2 edition of inherited erythroid ankyrin deficiency in normoblastosis found in the catalog.
inherited erythroid ankyrin deficiency in normoblastosis
Robert Allen White
Written in English
|Statement||by Robert Allen White.|
|Contributions||Boston College. Dept. of Biology.|
|The Physical Object|
|Pagination||x, 144 leaves ;|
|Number of Pages||144|
Ankyrin deficiency: Known also as hereditary spherocytosis (HS), this is a genetic disorder of the red blood cell membrane clinically characterized by anemia, jaundice (yellowing) and splenomegaly (enlargement of the spleen), due to deficiency of ankyrin, a protein in . The first ankyrin was characterized over 30 years ago as an adaptor protein that tethered the anion exchanger to β‐spectrin in red blood cells [ 1 ]. Ankyrins are now regarded as pivotal choreographers in the formation of protein complexes consisting of ion channels and Cited by:
After splenectomy, there was marked normoblastosis, up to fold in excess of the total leukocyte count, with prominent large, round macrocytes. The fetal hemoglobin level was %. Bone marrow morphology showed a predominantly erythroid marrow (83% erythroid precursors, 3% lymphocytes, 15% myeloid cells). NAME: Robert Allen White E-MAIL ADDRESS: [email protected] R. A. () An inherited erythroid ankyrin deficiency in normoblastosis: a mutation causing severe hemolytic anemia. Ph.D. Dissertation. Boston College. () Purkinje cell degeneration associated with erythroid ankyrin deficiency in nb/nb mice. Journal of Cell Biology
NX_P - ANK1 - Ankyrin-1 - Function. Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band , to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes . Red blood cells (RBCs), also referred to as red cells, red blood corpuscles, haematids, erythroid cells or erythrocytes (from Greek erythros for "red" and kytos for "hollow vessel", with -cyte translated as "cell" in modern usage), are the most common type of blood cell and the vertebrate's principal means of delivering oxygen (O 2) to the body tissues—via blood flow through the circulatory FMA:
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Normoblastosis, a murine model for ankyrin-deficient hemolytic anemia, is caused by a hypomorphic mutation in the erythroid ankyrin gene Ank1. Hematol J. ; – [ PubMed ]Cited by: Ankyrin deficiency is one of the most common causes of hereditary spherocytosis in humans.
A spontaneous mutation, normoblastosis (Ank1nb), discovered in in a mouse stock maintained at the Jackson Laboratory, provides an important animal model for these human ankyrin-deficient anemias.
Mice with normoblastosis, nb/nb, have a severe hemolytic anemia. The extreme fragility and shortened lifespan of the mutant erythrocytes result from a defective membrane skeleton.
Previous studies in our laboratory indicated a 50% deficiency of spectrin and an absence of normal ankyrin in erythrocyte membranes of nb/nb by: Normoblastosis, a murine model for ankyrin-deficient hemolytic anemia, is caused by a hypomorphic mutation in the erythroid ankyrin gene Ank1.,Cited by: Erythroid ankyrin (ANK1) functions in the red blood cell membrane skeleton as a high affinity binding protein linking the spectrin lattice to the plasma membrane through binding sites on beta‐spectrin and the cytoplasmic domain of band 3 8, 50, Cited by: Purkinje cell degeneration associated with erythroid ankyrin deficiency in nb/nb mice Article (PDF Available) in The Journal of Cell Biology (6) September with 37 Reads.
cated a 50% deficiency of spectrin and an absence of normal ankyrin in erythrocyte membranes of nb/nb mice. We now report genetic mapping data that localize both the nb and erythroid ankyrin (Ank-1) loci to the centromeric end of mouse chromosome 8.
Using immunological and biochemical meth-ods, we have further characterized the nature of the. tients with HS have combined spectrin and ankyrin defi-ciency  due to deficiency of the latter. Ankyrin (band ) is a kDa protein that links the red cell membrane skeleton composed primarily of alpha and beta spectrin to the membrane bilayer through band 3, the transmembrane anion transport channel (AE1) [5–11].
To date, gene therapy approaches for the treatment of inherited metabolic deficiencies are still limited, mainly because of the frequent lack of selective advantage of genetically corrected cells. This implies that high levels of transgene expression are required, as well as an efficient transduction of Cited by: 1.
A nonsense mutation Glu → Ter within the regulatory domain of human erythroid ankyrin leads to a selective deficiency of the major ankyrin isoform (band ) and a phenotype of autosomal dominant hereditary spherocytosisCited by: 9.
Although originally thought to be null for ankyrin-1 because of a paucity of Ank1 message and undetectable ankyrin-1 protein in RBC ghosts [17 x 17 Birkenmeier, C., Gifford, E., and Barker, J. Normoblastosis, a murine model for ankyrin-deficient hemolytic anemia, is caused by a hypomorphic mutation in the erythroid ankyrin gene by: The nb/nb cells synthesize normal amounts of a spectrin.
This supports our suggestion that ankyrin rather than spectrin is defective in the nb/nb mouse. A small amount of a spectrin is synthesized in ja/ja reticulocytes and a greater than normal amount is synthesized in sph"a/sph"a by: Anemias due to decreased erythropoiesis (termed hypoproliferative anemias) are recognized by reticulocytopenia, which is usually evident on the peripheral smear.
The RBC indices, mainly the mean corpuscular volume (MCV), can narrow the differential diagnosis of deficient erythropoiesis and help determine what further testing is necessary. In a kindred with autosomal dominant hereditary spherocytosis (SPH1; ), Jarolim et al.
() identified a unique mutation in the regulatory domain of ankyrin associated with a marked and selective deficiency of ankyrin isoform and a normal content of ankyrin isoform The deficiency of the ankyrin isoform was accompanied by a proportional deficiency of spectrin.
Previous studies in our laboratory indicated a 50% deficiency of spectrin and an absence of normal ankyrin in erythrocyte membranes of nb/nb mice. We now report genetic mapping data that localize both the nb and erythroid ankyrin (Ank-1) loci to the centromeric end of mouse chromosome 8.
T1 - Ankyrin deficiency is the most common defect in dominant and non dominant hereditary spherocytosis. AU - Lanciotti, Marina.
AU - Perutelli, Paolo. AU - Valetto, Angelo. AU - Di Martino, Daniela. AU - Mori, Pier Giorgio. PY - /7. Y1 - /7. N2 - Background and by: Subtypes.
Ankyrins are encoded by three genes (ANK1, ANK2 and ANK3) in gene in turn produces multiple proteins through alternative splicing. ANK1. The ANK1 gene encodes the AnkyrinR proteins. AnkyrinR was first characterized in human erythrocytes, where this ankyrin was referred to as erythrocyte ankyrin or band AnkyrinR enables erythrocytes to resist shear forces experienced HGNC: The deficiency of erythroid ankyrin causes a severe hemolytic anemia, as well as pathological consequences in other tissues (Peters et al., ).
To determine if skeletal muscle of nb / nb mice expresses normal Ank1 products, we examined frozen cross sections of diaphragm muscle that had been labeled with anti-p65 and anti-p6 by: Mice homozygous for the nb mutation (Chromosome 8) have a severe hemolytic anemia and develop a psychomotor disorder at 6 mo of age.
The nb/nb mice are deficient in erythroid ankyrin (Ank-1) but, until the present study, the role of Ank-1 and of Ank-2 (brain ankyrin) in disease genesis was unknown.
In normal erythroid tissues, we show that two major transcripts are expressed from Ank-1, and. Erythroid ankyrin gene expression in normal and ankyrin deficient mice: the normoblastosis mutation causes a neurological disorder related to erythroid ankyrin deficiency in the brain.
Genetics of the red cell membrane skeleton. Hereditar y spherocytosis associated with deletion ofhumanerythrocyte ankyrin gene on.
Although a spectrin deficiency is seen in most hereditary spherocytosis patients, the principal defect is an abnormality of the RBC membrane protein ankyrin. in the general population; mainly in white populations originating from areas around the Mediterranean sea.Hereditary spherocytosis is an abnormality of red blood cells, or disorder is caused by mutations in genes relating to membrane proteins that allow for the erythrocytes to change shape.
The abnormal erythrocytes are sphere-shaped (spherocytosis) rather than the normal biconcave disk ctional membrane proteins interfere with the cell's ability to be flexible to Specialty: Hematology.As a model of ankyrin-R deficiency, normoblastosis (nb/nb) mice display motor ataxia in addition to severe haemolytic anaemia [32, ].
These deficiencies are the result of a hypomorphic mutation in ankyrin-R [ ] and the movement disorder is consistent with the predominant expression of ankyrin-R in the cell bodies and dendrites of.