11Purple-fleshed sweet potato P40 has been shown to prevent colorectal cancer in a murine 12 model. This study is to identify anthocyanins by using HPLC/MS-MS and assess the stability 13 during various cooking conditions. P40 possesses a high content of anthocyanins up to 14 mg/g 14 dry matter. Total 12 acylated anthocyanins are identified. Top three anthocyanins, e.g., cyanidin 15 3-caffeoyl-p-hydroxybenzoyl sophoroside-5-glucoside, peonidin 3-caffeoyl sophoroside-5-16 glucoside, and cyanidin 3-(6'' -caffeoyl-6''-feruloylsophoroside)-5-glucoside, account for half 17 of the anthocyanin contents. Over 80% of anthocyanins measured by acid hydrolysis were 18 cyanidin derivatives, indicating P40 is unique when compared with other purple-fleshed sweet 19 potatoes that usually contain more peonidin than cyanidin. Steaming, pressure cooking, 20 microwaving, and frying but not baking significantly reduced 8-16% of total anthocyanin 21 contents. Mono-acylated anthocyanins showed a higher resistance against heat than di-and non-22 acylated. Among of which, cyanidin 3-p-hydroxybenzoylsophoroside-5-glucoside exhibited the 23 best thermal stability. The stable acylated and cyanidin-predominated anthocyanins in P40 may 24 provide extra benefits for cancer prevention. 25Keywords: Anthocyanins / purple-fleshed sweet potato / cancer prevention / stability / cooking 26 conditions 27

Scope Anthocyanins, the natural pigments in plant foods, have been associated with cancer prevention. However, the content of anthocyanins in staple foods is typically low and the mechanisms by which they exert anti-cancer activity is not yet fully defined. Methods and results We selected an anthocyanin-enriched purple-fleshed sweet potato clone, P40, and investigated its potential anti-cancer effect in both in vitro cell culture and in vivo animal model. In addition to a high level of total phenolics and antioxidant capacity, P40 possesses a high content of anthocyanins at 7.5 mg/g dry matter. Treatment of human colonic SW480 cancer cells with P40 anthocyanin extracts at 0–40 μM of peonidin-3-glucoside equivalent resulted in a dose-dependent decrease in cell number due to cytostatic arrest of cell cycle at G1 phase but not cytotoxicity. Furthermore, dietary P40 at 10–30% significantly suppressed azoxymethane-induced formation of aberrant crypt foci in the colons of CF-1 mice in conjunction with, at least in part, a lesser proliferative PCNA and a greater apoptotic caspase-3 expression in the colon mucosal epithelial cells. Conclusion These observations, coupled with both in vitro and in vivo studies reported here, suggest anthocyanin-enriched sweet potato P40 may protect against colorectal cancer by inducing cell cycle arrest, anti-proliferative and apoptotic mechanisms.

We study the graph isomorphism game that arises in quantum information theory from the perspective of bigalois extensions of compact quantum groups. We show that every algebraic quantum isomorphism between a pair of (quantum) graphs X and Y arises as a quotient of a certain measured bigalois extension for the quantum automorphism groups G X and G Y of the graphs X and Y . In particular, this implies that the quantum groups G X and G Y are monoidally equivalent. We also establish a converse to this result, which says that every compact quantum group G monoidally equivalent to G X is of the form G Y for a suitably chosen quantum graph Y that is quantum isomorphic to X. As an application of these results, we deduce that the * -algebraic, C * -algebraic, and quantum commuting (qc) notions of a quantum isomorphism between classical graphs X and Y all coincide. Using the notion of equivalence for non-local games, we deduce the same result for other synchronous non-local games, including the synBCS game and certain related graph homomorphism games. Universiteit Leuven, mateusz.wasilewski@kuleuven.be 2. Conversely, for any compact quantum group G monoidally equivalent to G X , one can construct from this monoidal equivalence a quantum graph Y , an isomorphism of quantum groups G ∼ = G Y , and an algebraic quantum isomorphism X ∼ = A * Y .Recasting all of the above in the context of the (classical) graph isomorphism game, our results show that the condition A(Iso(X, Y )) = 0 is sufficient to ensure the existence of perfect quantum strategies for this game (Corollary 4.8 and Theorem 4.9):Theorem Two classical graphs X and Y are algebraically quantum isomorphic if and only if the graph isomorphism game has a perfect quantum-commuting (qc)-strategy.We mention that a weaker version of the above theorem (that assumed the existence of a non-zero C * -algebra representation of A(Iso(X, Y ))) was recently proved in [18].

Mutational analysis has established that the cytoplasmic tail of the integrin ␤3 subunit binds c-Src (termed as Src in this study) and is critical for bidirectional integrin signaling. Here we show in washed human platelets that a cell-permeable, myristoylated RGT peptide (myr-RGT) corresponding to the integrin ␤3 C-terminal sequence dose-dependently inhibited stable platelet adhesion and spreading on immobilized fibrinogen, and fibrin clot retraction as well. Myr-RGT also inhibited the aggregation-dependent platelet secretion and secretion-dependent second wave of platelet aggregation induced by adenosine diphosphate, ristocetin, or thrombin. Thus, myr-RGT inhibited integrin outside-in signaling. In contrast, myr-RGT had no inhibitory effect on adenosine diphosphate-induced soluble fibrinogen binding to platelets that is dependent on integrin inside-out signaling. Furthermore, the RGT peptide induced dissociation of Src from integrin ␤3 and dose-dependently inhibited the purified recombinant ␤3 cytoplas- IntroductionIntegrins mediate cell adhesion and transduce signals that are critical in the dynamic regulation of cell adhesion, spreading, migration, and proliferation. 1,2 Bidirectional signaling of integrins is exemplified in the prototype platelet integrin, ␣IIb␤3. Inside-out signaling of integrin ␣IIb␤3 requires talin binding to the cytoplasmic domain of ␣IIb␤3, 3 and its subsequent conformational changes, 4 which propagate to the extracellular ligand binding domain, activate the ligand binding function. Ligand binding to ␣IIb␤3 not only forms adhesive bonds but also induces outside-in signaling, leading to platelet spreading, secretion, amplification of platelet aggregation, and subsequent clot retraction. 5 It is known that outside-in signaling of integrin ␣IIb␤3 requires phosphorylation of the ␤3 cytoplasmic domain at Y 747 and Y 759 . 6 It has also been reported, using multiple Src family protein tyrosine kinasedeficient mouse models, that Src plays an important role in the integrin outside-in signaling. 7 However, the exact molecular events and the direct requirement for this kinase in ␤3 tyrosine phosphorylation in human platelets remain to be established.The cytoplasmic domain of ␤3 is critical in integrin bidirectional signaling. Inside-out signaling requires the membrane proximal region of ␤3, including the highly conserved N 744 PXY 747 motif, which directly interacts with the talin head domain, allowing receptor activation. Arias-Salgado et al have shown that the C-terminus of ␤3 interacts with Src, which is important in integrin outside-in signaling leading to cell spreading, and that 2 residues in the ␤3 cytoplasmic tail, R 760 and T 762 , are necessary for Src binding. 8 Furthermore, deletion of the C-terminal RGT sequence of ␤3 abolishes Src binding. 9 However, whether RGT sequence is sufficient for Src binding or whether additional residues upstream of R 760 , in particular Y 759 of the NXXY motif, are also involved in this interaction, is still an unanswered question. Using a CHO cell mode...