Canine elliptocytosis due to a mutant beta-spectrin

• Published in: Veterinary clinical pathology Vol. 38; no. 1; pp. 52 - 58
• Main Authors: Di Terlizzi, Roberta, Gallagher, Patrick G, Mohandas, Narla, Steiner, Laurie A, Dolce, Karen S, Guo, Xinhua, Wilkerson, Melinda J, Stockham, Steven L
• Format: Journal Article
• Language: English
• Published: Malden, USA Blackwell Publishing Inc 01.03.2009
• Subjects: amino acid sequences; Animals; beta-spectrin; case studies; cell membranes; codons; Dog; dog diseases; Dog Diseases - pathology; Dogs; elliptocyte; elliptocytosis; Elliptocytosis, Hereditary - pathology; Elliptocytosis, Hereditary - veterinary; erythrocyte; Erythrocyte Membrane - physiology; erythrocytes; Erythrocytes - ultrastructure; Female; females; genes; genetic disorders; lameness; membrane; molecular sequence data; mutation; nucleotide sequences; ovalocyte; protein binding; signs and symptoms (animals and humans); spectrin; Spectrin - genetics
• ISSN: 0275-6382; 1939-165X
• DOI: 10.1111/j.1939-165X.2008.00092.x

: A 5‐year‐old, spayed female, mixed‐breed dog with persistent elliptocytosis was evaluated at the Veterinary Medical Teaching Hospital at Kansas State University. The elliptocytosis was asymptomatic and was detected during the evaluation of lameness. When subjected to shear stress in an ektacytometer, the dog's erythrocytes had reduced cellular deformability and erythrocyte membranes had decreased mechanical stability. Analysis of erythrocyte membrane spectrin by nondenaturing gel electrophoresis revealed an increased amount of spectrin dimers, indicating a defect in spectrin self‐association. DNA analysis detected a β‐spectrin mutation in codon 2110 in which threonine was replaced by methionine. This mutation likely altered the molecular structure of the erythrocyte membrane, leading to impaired spectrin self‐association and elliptocyte formation.