China
Africa
Explore chapters and articles related to this topic
Disorders of Keratinization and Other Genodermatoses
Published in Ayşe Serap Karadağ, Lawrence Charles Parish, Jordan V. Wang, Roxburgh's Common Skin Diseases, 2022
Roselyn Stanger, Nanette Silverberg
Laboratory studies: A skin biopsy can confirm the diagnosis but is not required and is rarely performed to make the diagnosis. If a syndrome is suspected based on associated features, then a genetic evaluation may be needed. As keratosis pilaris is sometimes noted with obesity, studies related to metabolic syndrome may be needed in some patients. Recently, altered ABCA12 expression has been demonstrated in keratosis pilaris skin.
Collodion baby and harlequin ichthyosis
Published in Biju Vasudevan, Rajesh Verma, Dermatological Emergencies, 2019
D. V. Lakshmi, Sahana M. Srinivas
In 2005, a Japanese dermatologist identified ABCA12 on chromosome 2q35 as the causative gene in HI on the basis of the principle of homozygosity. ABCA12 is a lipid transporter from the Golgi apparatus to the lamellar granule in differentiated keratinocyte, and the lack of ABCA12 leads to a marked reduction of lipid content in the horny layer, premature keratinocyte differentiation, and defective secretion of lipids from the lamellar granules into the extracellular space. In HI epidermis, the expression of kallikrein 5 and cathepsin D proteases was also found to be reduced [25,26].
In silico identification of putative roles of food-derived xeno-mirs on diet-associated cancer
Published in Nutrition and Cancer, 2020
In this study, we retrieved the top-ranked 75 transportable Xeno-miR candidates suggested in Shu et al. and analyzed their putative roles in human disease pathways using “in silico” tools. The initial step of our research included homology analyses of 75 Xeno-miRs and revealed 18 animal food-derived miRNAs to be exact sequence with human miRNAs. Two dietary miRNAs were assigned to the same human miRNAs and excluded. Thus, we further explored the target genes for all 16 animal food-derived miRNAs by grouping them into three sources of species and analyzed enrichments of their human homologs in human disease pathways. Our miRNA target interaction analyses aimed to identify the genes that are targeted by multiple miRNAs which are predicted to be highly tuned by epigenetic controls of miRNAs. We found 13 genes that were targeted by three groups of miRNAs identified by different databases of which were analyzed in IPA for their associations in human disease pathways. Majority of the genes were found to have evidence for their function in cancer and gastrointestinal disease (Supplementary Table S5). Moreover, the set of 10 (ABCA13, CRB1, DLGAP2, GRK3, HIPK2, KLHL18, MEIOC, NTRK2, PDLIM2, PPARA, SRGAP3, ZSCAN25, ZXDC) genes had the lowest P-value for their relationship with large intestine adenocarcinoma. Notably, ABCA12, HIP2, PPARA, and NTRK2 were the most known cancer-associated genes that were either proposed as prognosis marker or promising target for cancer therapies (23–26).
ABCG2 as a therapeutic target candidate for gout
Published in Expert Opinion on Therapeutic Targets, 2018
Kyoko Fujita, Kimiyoshi Ichida
The importance of ABC transporter genes is underscored by the fact that variations in such sequences cause severe inherited diseases. Over 20 ABC transporters representing all subfamilies have been associated with human diseases, such as Tangier disease (ABCA1), Stargardt disease (ABCA4), Harlequin and lamellar ichthyosis (ABCA12), hereditary biliary diseases (ABCB4, ABCB11, and ABCC2), pseudoxanthoma elasticum (ABCC6), cystic fibrosis (ABCC7), type II diabetes (ABCC8 and ABCC9), X-linked adrenoleukodystrophy (ABCD1), gout (ABCG2), and sitosterolemia (ABCG5 and ABCG8) [18]. Moreover, many others play clinically important roles in drug metabolism and resistance [19]. Thus, dysfunctional variants of these genes are of substantial relevance to therapeutic strategies, pharmacokinetics, and innumerable pharmacogenetic disorders [15].
The role of the ATP-Binding Cassette A1 (ABCA1) in neurological disorders: a mechanistic review
Published in Expert Opinion on Therapeutic Targets, 2023
Tahere Paseban, Mohaddeseh Sadat Alavi, Leila Etemad, Ali Roohbakhsh
ABCB1 (P-glycoprotein) is an outwardly directed drug and lipid flippase (phospholipids and glycosphingolipids) that promotes multidrug resistance [199]. ABCB1 has also been implicated in Aβ efflux in BBB endothelial cells [85,200]. A collaboration between ABCB1 and LRP-1 make Aβ efflux across BBB possible (see Figure 2). In addition to ABCA1, ABCA7 is involved in cholesterol efflux and HDL formation [201]. However, previous studies have implicated a secondary role for ABCA7 in lipid transport compared to ABCA1. While ABCA7 makes small cholesterol-poor HDL particles, ABCA1 mostly produces big cholesterol-rich HDL particles [202]. In vitro and in vivo experiments showed that ABCA7 has a role in neuronal Aβ production and/or clearance [203,204]. Microglia and macrophages from ABCA7-KO mice exhibited substantial reductions in Aβ phagocytosis [205]. Also, ABCA7 polymorphisms have been associated with memory impairment in AD [206]. ABCG1 is another ABC superfamily member that transports intracellular cholesterol and sphingolipids to HDL [207]. Similar to ABCA1, cholesterol excess provokes ABCG1 expression [208]. ABCA1 and ABCG1 have a notable role in cholesterol efflux from macrophages and astrocytes. This process is overwhelmed during aging and is restored by LXR agonist administration [37]. Interestingly, ABCG1 and ABCG4 functions change γ-secretase distribution on the plasma membrane and decrease Aβ secretion [209]. Similar to ABCB1, ABCG4 effluxes Aβ from BBB into plasma [210]. Another transporter identified in the luminal plasma membrane of endothelial cells is ABCG2. It may contribute to the brain efflux of Aβ [211]. However, ABCG2’s exact role in Aβ elimination from the brain is debated [200]. Lipid homeostasis is regulated by more ABC members. ABCA3 is a transporter expressed in alveolar type II pneumocytes that excrete lung surfactant. ABCA3 transfers lipids into the lamellar bodies and its mutation causes fatal respiratory distress syndrome in the newborn [212]. ABCA12 is phylogenetically related to ABCA3 and participates in epidermal keratinocyte lamellar granule secretion. As a lipid transporter, this protein helps to form ceramides, but not phospholipids [213]. In patients with ABCA12 dysfunction (mainly due to mutations, harlequin-type ichthyosis), the lipid barrier on the skin is compromised, making them more susceptible to pathogens [214].