Changes in high-intensity precipitation on the northern Apennines (Italy) as revealed by multidisciplinary data over the last 9000 years

Several record-breaking precipitation events have struck the mountainous area of the Emilia-Romagna region (northern Apennines, Italy) over the last 10 years. As a consequence, severe geomorphological processes such as debris avalanches and debris flows, shallow landslides, and over-bank flooding have affected the territory, causing severe damage to human-made structures. The unusual intensity of these phenomena prompted an investigation into their frequency in the past, beyond instrumental time. In the quest for an understanding of whether these phenomena are unprecedented in the region, peat bog and lake deposits were analyzed to infer the frequency of extreme precipitation events that may have occurred in the past. We present the results of a dedicated field campaign performed in summer 2017 at Lake Moo in the northern Apennines, a 0.15 km(2) peat bog located at an altitude of 1130 m a.s.l. During the extreme precipitation event of 13-14 September 2015, several debris flows generated by small streams affected the Lake Moo plain. In such a small drainage basin (<2 km(2)), high-density floods can be triggered only by high-intensity precipitation events. The sedimentary succession (ca. 13 m thick) was studied through the drilling of two cores and one trench. The sequence, characterized by clusters of coarse-grained alluvial deposits interbedded with organic-rich silty clays and peat layers, was analyzed by combining sedimentological, pollen, microanthracological and pedological data with radiocarbon dating (AMS C-14) in an innovative multidisciplinary approach for this area. Original data acquired during the field campaign were also correlated with other specific paleoclimatic proxies available in the literature for the northern Apennines area. We discover that the increase in extreme paleoflooding, associated with coarse-grained deposits similar to the ones observed recently, correlates well with the warm phases of the Holocene Thermal Maximum and with the ongoing warming trend observed that started at the beginning of the last century

Systemic amyloidosis and pneumatosis of bladder wall

A 72-year-old woman was admitted to our Department for syncopes, diarrhoea, and weight loss. We suspected the diagnosis of systemic amyloidosis after the detection of macroglossia and periorbital purpura, despite the biopsy of the previous year, that resulted negative for amyloid substance. We confirmed the diagnosis after the histological evidence of deposits of amyloid in bone marrow and the clinical evidence of pneumatosis of bladder wall. Chemotherapy improved only temporarily clinical condition

Structural characterization of transglutaminase-catalyzed cross-linking between glyceraldehyde 3-phosphate dehydrogenase and polyglutamine repeats

The accumulation of abnormal polyglutamine-containing protein aggregates within the cytosol and nuclei of affected neurons is a hallmark of the progressive neurodegenerative disorders caused by an elongated (CAG)n repeat in the genome. The polyglutamine domains are excellent substrates for the enzyme transglutaminase type 2 (tissue), resulting in the formation of cross-links with polypeptides containing lysyl groups. Enzymatic activity toward the Qn domains increases greatly upon lengthening of such Qn stretches (n > 40). Among the possible amine donors, the glycolytic enzyme glyceraldehyde-3-phosphate-dehydrogenase was shown to tightly bind several proteins involved in polyglutamine expansion diseases. Recently, the authors have shown that K191, K268, and K331, out of the 26 lysines present in glyceraldehyde-3-phosphate-dehydrogenase, are the reactive amine-donor sites forming cross-links with substance P, which bears the simplest Qn domain (n = 2). The present study reports that synthetic peptides of both pathological and nonpathological length (n = 43 and 17, respectively) form cross-links with the same K residues located in the C-terminal region of glyceraldehyde-3-phosphate-dehydrogenase. In addition, it is shown that extra K residues present in the C termini of glyceraldehyde-3-phosphate-dehydrogenase are susceptible to cross-linking in the presence of transglutaminase. The present results indicate a possible modulating effect of Qn stretches on tissue transglutaminase substrate specificity and mechanism of recognition

Identification of tissue transglutaminase-reactive lysine residues in glyceraldehyde-3-phosphate dehydrogenase

Polyglutamine domains are excellent substrates for tissue transglutaminase resulting in the formation of cross-links with polypeptides containing lysyl residues. This finding suggests that tissue transglutaminase may play a role in the pathology of neurodegenerative diseases associated with polyglutamine expansion. The glycolytic enzyme GAPDH previously was shown to tightly bind several proteins involved in such diseases. The present study confirms that GAPDH is an in vitro lysyl donor substrate of tissue transglutaminase. A dansylated glutamine-containing peptide was used as probe for labeling the amino-donor sites. SDS gel electrophoresis of a time-course reaction mixture revealed the presence of both fluorescent GAPDH monomers and high molecular weight polymers. Western blot analysis performed using antitransglutaminase antibodies reveals that tissue transglutaminase takes part in the formation of heteropolymers. The reactive amino-donor sites were identified using mass spectrometry. Here, we report that of the 26 lysines present in GAPDH, K191, K268, and K331 were the only amino-donor residues modified by tissue transglutaminase