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DNA microarray analysis using duodenum from wild-type or IAP knockout (Akp3-/-) mice administered with IIAEK (Ile-Ile-Ala-Glu-Lys)

ABSTRACT: To understand the molecular mechanism by which IIAEK ameliorates hepatic and intestinal cholesterol metabolism, we performed DNA microarray analysis using liver, duodenal, and jejunal samples from the control and IIAEK groups of WT or IAP KO mice. In total, 1406 transcripts were identified in the duodenum of WT mice ( ≥1.2 fold-change, p < 0.05). In contrast, we identified 777 transcripts in the duodenum of IAP-KO mice ( ≥1.2 fold-change, p < 0.05).

ORGANISM(S): Mus musculus

PROVIDER: GSE290758 | GEO | 2025/03/17

REPOSITORIES: GEO

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DNA microarray analysis using jejunum from wild-type or IAP knockout (Akp3-/-) mice administered with IIAEK (Ile-Ile-Ala-Glu-Lys)

Project description:To understand the molecular mechanism by which IIAEK ameliorates hepatic and intestinal cholesterol metabolism, we performed DNA microarray analysis using liver, duodenal, and jejunal samples from the control and IIAEK groups of WT or IAP KO mice. We found that 3503 transcripts were identified in the jejunum of WT mice [WT, Control (WC) vs. WT, IIAEK (WI)] and 1388 in IAP-KO mice [IAP-KO, Control (KOC) vs. IAP-KO, IIAEK (KOI)] ( ≥1.2 fold-change, p < 0.05).

2025-03-17 | GSE290759 | GEO

DNA microarray analysis using liver from wild-type or IAP knockout (Akp3-/-) mice administered with IIAEK (Ile-Ile-Ala-Glu-Lys)

Project description:To understand the molecular mechanism by which IIAEK ameliorates hepatic and intestinal cholesterol metabolism, we performed DNA microarray analysis using liver, duodenal, and jejunal samples from the control and IIAEK groups of WT or IAP KO mice. We found that 1995 transcripts were identified in the livers of WT mice [WT, Control (WC) vs. WT, IIAEK (WI)] and 3802 in IAP-KO mice [IAP-KO, Control (KOC) vs. IAP-KO, IIAEK (KOI)] ( ≥1.2 fold-change, p < 0.05). Of these, 1729 transcripts fluctuated only in the WT group (WC vs. WI) and 3536 fluctuated only in the IAP-KO group (KOC vs. KOI).

2025-03-17 | GSE290764 | GEO

DNA microarray analysis using duodenum from wild-type or IAP knockout (Akp3-/-) mice administered with IIAEK (Ile-Ile-Ala-Glu-Lys)

Project description:DNA microarray analysis using duodenum from wild-type or IAP knockout (Akp3-/-) mice administered with IIAEK (Ile-Ile-Ala-Glu-Lys)

| PRJNA1230066 | ENA

DNA microarray analysis using liver from wild-type or IAP knockout (Akp3-/-) mice administered with IIAEK (Ile-Ile-Ala-Glu-Lys)

Project description:DNA microarray analysis using liver from wild-type or IAP knockout (Akp3-/-) mice administered with IIAEK (Ile-Ile-Ala-Glu-Lys)

| PRJNA1230077 | ENA

DNA microarray analysis using jejunum from wild-type or IAP knockout (Akp3-/-) mice administered with IIAEK (Ile-Ile-Ala-Glu-Lys)

Project description:DNA microarray analysis using jejunum from wild-type or IAP knockout (Akp3-/-) mice administered with IIAEK (Ile-Ile-Ala-Glu-Lys)

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Mammalian Pragmin regulates Src family kinases via the Glu-Pro-Ile-Tyr-Ala (EPIYA) motif that is exploited by bacterial effectors.

Project description:Several pathogenic bacteria have adopted effector proteins that, upon delivery into mammalian cells, undergo tyrosine phosphorylation at the Glu-Pro-Ile-Tyr-Ala (EPIYA) or EPIYA-like sequence motif by host kinases such as Src family kinases (SFKs). This EPIYA phosphorylation triggers complex formation of bacterial effectors with SH2 domain-containing proteins that results in perturbation of host cell signaling and subsequent pathogenesis. Although the presence of such an anomalous protein interaction suggests the existence of a mammalian EPIYA-containing protein whose function is mimicked or subverted by bacterial EPIYA effectors, no molecule that uses the EPIYA motif for biological function has so far been reported in mammals. Here we show that mammalian Pragmin/SgK223 undergoes tyrosine phosphorylation at the EPIYA motif by SFKs and thereby acquires the ability to interact with the SH2 domain of the C-terminal Src kinase (Csk), a negative regulator of SFKs. The Pragmin-Csk interaction prevents translocalization of Csk from the cytoplasm to the membrane and subsequent inactivation of membrane-associated SFKs. As a result, SFK activity is sustained in cells where Pragmin is phosphorylated at the EPIYA motif. Because EPIYA phosphorylation of Pragmin is mediated by SFKs, cytoplasmic sequestration of Csk by Pragmin establishes a positive feedback regulation of SFK activation. Remarkably, the Helicobacter pylori EPIYA effector CagA binds to the Csk SH2 domain in place of Pragmin and enforces membrane recruitment of Csk and subsequent inhibition of SFKs. This work identifies Pragmin as a mammalian EPIYA effector and suggests that bacterial EPIYA effectors target Pragmin to subvert SFKs for successful infection.

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Anticooperativity in a Glu-Lys-Glu salt bridge triplet in an isolated alpha-helical peptide.

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Influence of Glu/Arg, Asp/Arg, and Glu/Lys Salt Bridges on ?-Helical Stability and Folding Kinetics.

Project description:Using a combination of ultraviolet circular dichroism, temperature-jump transient-infrared spectroscopy, and molecular dynamics simulations, we investigate the effect of salt bridges between different types of charged amino-acid residue pairs on ?-helix folding. We determine the stability and the folding and unfolding rates of 12 alanine-based ?-helical peptides, each of which has a nearly identical composition containing three pairs of positively and negatively charged residues (either Glu(-)/Arg(+), Asp(-)/Arg(+), or Glu(-)/Lys(+)). Within each set of peptides, the distance and order of the oppositely charged residues in the peptide sequence differ, such that they have different capabilities of forming salt bridges. Our results indicate that stabilizing salt bridges (in which the interacting residues are spaced and ordered such that they favor helix formation) speed up ?-helix formation by up to 50% and slow down the unfolding of the ?-helix, whereas salt bridges with an unfavorable geometry have the opposite effect. Comparing the peptides with different types of charge pairs, we observe that salt bridges between side chains of Glu(-) and Arg(+) are most favorable for the speed of folding, probably because of the larger conformational space of the salt-bridging Glu(-)/Arg(+) rotamer pairs compared to Asp(-)/Arg(+) and Glu(-)/Lys(+). We speculate that the observed impact of salt bridges on the folding kinetics might explain why some proteins contain salt bridges that do not stabilize the final, folded conformation.

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Computational Prediction of the Protonation Sites of Ac-Lys-(Ala)n-Lys-NH2 Peptides through Conceptual DFT Descriptors.

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Hb J- Meerut [alpha 120 (H3) Ala ->Glu (alpha1)] in a Turkish male.

Project description:Hb J Meerut is an infrequently found alpha-globin variant. It has previously been reported in various populations around the world. One particular case reported in 1994 included a Turkish family. In this report, details of a second case of Hb J Meerut in a Turkish male who is unrelated to the first family are described. In the present case a slight increase in the oxygen affinity of Hb J Meerut, relative to that of the normal control, has been observed as detected by low p50 values in arterial whole blood. Additionally, a slight increase in red blood cell count, as compared against a normal individual, was observed.

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