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Alagille Syndrome
Published in Dongyou Liu, Handbook of Tumor Syndromes, 2020
The NOTCH2 neurogenic locus notch homolog protein 2 (NOTCH2) gene on chromosome 1p12 consists of 34 exons and encodes a transmembrane protein (NOTCH2), which represents one of the Notch family of transmembrane receptors (i.e., NOTCH1, NOTCH2, NOTCH3, and NOTCH4) in humans. Structurally, Notch transmembrane receptors include an extracellular domain with multiple EGF-like repeats and an intracellular domain with multiple different domain types. The intracellular domain consists of seven ankyrin (ANK) repeats that participate in protein−protein interaction [6,7].
Disorders of blood and immune function
Published in Angus Clarke, Alex Murray, Julian Sampson, Harper's Practical Genetic Counselling, 2019
Hereditary spherocytosis is a disorder of the red cell membrane which usually follows autosomal dominant inheritance, but haemolysis is often mild, requiring red cell fragility tests to be sure that an individual is not affected. Numerous other causes of spherocytosis must be excluded before this diagnosis is made. Specific forms of hereditary spherocytosis have been identified as due to defects in several different red cell membrane proteins, including spectrin and ankyrin.
Hemolytic Anemia Associated with Red Cell Membrane Defects
Published in Harold R. Schumacher, William A. Rock, Sanford A. Stass, Handbook of Hematologic Pathology, 2019
HS is produced by mutations in the genes encoding several different component proteins of the membrane skeleton (Fig. 1). The most frequent mutations that give rise to HS affect the genes for ankyrin and band 3 (anion channel). Mutations also occur in α spectrin, β spectrin, and protein 4.2 (pallidin). The final common pathophysiologic pathway produced by most HS mutations is spectrin deficiency. Spectrin deficiency leads to membrane loss and spherocytosis. It is a consistent characteristic of HS that most hemolysis occurs selectively in the spleen.
A Review of Lens Biomechanical Contributions to Presbyopia
Published in Current Eye Research, 2023
Other studies confirm that biomechanical properties and fiber cell arrangement are maintained by filensin and anchoring membrane proteins which colocalize with aquaporin 0. Aquaporin assists with microcirculation in the lens and water balance as a membrane water channel. Ankyrin-B, a membrane connective protein maintains the organized hexagonal structure of fiber cell bundles. Lenses without ankyrin-B exhibit significantly decreased elastic moduli as well. It is thought that the cytoskeletal element periaxin maintains fiber cell organization which allows for lens clarity. Periaxin and ankyrin-B together maintain tensile strength between fiber cells in the lens.34,35,98,125,128 Furthermore, studies have shown that some connexin proteins found in the lens are mechanosensitive. These results show another way in which accommodative biomechanical force can alter lens cellular behavior and lens chemistry.129,130 It is overwhelmingly apparent that multiple proteins expressed in the ocular lens are essential to proper lens function, overlap in complex webs, and that age associated degradation has great potential to interfere with the balance of these systems.
Relation between mutations in the 5′ UTR of ANKRD26 gene and inherited thrombocytopenia with predisposition to myeloid malignancies. An Egyptian study
Published in Platelets, 2021
Nahla Ibrahim Zidan, Doaa Metwally AbdElmonem, Haitham Mohamed Elsheikh, Elsayed Anany Metwally, Wesam AbdElmonem Mokhtar, Gamal Mohamed Osman
Ankyrin repeat domain 26 (ANKRD26) is the ancestor of a family of primate-specific genes termed POTE (Prostate-, Ovary-, Testis-, and placenta-Expressed genes), its expression is variable in different organs but consistently high across many normal tissues as the cerebral cortex and some pathological tissues as breast and prostatic cancers [5] (Figure 1). An increased expression pattern in some pathological tissues would support evidence for the involvement of this gene and its mutations in malignancies. With regard to human bone marrow cells, Macaulay et al. reported that ANKRD26 is expressed in megakaryocytes, and to a lesser extent, in erythroid cells. The functional role of ANKRD26 is unknown. The ANKRD26 protein is associated with the inner part of the cell membrane and contains ankyrin repeats and spectrin helices for interaction with signaling proteins [6].
Effects of homocysteine and memantine on oxidative stress related TRP cation channels in in-vitro model of Alzheimer’s disease
Published in Journal of Receptors and Signal Transduction, 2021
İshak Suat Övey, Mustafa Nazıroğlu
Transient receptor potential (TRP) superfamily contains 28 channel protein members in mammalian. TRP ankyrin 1 (TRPA1) is single member of ankyrin subfamily, because of ankyrin repeats of the N-terminal region. TRPA1 is activated by different stimuli, including cinnamaldehyde (CIN) [7]. TRP Melastatin 2 (TRPM2) is second member of melastatin TRP subfamily, has unique Adenosine diphosphate ribose (ADPR) pyrophosphatase enzyme activity domain in the C-terminal Nudix motif. TRPM2 is separately activated by ADPR and NAD+ [8]. TRP vanilloid 1 (TRPV1) is also a member of vanilloid subfamily and it is activated by different chemical stimuli such as capsaicin (CAPSN), piperine and resiniferatoxin [9]. Results of recent studies indicated that the TRPA1, TRPM2 and TRPV1 in hippocampus are also activated by oxidative stress [10–12]. Brain areas such as hippocampus, temporal and frontal lobes have main roles in etiology of AD and expression levels of TRPA1, TRPM2 and TRPV1 are high in the areas [13–15]. However, involvements of the TRPA1, TRPM2 and TRPV1 in etiology of AD have not been clarified yet.