The Experts below are selected from a list of 441 Experts worldwide ranked by ideXlab platform
J Delaunay - One of the best experts on this subject based on the ideXlab platform.
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a genomic deletion causes truncation of α spectrin and ellipto Poikilocytosis
Blood Cells Molecules and Diseases, 2011Co-Authors: A Iolascon, M J King, S Robertson, R A Avvisati, F Vitiello, R Asci, M N Scoppettuolo, J DelaunayAbstract:We report on a truncated α-spectrin chain, spectrin(Exeter), associated with ellipto-Poikilocytosis. Analysis of erythrocyte membranes of affected individuals revealed a truncated α-spectrin chain with normal amounts of spectrin dimer. In the proband and her father, one haploid set of α-spectrin cDNA lacked exons 11 and 12, leading to partial deletion of repeats α4 and α5 (83 amino acids) of the α-spectrin chain. In one allele of genomic DNA, a 3567bp deletion starting in intron 10 and ending in intron 12 of the SPTA1 gene was found. The common polymorphic SPTA1 α(LELY) allele was found in trans to the SPTA1αExeter allele in the proband. The proband had inherited the SPTA1Exeter allele from her father and the αLELY allele from her healthy, asymptomatic mother. This is the first report of an interstitial deletion in the SPTA1 gene associated with ellipto-Poikilocytosis.
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GENETIC DISORDERS OF THE RED CELL MEMBRANES
FEBS letters, 1995Co-Authors: J DelaunayAbstract:The red cell membrane is comprised of a lipid bilayer studded with transmembrane proteins, and laminated by a protein network, the membrane skeleton, at the surface of the inner monolayer. The erythrocyte owes its mechanical properties to the membrane skeleton. Hereditary spherocytosis, hereditary elliptocytosis or Poikilocytosis, Southeast Asian ovalocytosis are hereditary hemolytic anemias, due to mutations in the genes encoding ankyrin, the anion exchanger, spectrin, protein 4.1 or protein 4.2, which are main proteins of the membrane. Recent advances in the field have led to fundamental questions.
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Severe Poikilocytosis Associated With A Denovo Alpha-28 Arg-]cys Mutation In Spectrin
'Wiley', 1993Co-Authors: F. Lorenzo, Nicole Alloisio, L Morle, A Iolascon, E. M. Delgiudice, A. Forissier, S. Perrotta, G. Sciarratta, J DelaunayAbstract:Severe Poikilocytosis was observed in an Italian child. The mutation responsible was a de novo alpha28 Arg --> Cys substitution (CGT --> TGT) in spectrin, a mutation known to cause hereditary elliptocytosis or hereditary pyroPoikilocytosis. In this particular case the severity of the manifestations were accounted for by the occurrence, in trans to the alpha28 mutation, of the alpha(V/41) polymorphism. The latter has been shown previously to be associated with structural abnormalities at the alphaIV-alphaV domain junction and with a low expression level. The pronounced alteration of the dimer self association process was also explained by the location of the alpha28 mutation. This mutation occurs in helix 3 of repeating segment alpha1, e.g. precisely in the head-to-head contact between the spectrin alpha and beta chains. The present phenotype was compared to that yielded by another alpha28 mutation (Arg --> His) also combined, in trans, with the alpha(V/41) polymorphism. The pictures were very much alike, stressing the functional importance of residue alpha28. The de novo character of the present mutation strengthens the view that codon alpha28 is a 'hot spot' for mutations
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severe Poikilocytosis associated with a de novo alpha 28 arg cys mutation in spectrin
British Journal of Haematology, 1993Co-Authors: F. Lorenzo, Nicole Alloisio, L Morle, A Iolascon, A. Forissier, S. Perrotta, G. Sciarratta, Miraglia E Del Giudice, J DelaunayAbstract:Severe Poikilocytosis was observed in an Italian child. The mutation responsible was a de novo alpha 28 Arg-->Cys substitution (CGT-->TGT) in spectrin, a mutation known to cause hereditary elliptocytosis or hereditary pyroPoikilocytosis. In this particular case the severity of the manifestations were accounted for by the occurrence, in trans to the alpha 28 mutation, of the alpha V/41 polymorphism. The latter has been shown previously to be associated with structural abnormalities at the alpha IV-alpha V domain junction and with a low expression level. The pronounced alteration of the dimer self association process was also explained by the location of the alpha 28 mutation. This mutation occurs in helix 3 of repeating segment alpha 1, e.g. precisely in the head-to-head contact between the spectrin alpha and beta chains. The present phenotype was compared to that yielded by another alpha 28 mutation (Arg-->His) also combined, in trans, with the alpha V/41 polymorphism. The pictures were very much alike, stressing the functional importance of residue alpha 28. The de novo character of the present mutation strengthens the view that codon alpha 28 is a 'hot spot' for mutations.
A Iolascon - One of the best experts on this subject based on the ideXlab platform.
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a genomic deletion causes truncation of α spectrin and ellipto Poikilocytosis
Blood Cells Molecules and Diseases, 2011Co-Authors: A Iolascon, M J King, S Robertson, R A Avvisati, F Vitiello, R Asci, M N Scoppettuolo, J DelaunayAbstract:We report on a truncated α-spectrin chain, spectrin(Exeter), associated with ellipto-Poikilocytosis. Analysis of erythrocyte membranes of affected individuals revealed a truncated α-spectrin chain with normal amounts of spectrin dimer. In the proband and her father, one haploid set of α-spectrin cDNA lacked exons 11 and 12, leading to partial deletion of repeats α4 and α5 (83 amino acids) of the α-spectrin chain. In one allele of genomic DNA, a 3567bp deletion starting in intron 10 and ending in intron 12 of the SPTA1 gene was found. The common polymorphic SPTA1 α(LELY) allele was found in trans to the SPTA1αExeter allele in the proband. The proband had inherited the SPTA1Exeter allele from her father and the αLELY allele from her healthy, asymptomatic mother. This is the first report of an interstitial deletion in the SPTA1 gene associated with ellipto-Poikilocytosis.
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Severe Poikilocytosis Associated With A Denovo Alpha-28 Arg-]cys Mutation In Spectrin
'Wiley', 1993Co-Authors: F. Lorenzo, Nicole Alloisio, L Morle, A Iolascon, E. M. Delgiudice, A. Forissier, S. Perrotta, G. Sciarratta, J DelaunayAbstract:Severe Poikilocytosis was observed in an Italian child. The mutation responsible was a de novo alpha28 Arg --> Cys substitution (CGT --> TGT) in spectrin, a mutation known to cause hereditary elliptocytosis or hereditary pyroPoikilocytosis. In this particular case the severity of the manifestations were accounted for by the occurrence, in trans to the alpha28 mutation, of the alpha(V/41) polymorphism. The latter has been shown previously to be associated with structural abnormalities at the alphaIV-alphaV domain junction and with a low expression level. The pronounced alteration of the dimer self association process was also explained by the location of the alpha28 mutation. This mutation occurs in helix 3 of repeating segment alpha1, e.g. precisely in the head-to-head contact between the spectrin alpha and beta chains. The present phenotype was compared to that yielded by another alpha28 mutation (Arg --> His) also combined, in trans, with the alpha(V/41) polymorphism. The pictures were very much alike, stressing the functional importance of residue alpha28. The de novo character of the present mutation strengthens the view that codon alpha28 is a 'hot spot' for mutations
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severe Poikilocytosis associated with a de novo alpha 28 arg cys mutation in spectrin
British Journal of Haematology, 1993Co-Authors: F. Lorenzo, Nicole Alloisio, L Morle, A Iolascon, A. Forissier, S. Perrotta, G. Sciarratta, Miraglia E Del Giudice, J DelaunayAbstract:Severe Poikilocytosis was observed in an Italian child. The mutation responsible was a de novo alpha 28 Arg-->Cys substitution (CGT-->TGT) in spectrin, a mutation known to cause hereditary elliptocytosis or hereditary pyroPoikilocytosis. In this particular case the severity of the manifestations were accounted for by the occurrence, in trans to the alpha 28 mutation, of the alpha V/41 polymorphism. The latter has been shown previously to be associated with structural abnormalities at the alpha IV-alpha V domain junction and with a low expression level. The pronounced alteration of the dimer self association process was also explained by the location of the alpha 28 mutation. This mutation occurs in helix 3 of repeating segment alpha 1, e.g. precisely in the head-to-head contact between the spectrin alpha and beta chains. The present phenotype was compared to that yielded by another alpha 28 mutation (Arg-->His) also combined, in trans, with the alpha V/41 polymorphism. The pictures were very much alike, stressing the functional importance of residue alpha 28. The de novo character of the present mutation strengthens the view that codon alpha 28 is a 'hot spot' for mutations.
F. Lorenzo - One of the best experts on this subject based on the ideXlab platform.
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Severe Poikilocytosis Associated With A Denovo Alpha-28 Arg-]cys Mutation In Spectrin
'Wiley', 1993Co-Authors: F. Lorenzo, Nicole Alloisio, L Morle, A Iolascon, E. M. Delgiudice, A. Forissier, S. Perrotta, G. Sciarratta, J DelaunayAbstract:Severe Poikilocytosis was observed in an Italian child. The mutation responsible was a de novo alpha28 Arg --> Cys substitution (CGT --> TGT) in spectrin, a mutation known to cause hereditary elliptocytosis or hereditary pyroPoikilocytosis. In this particular case the severity of the manifestations were accounted for by the occurrence, in trans to the alpha28 mutation, of the alpha(V/41) polymorphism. The latter has been shown previously to be associated with structural abnormalities at the alphaIV-alphaV domain junction and with a low expression level. The pronounced alteration of the dimer self association process was also explained by the location of the alpha28 mutation. This mutation occurs in helix 3 of repeating segment alpha1, e.g. precisely in the head-to-head contact between the spectrin alpha and beta chains. The present phenotype was compared to that yielded by another alpha28 mutation (Arg --> His) also combined, in trans, with the alpha(V/41) polymorphism. The pictures were very much alike, stressing the functional importance of residue alpha28. The de novo character of the present mutation strengthens the view that codon alpha28 is a 'hot spot' for mutations
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severe Poikilocytosis associated with a de novo alpha 28 arg cys mutation in spectrin
British Journal of Haematology, 1993Co-Authors: F. Lorenzo, Nicole Alloisio, L Morle, A Iolascon, A. Forissier, S. Perrotta, G. Sciarratta, Miraglia E Del Giudice, J DelaunayAbstract:Severe Poikilocytosis was observed in an Italian child. The mutation responsible was a de novo alpha 28 Arg-->Cys substitution (CGT-->TGT) in spectrin, a mutation known to cause hereditary elliptocytosis or hereditary pyroPoikilocytosis. In this particular case the severity of the manifestations were accounted for by the occurrence, in trans to the alpha 28 mutation, of the alpha V/41 polymorphism. The latter has been shown previously to be associated with structural abnormalities at the alpha IV-alpha V domain junction and with a low expression level. The pronounced alteration of the dimer self association process was also explained by the location of the alpha 28 mutation. This mutation occurs in helix 3 of repeating segment alpha 1, e.g. precisely in the head-to-head contact between the spectrin alpha and beta chains. The present phenotype was compared to that yielded by another alpha 28 mutation (Arg-->His) also combined, in trans, with the alpha V/41 polymorphism. The pictures were very much alike, stressing the functional importance of residue alpha 28. The de novo character of the present mutation strengthens the view that codon alpha 28 is a 'hot spot' for mutations.
D T Nomura - One of the best experts on this subject based on the ideXlab platform.
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haematological alterations of leporinus macrocephalus osteichtyes anostomidae naturally infected by goezia leporini nematoda anisakidae in fish pond
Arquivo Brasileiro De Medicina Veterinaria E Zootecnia, 2004Co-Authors: Mauricio Laterca Martins, Eduardo Makoto Onaka, Marcos Tavaresdias, Rodrigo Yudi Fujimoto, D T NomuraAbstract:The effect of Goezia leporini Martins & Yoshitoshi, 2003 (Nematoda: Anisakidae) infection on the haematological characteristics of cultivated Leporinus macrocephalus (Osteichthyes:Anostomidae) was studied. Paleness of gills, kidneys, liver and heart, black spots on the kidney and accumulation of fluid in the visceral cavity, stomach and intestines were observed. Gall bladder content had pale and translucent aspect. Strong and slight positive correlations between number of nematodes and fish weight were estimated within the 0-100g and 100-200g fish weight group, respectively. Blood smears from infected fish showed variation in erythrocyte size (anisocytosis) and shape (Poikilocytosis), and also dividing erythrocytes. No significant alteration (P>0.05) was shown as to erythrocyte, leukocyte count, haemoglobin concentration and thrombocyte and monocyte percentage. Parasite infection provoked significant reduction (P<0.05) in hematocrit, mean corpuscular volume, mean corpuscular haemoglobin concentration and lymphocyte percentage. On the other hand, significant increase (P<0.05) in neutrophil and eosinophil percentage in circulating blood of infected fish was observed. This is the first report regarding haematology of nematode infected freshwater cultivated fish in Brazil.
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Haematological alterations of Leporinus macrocephalus (Osteichtyes: Anostomidae) naturally infected by Goezia leporini (Nematoda: Anisakidae) in fish pond Alterações hematológicas em Leporinus macrocephalus (Osteichtyes: Anostomidae) infectado naturalmente por Goezia leporini (Nematoda: Anisakidae) em viveiro de piscicultura
Universidade Federal de Minas Gerais, 2004Co-Authors: Mauricio Laterca Martins, Eduardo Makoto Onaka, Rodrigo Yudi Fujimoto, M. Tavares-dias, D T NomuraAbstract:The effect of Goezia leporini Martins & Yoshitoshi, 2003 (Nematoda: Anisakidae) infection on the haematological characteristics of cultivated Leporinus macrocephalus (Osteichthyes:Anostomidae) was studied. Paleness of gills, kidneys, liver and heart, black spots on the kidney and accumulation of fluid in the visceral cavity, stomach and intestines were observed. Gall bladder content had pale and translucent aspect. Strong and slight positive correlations between number of nematodes and fish weight were estimated within the 0-100g and 100-200g fish weight group, respectively. Blood smears from infected fish showed variation in erythrocyte size (anisocytosis) and shape (Poikilocytosis), and also dividing erythrocytes. No significant alteration (P>0.05) was shown as to erythrocyte, leukocyte count, haemoglobin concentration and thrombocyte and monocyte percentage. Parasite infection provoked significant reduction (P
L Morle - One of the best experts on this subject based on the ideXlab platform.
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severe hereditary spherocytosis and distal renal tubular acidosis associated with the total absence of band 3
Blood, 2000Co-Authors: Maria Leticia Ribeiro, Nicole Alloisio, Helena Almeida, Clara Gomes, P Texier, Carlos Lemos, Gabriela Mimoso, L Morle, Faiza Beycabet, Renecharles RudigozAbstract:Absence of band 3, associated with the mutation Coimbra (V488M) in the homozygous state, caused severe hereditary spherocytosis in a young child. Although prenatal testing was made available to the parents, it was declined. Because the fetus stopped moving near term, an emergency cesarean section was performed and a severely anemic, hydropic female baby was delivered. She was resuscitated and initially kept alive with respiratory assistance and hypertransfusion therapy. Cord blood smears revealed erythroblastosis, Poikilocytosis, and red cells with stalk-like elongations. Band 3 and protein 4.2 were absent; spectrin, ankyrin, and glycophorin A were significantly reduced. Renal tubular acidosis was detected by the age of 3 months. Nephrocalcinosis appeared soon thereafter. After 3 years of follow-up the child is doing reasonably well on a regimen that includes regular blood transfusions and daily bicarbonate supplements. The long-term prognosis remains uncertain given the potential for hematologic and renal complications.
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Severe Poikilocytosis Associated With A Denovo Alpha-28 Arg-]cys Mutation In Spectrin
'Wiley', 1993Co-Authors: F. Lorenzo, Nicole Alloisio, L Morle, A Iolascon, E. M. Delgiudice, A. Forissier, S. Perrotta, G. Sciarratta, J DelaunayAbstract:Severe Poikilocytosis was observed in an Italian child. The mutation responsible was a de novo alpha28 Arg --> Cys substitution (CGT --> TGT) in spectrin, a mutation known to cause hereditary elliptocytosis or hereditary pyroPoikilocytosis. In this particular case the severity of the manifestations were accounted for by the occurrence, in trans to the alpha28 mutation, of the alpha(V/41) polymorphism. The latter has been shown previously to be associated with structural abnormalities at the alphaIV-alphaV domain junction and with a low expression level. The pronounced alteration of the dimer self association process was also explained by the location of the alpha28 mutation. This mutation occurs in helix 3 of repeating segment alpha1, e.g. precisely in the head-to-head contact between the spectrin alpha and beta chains. The present phenotype was compared to that yielded by another alpha28 mutation (Arg --> His) also combined, in trans, with the alpha(V/41) polymorphism. The pictures were very much alike, stressing the functional importance of residue alpha28. The de novo character of the present mutation strengthens the view that codon alpha28 is a 'hot spot' for mutations
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severe Poikilocytosis associated with a de novo alpha 28 arg cys mutation in spectrin
British Journal of Haematology, 1993Co-Authors: F. Lorenzo, Nicole Alloisio, L Morle, A Iolascon, A. Forissier, S. Perrotta, G. Sciarratta, Miraglia E Del Giudice, J DelaunayAbstract:Severe Poikilocytosis was observed in an Italian child. The mutation responsible was a de novo alpha 28 Arg-->Cys substitution (CGT-->TGT) in spectrin, a mutation known to cause hereditary elliptocytosis or hereditary pyroPoikilocytosis. In this particular case the severity of the manifestations were accounted for by the occurrence, in trans to the alpha 28 mutation, of the alpha V/41 polymorphism. The latter has been shown previously to be associated with structural abnormalities at the alpha IV-alpha V domain junction and with a low expression level. The pronounced alteration of the dimer self association process was also explained by the location of the alpha 28 mutation. This mutation occurs in helix 3 of repeating segment alpha 1, e.g. precisely in the head-to-head contact between the spectrin alpha and beta chains. The present phenotype was compared to that yielded by another alpha 28 mutation (Arg-->His) also combined, in trans, with the alpha V/41 polymorphism. The pictures were very much alike, stressing the functional importance of residue alpha 28. The de novo character of the present mutation strengthens the view that codon alpha 28 is a 'hot spot' for mutations.