma protein N-glycosylation performed in type 2 diabetes predisposition research, as well as in the research of maturity-onset diabetes of the young (MODY), identified changes in glycosylation believed to originate from alpha-1-acid glycoprotein (AGP). In order to investigate these changes in more detail, a method for high-throughput AGP N-glycosylation analysis was developed. The method is based on enrichment of AGP and analysis of its glycopeptides by liquid chromatography coupled to mass spectrometry (LC-MS). Initial analysis performed on 14 healthy subjects confirmed the temporal stability of AGP N-glycome, as a general prerequisite for diagnostic use. The newly developed method was then used to analyze AGP glycosylation in 108 subjects differing in their predisposition for type 2 diabetes development. The results confirmed an association of increased branching and decreased sialylation of AGP glycans with an increased risk of type 2 diabetes development. Analysis of samples from 466 patients diagnosed with different types of diabetes (HNF1A-, HNF4A-MODY, type 1 and type 2 diabetes) revealed a reduction in AGP fucosylation, which was shown to be specific for HNF1A-MODY. Furthermore, analysis of samples from 98 patients with early-onset non-autoimmune diabetes showed that decreased fucosylation was present only in patients carrying damaging HNF1A mutations - the core cause of the disease. Also, high success rate of identification of HNF1A-MODY patients based on individual AGP glycopeptides was demonstrated. The findings suggest the possibility of utilizing AGP glycosylation as a predictor of type 2 diabetes, as well as a marker for identification of HNF1A-MODY patients. This would present a valuable contribution to timely risk identification and differential diagnosis of diabetes

High-throughput N-glycosylation analysis of alpha-1-acid glycoprotein in the identification of diabetes mellitus biomarkers

N-glikozilacija, proces enzimski posredovanog vezanja šećernih struktura na asparaginske ostatke proteina, istraživana je u brojnim bolestima, u mnogima od kojih su promjene i potvrđene. Pronalazak specifičnih promjena N-glikozilacije nudi mogućnost razvoja predikcijskih, dijagnostičkih i prognostičkih alata potrebnih u sprječavanju i liječenju različitih bolesti. Studije ukupne N-glikozilacije proteina plazme provedene u istraživanju predispozicije za šećernu bolest tipa 2, kao i istraživanju šećerne bolesti zrele dobi kod mladih osoba (MODY), identificirale su promjene u glikozilaciji za koje se vjeruje da potječu s alfa-1-kiseloga glikoproteina (AGP). S ciljem detaljnijeg istraživanja ovih promjena, razvijena je metoda za visokoprotočnu analizu N-glikozilacije AGP-a koja uključuje obogaćenje ovog proteina te analizu njegovih glikopeptida metodom tekućinske kromatografije spregnute sa spektometrijom masa (LC-MS). Inicijalnom analizom 14 zdravih ispitanika utvrđena je temporalna stabilnost Nglikoma AGP-a, kao općeniti preduvjet za dijagnostičku upotrebu. Novorazvijenom metodom zatim je analizirana glikozilacija AGP-a 108 ispitanika koji se razlikuju po svojoj predispoziciji za razvoj šećerne bolesti tipa 2 te je utvrđena povezanost porasta grananja i smanjenja sijalinizacije glikana AGP-a s povećanim rizikom od razvoja šećerne bolesti tipa 2. Nadalje, kod 466 pacijenata oboljelih od različitih tipova šećerne bolesti (HNF1A-, HNF4AMODY, šećerna bolesti tipa 1 i tipa 2) analizom fukozilacije AGP-a ustanovljeno je njezino smanjenje koje je pokazano specifično za HNF1A-MODY. Nadalje, analizom uzoraka 98 pacijenata oboljelih od šećerne bolesti ranog nastupa bez autoimunosne podloge, pokazano je da je smanjena fukozilacija prisutna samo kod pacijenata s oštećujućim HNF1A mutacijama – sržnim uzrokom bolesti. Također, pokazana je visoka uspješnost identifikacije HNF1A-MODY pacijenata na temelju individualnih glikopeptida AGP-a. Prikupljene spoznaje upućuju na mogućnost upotrebe glikozilacije AGP-a kao predikcijskog biljega za šećernu bolest tipa 2, kao i biljega identifikacije pacijenata oboljelih od HNF1A-MODY-a što bi dalo velik doprinos pravovremenom prepoznavanju rizika kao i diferencijalnoj dijagnostici šećerne bolesti.N-glycosylation, the process of enzymatically mediated binding of sugar structures to proteins' asparagine residues, has been investigated in a number of diseases, in many of which the changes have been confirmed. The discovery of specific N-glycosylation changes offers a possibility for development of prediction, diagnostic and prognostic tools needed in the prevention and treatment of various diseases. Studies of total plasma protein N-glycosylation performed in type 2 diabetes predisposition research, as well as in the research of maturity-onset diabetes of the young (MODY), identified changes in glycosylation believed to originate from alpha-1-acid glycoprotein (AGP). In order to investigate these changes in more detail, a method for high-throughput AGP N-glycosylation analysis was developed. The method is based on enrichment of AGP and analysis of its glycopeptides by liquid chromatography coupled to mass spectrometry (LC-MS). Initial analysis performed on 14 healthy subjects confirmed the temporal stability of AGP N-glycome, as a general prerequisite for diagnostic use. The newly developed method was then used to analyze AGP glycosylation in 108 subjects differing in their predisposition for type 2 diabetes development. The results confirmed an association of increased branching and decreased sialylation of AGP glycans with an increased risk of type 2 diabetes development. Analysis of samples from 466 patients diagnosed with different types of diabetes (HNF1A-, HNF4A-MODY, type 1 and type 2 diabetes) revealed a reduction in AGP fucosylation, which was shown to be specific for HNF1A-MODY. Furthermore, analysis of samples from 98 patients with early-onset non-autoimmune diabetes showed that decreased fucosylation was present only in patients carrying damaging HNF1A mutations - the core cause of the disease. Also, high success rate of identification of HNF1A-MODY patients based on individual AGP glycopeptides was demonstrated. The findings suggest the possibility of utilizing AGP glycosylation as a predictor of type 2 diabetes, as well as a marker for identification of HNF1A-MODY patients. This would present a valuable contribution to timely risk identification and differential diagnosis of diabetes

High-throughput N-glycosylation analysis of alpha-1-acid glycoprotein in the identification of diabetes mellitus biomarkers

N-glikozilacija, proces enzimski posredovanog vezanja šećernih struktura na asparaginske ostatke proteina, istraživana je u brojnim bolestima, u mnogima od kojih su promjene i potvrđene. Pronalazak specifičnih promjena N-glikozilacije nudi mogućnost razvoja predikcijskih, dijagnostičkih i prognostičkih alata potrebnih u sprječavanju i liječenju različitih bolesti. Studije ukupne N-glikozilacije proteina plazme provedene u istraživanju predispozicije za šećernu bolest tipa 2, kao i istraživanju šećerne bolesti zrele dobi kod mladih osoba (MODY), identificirale su promjene u glikozilaciji za koje se vjeruje da potječu s alfa-1-kiseloga glikoproteina (AGP). S ciljem detaljnijeg istraživanja ovih promjena, razvijena je metoda za visokoprotočnu analizu N-glikozilacije AGP-a koja uključuje obogaćenje ovog proteina te analizu njegovih glikopeptida metodom tekućinske kromatografije spregnute sa spektometrijom masa (LC-MS). Inicijalnom analizom 14 zdravih ispitanika utvrđena je temporalna stabilnost Nglikoma AGP-a, kao općeniti preduvjet za dijagnostičku upotrebu. Novorazvijenom metodom zatim je analizirana glikozilacija AGP-a 108 ispitanika koji se razlikuju po svojoj predispoziciji za razvoj šećerne bolesti tipa 2 te je utvrđena povezanost porasta grananja i smanjenja sijalinizacije glikana AGP-a s povećanim rizikom od razvoja šećerne bolesti tipa 2. Nadalje, kod 466 pacijenata oboljelih od različitih tipova šećerne bolesti (HNF1A-, HNF4AMODY, šećerna bolesti tipa 1 i tipa 2) analizom fukozilacije AGP-a ustanovljeno je njezino smanjenje koje je pokazano specifično za HNF1A-MODY. Nadalje, analizom uzoraka 98 pacijenata oboljelih od šećerne bolesti ranog nastupa bez autoimunosne podloge, pokazano je da je smanjena fukozilacija prisutna samo kod pacijenata s oštećujućim HNF1A mutacijama – sržnim uzrokom bolesti. Također, pokazana je visoka uspješnost identifikacije HNF1A-MODY pacijenata na temelju individualnih glikopeptida AGP-a. Prikupljene spoznaje upućuju na mogućnost upotrebe glikozilacije AGP-a kao predikcijskog biljega za šećernu bolest tipa 2, kao i biljega identifikacije pacijenata oboljelih od HNF1A-MODY-a što bi dalo velik doprinos pravovremenom prepoznavanju rizika kao i diferencijalnoj dijagnostici šećerne bolesti.N-glycosylation, the process of enzymatically mediated binding of sugar structures to proteins' asparagine residues, has been investigated in a number of diseases, in many of which the changes have been confirmed. The discovery of specific N-glycosylation changes offers a possibility for development of prediction, diagnostic and prognostic tools needed in the prevention and treatment of various diseases. Studies of total plasma protein N-glycosylation performed in type 2 diabetes predisposition research, as well as in the research of maturity-onset diabetes of the young (MODY), identified changes in glycosylation believed to originate from alpha-1-acid glycoprotein (AGP). In order to investigate these changes in more detail, a method for high-throughput AGP N-glycosylation analysis was developed. The method is based on enrichment of AGP and analysis of its glycopeptides by liquid chromatography coupled to mass spectrometry (LC-MS). Initial analysis performed on 14 healthy subjects confirmed the temporal stability of AGP N-glycome, as a general prerequisite for diagnostic use. The newly developed method was then used to analyze AGP glycosylation in 108 subjects differing in their predisposition for type 2 diabetes development. The results confirmed an association of increased branching and decreased sialylation of AGP glycans with an increased risk of type 2 diabetes development. Analysis of samples from 466 patients diagnosed with different types of diabetes (HNF1A-, HNF4A-MODY, type 1 and type 2 diabetes) revealed a reduction in AGP fucosylation, which was shown to be specific for HNF1A-MODY. Furthermore, analysis of samples from 98 patients with early-onset non-autoimmune diabetes showed that decreased fucosylation was present only in patients carrying damaging HNF1A mutations - the core cause of the disease. Also, high success rate of identification of HNF1A-MODY patients based on individual AGP glycopeptides was demonstrated. The findings suggest the possibility of utilizing AGP glycosylation as a predictor of type 2 diabetes, as well as a marker for identification of HNF1A-MODY patients. This would present a valuable contribution to timely risk identification and differential diagnosis of diabetes

Plasma N-glycome shows continuous deterioration as the diagnosis of insulin resistance approaches

INTRODUCTION: Prediction of type 2 diabetes mellitus (T2DM) and its preceding factors, such as insulin resistance (IR), is of great importance as it may allow delay or prevention of onset of the disease. Plasma protein N-glycome has emerged as a promising predictive biomarker. In a prospective longitudinal study, we included patients with a first diagnosis of impaired glucose metabolism (IR or T2DM) to investigate the N-glycosylation’s predictive value years before diabetes development. RESEARCH DESIGN AND METHODS: Plasma protein N-glycome was profiled by hydrophilic interaction ultra-performance liquid chromatography in 534 TwinsUK participants free from disease at baseline. This included 89 participants with incident diagnosis of IR or T2DM during the follow-up period (7.14±3.04 years) whose last sample prior to diagnosis was compared using general linear regression with 445 age-matched unrelated controls. Findings were replicated in an independent cohort. Changes in N-glycome have also been presented in connection with time to diagnosis. RESULTS: Eight groups of plasma N-glycans were different between incident IR or T2DM cases and controls (p<0.05) after adjusting for multiple testing using Benjamini-Hochberg correction. These differences were noticeable up to 10 years prior to diagnosis and are changing continuously as becoming more expressed toward the diagnosis. The prediction model was built using significant glycan traits, displaying a discriminative performance with an area under the receiver operating characteristic curve of 0.77. CONCLUSIONS: In addition to previous studies, we showed the diagnostic potential of plasma N-glycome in the prediction of both IR and T2DM development years before the clinical manifestation and indicated the continuous deterioration of N-glycome toward the diagnosis

Human complement component C3 N-glycome changes in type 1 diabetes complications

Aim: Changes in N-glycosylation have been described in numerous diseases and are being considered as biomarkers of ongoing pathological condition. Previous studies demonstrated the interrelation of N-glycosylation and type 1 diabetes (T1D), particularly linking serum N-glycan changes with complications accompanying the disease. Moreover, the role of complement component C3 in diabetic nephropathy and retinopathy has been implicated, and C3 N-glycome was found to be altered in young T1D patients. Therefore, we investigated associations between C3 N-glycan profiles and albuminuria and retinopathy accompanying T1D, as well as glycosylation connection with other known T1D complication risk factors. Research design and methods: Complement component C3 N-glycosylation profiles have been analyzed from 189 serum samples of T1D patients (median age 46) recruited at a Croatian hospital centre. Using our recently developed high-throughput method, relative abundances of all six of the C3 glycopeptides have been determined. Assessment of C3 N-glycome interconnection with T1D complications, hypertension, smoking status, estimated glomerular filtration rate (eGFR), glycaemic control and duration of the disease was done using linear modelling. Results: Significant changes of C3 N-glycome in severe albuminuria accompanying type 1 diabetes were observed, as well as in T1D subjects with hypertension. All except one of the C3 glycopeptides proved to be associated with measured HbA1c levels. One of the glycoforms was shown to be changed in non-proliferative T1D retinopathy. Smoking and eGFR showed no effect on C3 N-glycome. Furthermore, C3 N-glycosylation profile was shown to be independent of disease duration. Conclusion: This study empowered the role of C3 N-glycosylation in T1D, showing value in distinguishing subjects with different diabetic complications. Being independent of the disease duration, these changes may be associated with the disease onset, making C3 N-glycome a potential novel marker of the disease progression and severity

Fucosylated AGP glycopeptides as biomarkers of HNF1A-Maturity onset diabetes of the young

Aims: We previously demonstrated that antennary fucosylated N-glycans on plasma proteins are regulated by HNF1A and can identify cases of Maturity-Onset Diabetes of the Young caused by HNF1A variants (HNF1A-MODY). Based on literature data, we further postulated that N-glycans with best diagnostic value mostly originate from alpha-1-acid glycoprotein (AGP). In this study we analyzed fucosylation of AGP in subjects with HNF1A-MODY and other types of diabetes aiming to evaluate its diagnostic potential. Methods: A recently developed LC-MS method for AGP N-glycopeptide analysis was utilized in two independent cohorts: a) 466 subjects with different diabetes subtypes to test the fucosylation differences, b) 98 selected individuals to test the discriminative potential for pathogenic HNF1A variants. Results: Our results showed significant reduction in AGP fucosylation associated to HNF1A-MODY when compared to other diabetes subtypes. Additionally, ROC curve analysis confirmed significant discriminatory potential of individual fucosylated AGP glycopeptides, where the best performing glycopeptide had an AUC of 0.94 (95% CI 0.90–0.99). Conclusions: A glycopeptide based diagnostic tool would be beneficial for patient stratification by providing information about the functionality of HNF1A. It could assist the interpretation of DNA sequencing results and be a useful addition to the differential diagnostic process

Virtuoso : Hrvatski skladatelji (studenti Muzičke akademije u Zagrebu, 27.5.2021.)

Koncert iz studentskog ciklusa Virtuoso održan na Muzičkoj akademiji u Koncertnoj dvorani "Blagoje Bersa" 27.5.2021. Izvođači: Mihael Hrgar (tuba), Martina Barišić (sopran), Petar Krokar (klavir), Božidar Vlašić (klavir), Matej Fridl (rog), Marko Gugić (rog), Lovre Laskač (rog), Bruno Laktaš (rog), Stefani Pijetlović (sopran), Brigita Kitner (klavir); Ansambl flauta Muzičke akademije u Zagrebu: Iva Primorac (flauta piccolo), Ana Tutić (flauta), Nikolina Hapač (flauta), Marija Sušić (flauta), Maja Mustapić (flauta), Lucija Družinec (alt flauta), Ana Kovačev (alt flauta), Sara Lončar (alt flauta), Erin Keleuva (bas flauta), Doris Vincek (bas flauta). Program: 1. M. Brekalo: Game of Kobalos (izvođač: Mihael Hrgar); 2. M. Cipra: Dvije djevojačke pjesme (I. Udaralo u tamburu đače - II. Oj volaru medena ti usta) (izvođači: Martina Barišić, Petar Krokar); 3. B. Papandopulo: Kaleidoskop 74, suita za glasovir (I. - V. - VI. Vivo) (izvođač: Božidar Vlašić); 4. T. Uhlik: Sjećanje na prijatelja, studija za četiri roga (izvođači: Matej Fridl, Marko Gugić, Lovre Laskač, Bruno Laktaš); 5. J. Hatze: „Arija rastanka“, arija Mare iz opere „Adel i Mara“ (izvođači: Stefani Pijetlović, Brigita Kitner); 6. I. Tijardović: „Daleko me biser mora“, arija Suzette iz operete „Mala Floramye“ (izvođači: Stefani Pijetlović, Brigita Kitner); 7. T. Uhlik: Karusel (izvođači: Ansambl flauta Muzičke akademije u Zagrebu)

Virtuoso : Hrvatski skladatelji (studenti Muzičke akademije u Zagrebu, 27.5.2021.)

Koncert iz studentskog ciklusa Virtuoso održan na Muzičkoj akademiji u Koncertnoj dvorani "Blagoje Bersa" 27.5.2021. Izvođači: Mihael Hrgar (tuba), Martina Barišić (sopran), Petar Krokar (klavir), Božidar Vlašić (klavir), Matej Fridl (rog), Marko Gugić (rog), Lovre Laskač (rog), Bruno Laktaš (rog), Stefani Pijetlović (sopran), Brigita Kitner (klavir); Ansambl flauta Muzičke akademije u Zagrebu: Iva Primorac (flauta piccolo), Ana Tutić (flauta), Nikolina Hapač (flauta), Marija Sušić (flauta), Maja Mustapić (flauta), Lucija Družinec (alt flauta), Ana Kovačev (alt flauta), Sara Lončar (alt flauta), Erin Keleuva (bas flauta), Doris Vincek (bas flauta). Program: 1. M. Brekalo: Game of Kobalos (izvođač: Mihael Hrgar); 2. M. Cipra: Dvije djevojačke pjesme (I. Udaralo u tamburu đače - II. Oj volaru medena ti usta) (izvođači: Martina Barišić, Petar Krokar); 3. B. Papandopulo: Kaleidoskop 74, suita za glasovir (I. - V. - VI. Vivo) (izvođač: Božidar Vlašić); 4. T. Uhlik: Sjećanje na prijatelja, studija za četiri roga (izvođači: Matej Fridl, Marko Gugić, Lovre Laskač, Bruno Laktaš); 5. J. Hatze: „Arija rastanka“, arija Mare iz opere „Adel i Mara“ (izvođači: Stefani Pijetlović, Brigita Kitner); 6. I. Tijardović: „Daleko me biser mora“, arija Suzette iz operete „Mala Floramye“ (izvođači: Stefani Pijetlović, Brigita Kitner); 7. T. Uhlik: Karusel (izvođači: Ansambl flauta Muzičke akademije u Zagrebu)