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Dotolo, Raffaele (2016) Studio dell'espressione e della localizzazione di tre proteine, PTMA, PREP e DAAM1, per la prima volta associate alla spermatogenesi dei Vertebrati. [Ph.D. thesis]

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Abstract (english)

During the years of activity as a PhD student in the group of Prof. Sergio Minucci (Dept. of Experimental Medicine, Second University of Naples) I studied the expression and localization of two proteins, prothymosin alpha (Part I) and discevelled-associated activator of morphogenesis (Part III) in male gametogenesis. Moreover, I spent six months in US at the School of Medicine of Yale University (NH, Connecticut). There I focused on the possible role for Prolyl endopeptidase on spermatogenesis in mouse (Part II).
Part I: PTMA expression and localization during the spermatogenesis of Danio rerio
Prothymosin alpha (PTMA) is a highly acidic (Frangou-Lazaridis et al., 1988), intrinsically disordered protein (Gast et al., 1995), which was first extracted from rat thymus and characterized as an immunogenic factor (Haritos et al., 1984a) but soon detected in a variety of mammalian tissues (Haritos et al., 1984b; Clinton et al., 1989). The presence of a nuclear localization signal and the adoption of a peculiar random coil conformation are amongst the reasons behind its interaction with a number of molecular partners; hence, today PTMA is known to be a very conserved and widely-expressed molecule, involved in several and diverse biological processes, like H1 histone interaction and chromatin remodeling (Karetsou et al., 1998; Ueda et al., 2012), cell death (Enkermann et al., 2000a; Jiang et al., 2003; Malicet et al., 2006; Ueda, 2009), transcriptional regulation (Karetsou et al., 2002; Martini et al., 2000; Martini and Katzenellenbogen, 2003) cancer development (Dominguez et al., 1993; Skopeliti et al., 2006; Tsitsiloni et al., 1993; Wu et al., 1997; Zhang et al., 2014) and, as already alluded to, immunity (Baxevanis et al., 1992; Pan et al., 1986; Voutsas et al., 2000).
Since 2002 our group has studied PTMA during the spermatogenesis of several vertebrate species (Aniello et al., 2002; Ferrara et al., 2009; Prisco et al., 2009; Ferrara et al., 2010; Ferrara et al., 2013): the expression of PTMA in meiotic and post-meiotic germ cells inside testicular tubules and its presence in spermatozoa (associated with the acrosome, where present) reveal a striking conservation of the pattern during phylogenesis and suggest a possible role for the protein in gametogenesis and in fertilization. Since many vertebrate models show an established association between PTMA and the acrosome (Ferrara et al., 2013), the study of the possible differences in an acrosome-less sperm model may prove very compelling. In the light of the above Danio rerio was chosen as a model for the continuation of the project (first part of thesis work), given its peculiar anastomosing tubular organization of the testis and, above all, the fact that the spermatozoa (SPZ) do not develop an acrosome system at all, being its fertilization a mechanical process (Hirai, 1988).
Ptma transcript localization in the testis of Danio rerio approximately matches the pattern that we and others had previously highlighted in other species (Aniello et al., 2002, Ferrara et al., 2009; Prisco et al., 2009; Ferrara et al., 2010; Ferrara et al., 2013), with a clear predilection for meiotic and post-meiotic germ cells.
The immunohistochemical data clearly show that the protein shares the same localization. Indeed, it is absent in spermatogonia, which suggests that it does not participate in the proliferation of staminal/mitotic phases, while its presence in primary spermatocytes (SPC) and in spermatids (SPT) supports its possible role during meiosis and/or during the subsequent stages of SPT differentiation into mature SPZ. Specifically, soon after its first appearance in the cytoplasm of leptotene/zygotene primary SPC, PTMA extends its localization to the membrane-free chromatin region of dividing cells and, then, it retains its nuclear distribution during SPT differentiation.
The nuclear localization in the acrosome-lacking spermatozoa suggests a role for PTMA in chromatin remodeling during gamete differentiation. These data further provide a compelling starting point for the study of PTMA functions during vertebrate fertilization.
Part II: PREP is associated with male reproductive function and male gametes in mice
Prolyl endopeptidase (PREP) is a member of the serine peptidase group, which is widely conserved through evolution (Venäläinen et al., 2004). PREP is involved in the maturation and degradation of peptide hormones and neuropeptides (Mentlein, 1988; Wilk, 1983), but its activity is restricted to oligopeptides comprising no more than about 30 amino acid residues.
Despite its common cytosolic localization, it is believed that PREP may act outside the cells by inactivating extracellular neuropeptides. In fact, it was suggested that PREP may be released from the cells (Ahmed et al., 2005), even though it lacks a secretion signal and it does not contain a transmembrane region, or a lipid anchor sequence (Venäläinen et al, 2004). PREP has been implicated in many biological processes, such as the maturation and degradation of peptide hormones and neuropeptides (Mentlein, 1988), learning and memory (Cunningham and O’Connor, 1997; D’Agostino et al., 2013), cell proliferation and differentiation (Matsubara et al., 1998; Suzuki et al., 2014) and glucose metabolism (Kim et al., 2014). A small number of reports have also suggested PREP participation in both male and female reproduction-associated processes (Kimura et al., 1998; Kimura et al., 2002). In order to improve the understanding of the possible role of PREP in male reproduction, in this second part of thesis work the effect of PREP knockdown (Prepgt/gt) on testis and sperm in adult mice was examined.
After confirming PREP expression in wild type (wt) testis and spermatozoa (SPZ), as opposed to Prepgt/g samples, we performed a comparison of macroscopic parameters on wt and knockdown testes: the data show that Prepgt/gt gonads are smaller and weigh less than the wild type. Likewise, histological analysis shows that, while the general morphology appears to be preserved, tubule and lumen diameters are reduced in Prepgt/gt mice, and that the percentage of spermiated tubules is also lower than wt.
Inside the gonad, the protein is localized in elongating spermatids and luminal SPZ of wt mice, as well as Sertoli cells, Leydig cells and peritubular cells. PREP is also expressed in epididymal SPZ, where it is detected in the head, as well as in the midpiece of the sperm flagellum, while the remaining tail region shows a weaker signal. Conversely, in knockdown testis and SPZ the signal is almost undetectable. These data suggest that the endopeptidase may be involved in mature sperm function; indeed, this is supported and enriched by final data on sperm parameters, which show that total count, normal morphology, and motility are altered and reduced in Prepgt/gt mice, compared to the wild type.
These results suggest that PREP may play a fundamental role in mouse spermatogenesis, and sperm motility. Further experiments are required to understand whether the role played by this protein in spermatogenesis affects gonadal tissue development and gamete function directly.
Part III: DAAM1 expression and localization during the spermatogenesis of rat and in human spermatozoa
DAAM1 is a protein belonging to the formins, a large group of molecules which control the nucleation and assembly of actin fibers in response to several signals (Kovar, 2006; Goode and Eck, 2007). Several studies have shown that DAAM1 participates in essential biological processes, such as cytoskeletal organization, movement and adhesion during morphogenesis and organogenesis, as well as cell polarity (Zallen, 2007; Sato et al., 2006; Matusek et al., 2006; Aspenstrom et al., 2006; Lu et al., 2007; Yamashita et al., 2007).
Cytoskeletal remodelling is a process that allows the cells to modulate their architecture and shape following intracellular and/or extracellular stimuli. As a formin, DAAM 1 has the ability to nucleate unbranched actin filaments and, thus, it acts as a regulator of the cytoskeleton in cell polarity and movement. Although its role during the development has been well studied, its potential activity in adult tissues is still unexplored. As of now, no reports have directly associated DAAM1 with reproductive processes, but it is known that factors which participate in the same molecular pathways are expressed during spermatogenesis: these include Dvl1, Dvl2 and 3 (Ma et al., 2006), as well as several GTPases and Rho-related proteins (Naud et al., 2003).
In 2011, our group isolated a cDNA coding for DAAM1 from the testis of Pelophylax esculentus. The first studies, carried out on this model, showed that the protein localizes inside the spermatocysts. In this third part of thesis work, the study was focused on another model, Rattus norvegicus, since its testicular anatomy and the events which occur during spermatogenesis are emblematic of those of Mammals (Russell et al., 1989). First, the presence of DAAM1 was confirmed in rat testis at several time points during post-natal development (7-14-21-28-35-42-60 days post-partum, dpp), which suitably recapitulate the key events of the first spermatogenetic wave. In order to better characterize DAAM1 profile and to confirm its possible involvement during spermatogenesis, the localization of the protein during the post-natal development of the male gonad was studied by immunofluorescence analysis. A remarkable variation in DAAM1 distribution was detected through the times point studied: at 7 dpp, the protein localizes in the central region of the tubules; at 14 dpp, the signal is evident in A and B spermatogonia in the same central region, up until 21-28 dpp, when the signal is detectable inside the spermatocytes. During spermiohistogenesis (35 dpp and 42 dpp), DAAM1 signal is detectable in spermatids, with a peculiar localization in the forming acrosomal region. Finally, at 60 dpp, the signal is also present in mature spermatozoa (SPZ), in the cytoplasmic droplet.
Given DAAM1 involvement in cytoskeletal remodeling, the localization profile of the formin was compared with the distribution of other cytoskeletal proteins: actin and tubulin. Actin signal is consistent with DAAM1 during the first phases of testis development, but it is also present in Sertoli cells which form the blood-testis barrier; later, at 35 dpp, the signal is evident in the now-complete barrier, as well as, during spermiohistogenesis, in the epithelial cells which rearrange their architecture to support the path of the evolving germ cells toward the lumen (42 dpp). Inside the adult testis, actin is expressed by all the cell types, including the SPZ. As for tubulin, it is also expressed in all stages, located inside the Sertoli cells which nurse the germ cells during their differentiation into SPZ. In order to deepen the knowledge on DAAM1 localization in male gametes, an immunofluorescence analysis was carried out on rat epididymal SPZ: there, the protein is mainly detectable inside the flagellum. Then, the analysis was extended to DAAM1 localization in human ejaculated SPZ, where the droplet is often physiologically retained (WHO 2010; Mortimer & Menkveld, 2001). Indeed, the signal in human gametes confirmed DAAM1 retention inside this cytoplasmic structure. Finally, a comparative analysis of the localization of cytoskeletal proteins was also performed on rat epididymal SPZ and in human ejaculated sperm: in both species actin is located in the head, in the acrosomal region, as well as in the flagellum, while tubulin is mainly distributed in the latter region.
These results show, for the first time, the expression and the localization of DAAM1 during rat spermatogenesis and in rat and human SPZ, and they provide a comparative profile of its distribution versus the main germinal-compartment architectural factors, suggesting its possible involvement as an actor in morpho-functional remodeling and organization of the gonad and of male gametes

Abstract (italian)

Durante l’attività di ricerca svolta, come dottorando, nel gruppo del Prof. Sergio Minucci (Dipartimento di Medicina Sperimentale, Seconda Università di Napoli), ho contribuito allo studio dell’espressione e della localizzazione di due proteine, prothymosin alpha (Parte I) e discevelled-associated activator of morphogenesis (Parte III), nella gametogenesi maschile. Inoltre, durante il periodo di studi all’estero presso la School of Medicine della Yale University (NH, Connecticut), ho analizzato il possibile coinvolgimento dell’enzima Prolil-endopeptidasi nella spermatogenesi, utilizzando modelli murini geneticamente modificati (Parte II).
Parte I: Espressione e localizzazione di PTMA durante la spermatogenesi di Danio rerio
La protimosina alfa (PTMA) è una proteina altamente acida (Frangou-Lazaridis et al., 1988), appartenente alle proteine intrinsecamente non strutturate (Gast et al., 1995), isolata per la prima volta nel timo di ratto. Caratterizzata inizialmente come un fattore immunogeno (Haritos et al., 1984a), presto è stata ritrovata in diversi tessuti dei Mammiferi (Haritos et al., 1984b; Clinton et al., 1989). La presenza di un segnale nucleare, oltre alla peculiare conformazione random coil, permettono a tale proteina di interagire con numerosi partner molecolari. PTMA è una molecola altamente conservata nella filogenesi e coinvolta in diversi processi biologici, come nell’interazione con l’istone H1 e il rimodellamento cromatinico (Karetsou et al., 1998; Ueda et al., 2012), la morte cellulare (Enkermann et al., 2000a; Jiang et al., 2003; Malicet et al., 2006; Ueda, 2009), la regolazione della trascrizione (Karetsou et al., 2002; Martini et al., 2000; Martini and Katzenellenbogen, 2003), lo sviluppo del cancro (Dominguez et al., 1993; Skopeliti et al., 2006; Tsitsiloni et al., 1993; Wu et al., 1997; Zhang et al., 2014), e l’immunità (Baxevanis et al., 1992; Pan et al., 1986; Voutsas et al., 2000).
Dal 2002 il nostro gruppo ha iniziato uno studio di espressione e localizzazione di PTMA durante la spermatogenesi di diversi Vertebrati (Aniello et al., 2002; Ferrara et al., 2009; Prisco et al., 2009; Ferrara et al., 2010; Ferrara et al., 2013): l’espressione della proteina nelle cellule meiotiche e post-meiotiche dei testicoli e la sua presenza negli spermatozoi (associata con l’acrosoma, dove presente) rivelano un pattern molto conservato durante la filogenesi e suggeriscono un possibile ruolo per PTMA nella gametogenesi e nella fecondazione. Dato che alcuni Vertebrati mostrano un’associazione di PTMA e l’acrosoma (Ferrara et al., 2013), lo studio della proteina in modelli animali che presentano spermatozoi privi della suddetta struttura risulta particolarmente interessante. Per questo motivo è stato scelto il modello Danio rerio per continuare il progetto di ricerca (prima parte del lavoro di tesi), data la sua peculiare organizzazione dei testicoli in tubuli anastomizzati e principalmente per la caratteristica assenza dell’acrosoma nello spermatozoo (SPZ), il quale feconda l’uovo attraverso una penetrazione meccanica (Hirai, 1988).
La localizzazione del trascritto di ptma nel testicolo di Danio rerio, presenta un pattern simile a quanto osservato in altre specie (Aniello et al., 2002, Ferrara et al., 2009; Prisco et al., 2009; Ferrara et al., 2010; Ferrara et al., 2013), in particolare nelle cellule meiotiche e post-meiotiche.
I dati dell’analisi immunoistochimica mostrano che la proteina mantiene la propria localizzazione anche in questa specie. Infatti, risulta assente negli spermatogoni, suggerendo che essa non partecipa nella fasi proliferative, mentre la presenza della proteina negli spermatociti (SPC) primari e negli spermatidi (SPT) supporta un suo possibile ruolo durante la meiosi e/o nelle fasi di differenziamento degli SPT in SPZ. In particolare, la proteina è presente nel citoplasma degli SPC in leptotene/zigotene; in seguito Ptma estende la sua localizzazione alla regione cromatinica delle cellule in divisione, e mantiene la sua distribuzione nucleare anche durante il differenziamento degli SPT.
La localizzazione nucleare in spermatozoi privi di acrosoma suggerisce un ruolo per Ptma nel rimodellamento cromatinico durante il differenziamento dei gameti. Questi dati, quindi, forniscono un’interessante punto di partenza per lo studio delle funzioni di Ptma nella riproduzione dei Vertebrati.
Parte II: PREP è associato alle funzioni riproduttive maschili ed ai gameti maschili in topo
La prolil endopeptidasi (PREP) è un membro della famiglia delle serina peptidasi molto conservato durante l’evoluzione (Venäläinen et al., 2004). PREP è coinvolto nella maturazione e degradazione di ormoni peptidici e neuropeptidi (Mentlein, 1988; Wilk, 1983), ma la sua attività è limitata a oligopeptidi composti da non più di trenta residui amminoacidici.
Nonostante la sua localizzazione citoplasmatica, tale enzima può svolgere la propria attività esternamente alla cellula, inattivando neuropeptidi nell’ambiente extracellulare. Infatti, è stato suggerito che PREP può essere rilasciato dalle cellule (Ahmed et al., 2005), anche se non possiede un segnale di secrezione o una regione di interazione con la membrana plasmatica (Venäläinen et al, 2004). PREP è stato implicato in diversi processi biologici, come la maturazione e la degradazione di ormoni e neuropeptidi (Mentlein, 1988), apprendimento e memoria (Cunningham and O’Connor, 1997; D’Agostino et al., 2013), proliferazione cellulare e differenziamento (Matsubara et al., 1998; Suzuki et al., 2014), e nel metabolismo del glucosio (Kim et al., 2014). Ad oggi, alcuni studi hanno ipotizzato una partecipazione di PREP anche nei processi associati alla riproduzione (Kimura et al., 1998; Kimura et al., 2002). Allo scopo di approfondire un possibile ruolo della proteina nella riproduzione maschile, in questo seconda parte del lavoro di tesi sono stati esaminati gli effetti della sua mancata espressione genica, utilizzando topi transgenici PREP knockdown (Prepgt/gt), su testicoli e spermatozoi (SPZ).
Dopo aver confermato la presenza dell’espressione di PREP nei testicoli e SPZ wild type (wt), rispetto ai campioni Prepgt/gt, è stata eseguita un’analisi comparata dei parametri macroscopici sui testicoli di wt e knockdown: i dati mostrano che le gonadi di Prepgt/gt presentano un peso e dimensione ridotta rispetto ai wt. Similmente, le analisi istologiche mostrano che, mentre la morfologia generale è preservata tra i due genotipi, il diametro e il lume dei tubuli sono ridotti nei topi Prepgt/gt, e che la percentuale di tubuli seminiferi spermiati è maggiore nei wt.
Nella gonade maschile la proteina localizza negli spermatidi allungati e negli SPZ luminali dei topi wt, nelle cellule di Sertoli, Leydig e nelle cellule peritubulari. PREP è espresso anche negli SPZ epididimali, dove localizza nella testa e nel tratto intermedio del flagello, mentre nella restante regione della coda il segnale è ridotto. Come atteso, nei campioni knockdown sia nel testicolo che negli SPZ il segnale non è rilevabile.
Questi dati suggeriscono che la endopeptidasi potrebbe essere associata alla maturazione dei gameti; infatti, a supporto di ciò, i dati finali ottenuti analizzando i parametri spermatici mostrano una riduzione della conta totale e della motilità, nonché una maggiore alterazione della normale morfologia nei topi Prepgt/gt, rispetto ai wt.
Questi risultati suggeriscono che PREP potrebbe avere un ruolo fondamentale nella spermatogenesi di topo e nella motilità dello spermatozoo. Tuttavia, ulteriori esperimenti sono richiesti per comprendere se il ruolo di questo enzima nella spermatogenesi è svolto durante lo sviluppo testicolare o direttamente nella fisiologia del gamete maturo.
Parte III: Espressione e localizzazione di DAAM1 durante la spermatogenesi di ratto e negli spermatozoi di uomo
DAAM1 è una proteina appartenente alla famiglia delle formine, un gruppo di molecole che controllano la nucleazione e l’assemblaggio delle fibre di actina in risposta a diversi segnali (Kovar, 2006; Goode and Eck, 2007). Molti studi hanno mostrato che DAAM1 è coinvolto in processi biologici essenziali, come la polarità cellulare, il movimento e l’adesione durante la morfogenesi e organogenesi, così come l’organizzazione citoscheletrica (Zallen, 2007; Sato et al., 2006; Matusek et al., 2006; Aspenstrom et al., 2006; Lu et al., 2007; Yamashita et al., 2007).
Il rimodellamento citoscheletrico è un processo mediante il quale le cellule modulano la loro architettura e forma in seguito a stimoli intracellulari e/o extracellulari. Come tutte le formine, DAAM1 possiede la capacità di nucleare filamenti di actina ed agire come regolatore del citoscheletro nel movimento e nella polarità cellulare. Sebbene il ruolo di questa proteina durante lo sviluppo sia stato ben studiato, la sua potenziale attività nei tessuti adulti resta ancora da esplorare.
Fino ad oggi, non ci sono studi che mostrano un coinvolgimento di DAAM1 nei processi riproduttivi, tuttavia alcune molecole che sono coinvolte negli stessi pathway molecolari risultano espresse durante la spermatogenesi (Ma et al., 2006).
Nel 2011, il nostro gruppo ha isolato un cDNA codificante DAAM1 dal testicolo di Pelophylax esculentus. I primi studi, condotti utilizzando questo modello, hanno mostrato che la proteina localizza nelle spermatocisti. In questa terza parte del lavoro di tesi lo studio è stato spostato su un altro modello, Rattus norvegicus, dato che in questa specie l’anatomia testicolare e gli eventi che avvengono durante la spermatogenesi sono rappresentatiti dei Mammiferi (Russell et al., 1989). Inizialmente, è stata confermata la presenza di DAAM1 nel testicolo di ratto a diversi stadi durante lo sviluppo post-natale (7-14-21-28-35-42-60 days post-partum, dpp), che ricapitola gli eventi chiave della prima ondata spermatogenetica. Allo scopo di caratterizzare un profilo di espressione della proteina e confermare il suo possibile coinvolgimento durante la spermatogenesi, è stata studiata la sua localizzazione durante lo sviluppo post-natale delle gonade di ratto, tramite immunofluorescenza. DAAM1 mostra una particolare distribuzione negli stadi analizzati: a 7 dpp, la proteina localizza nella regione centrale dei tubuli; a 14 dpp, il segnale è evidente negli spermatogoni A e B nella stessa regione centrale, fino ai 21- 28 dpp, quando il segnale si evidenzia negli spermatociti. Durante la spermioistogenesi (35 e 42 dpp), DAAM1 è presente negli spermatidi, con una peculiare localizzazione nella regione acrosomica in formazione. Infine a 60 dpp, quando la prima ondata spermatogenetica è completata, il segnale è presente anche negli spermatozoi (SPZ), a livello del residuo citoplasmatico.
Dato il coinvolgimento di DAAM1 nel rimodellamento citoscheletrico, il profilo di localizzazione della formina è stato comparato con la distribuzione di altre proteine citoscheletriche: actina e tubulina. Il segnale dell’actina è simile a quello di DAAM1 durante le prime fasi dello sviluppo testicolare, ma essa è presente anche nelle cellule di Sertoli che iniziano a formare la barriera emato-testicolare; in seguito, a 35 dpp, il segnale è evidente nella barriera completata. Inoltre, durante la spermioistogenesi, l’actina localizza anche nelle cellule epiteliali che supportano il riarrangiamento cito-strutturale delle cellule germinali verso il lume (42 dpp). Nel testicolo adulto, l’actina è espressa in tutte le cellule, inclusi gli SPZ. La tubulina risulta espressa in tutte le fasi dello sviluppo, e localizza nelle cellule di Sertoli che svolgono un ruolo essenziale nel sostenere le cellule germinale durante il loro differenziamento in SPZ. Allo scopo di approfondire la localizzazione di DAAM1 nei gameti maschili, è stata eseguita un’analisi di immunofluorescenza su spermatozoi epididimali di ratto: i risultati mostrano che la proteina è presente nel flagello. Successivamente, l’analisi è stata estesa a SPZ eiaculati di uomo, dove la goccia citoplasmatica è spesso fisiologicamente ritenuta (WHO 2010; Mortimer & Menkveld, 2001). Infatti, è stata confermata la localizzazione di DAAM1 nel residuo citoplasmatico dei gameti umani. Infine, è stata condotta un‘analisi comparativa della localizzazione delle proteine citoscheletriche negli SPZ di ratto e uomo: in entrambe le specie l’actina localizza nella testa, nella regione acrosomale, e nella coda; mentre la tubulina è distribuita nel flagello.
Questi risultati mostrano, per la prima volta, l’espressione e la localizzazione di DAAM1 durante la spermatogenesi di ratto e negli spermatozoi di ratto e uomo, e forniscono un profilo comparato della distribuzione della formina rispetto ai principali fattori che controllano la cito-architettura delle cellule germinali, suggerendo un suo possibile coinvolgimento nel rimodellamento morfo-funzionale e nell’organizzazione della gonade e dei gameti maschili.

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EPrint type:Ph.D. thesis
Tutor:Minucci, Sergio
Ph.D. course:Ciclo 28 > Scuole 28 > BIOMEDICINA > MEDICINA RIGENERATIVA
Data di deposito della tesi:16 January 2016
Anno di Pubblicazione:16 January 2016
Key Words:PTMA, PREP, DAAM1, spermatogenesi, testicolo, spermatozoi
Settori scientifico-disciplinari MIUR:Area 05 - Scienze biologiche > BIO/13 Biologia applicata
Struttura di riferimento:Dipartimenti > Dipartimento di Medicina Molecolare
Codice ID:9043
Depositato il:06 Oct 2016 16:33
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