SEARCH:   Advanced

Prepublished online as a Blood First Edition Paper on March 20, 2003; DOI 10.1182/blood-2002-07-2288. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-07-2288v1 102/1/353    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Corrons, J.-L. V. Articles by Beutler, E. Search for Related Content PubMed PubMed Citation Articles by Corrons, J.-L. V. Articles by Beutler, E. Related Collections Red Cells Clinical Trials and Observations Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 1 July 2003, Vol. 102, No. 1, pp. 353-356 RED CELLS Red cell adenylate kinase deficiency: molecular study of 3 new mutations (118G>A, 190G>A, and GAC deletion) associated with hereditary nonspherocytic hemolytic anemia Joan-Lluis Vives Corrons, Estefania Garcia, Joan J. Tusell, Kottayil I. Varughese, Carol West, and Ernest Beutler From the Red Cell Pathology Unit, Hospital Clinic i Provincial, Institut d'Investigacions Biomèdiques August Pi i Sunyer (IDIBAPS), Barcelona, Spain; the Haematology Department, Hospital Materno-Infantil Vall d'Hebron, Barcelona, Spain; and The Scripps Research Institute, Department of Molecular and Experimental Medicine, La Jolla, CA. We report here 2 patients with chronic nonspherocytic hemolytic anemia (CNSHA) and severe red blood cell (RBC) adenylate kinase (AK) deficiency. One of these patients, a boy of Spanish origin, exhibited a neonatal icterus and splenomegaly and required blood transfusions until the age of 2 years. The other patient was a white, American infant born to parents who were first cousins; he also presented with neonatal icterus and anemia. In neither case was psychomotor impairment observed. The first patient was found to be a compound heterozygote for 2 different missense mutations, 118G>A(Gly40Arg) and 190G>A(Gly64Arg) (cDNA sequence first described by Matsuura et al, 1989). The second patient was homozygous for an in-frame deletion (GAC) from nucleotide (nt) 498 to 500 or nt 501 to 503 of the cDNA sequence, predicting deletion of either aspartic acid (Asp) 140 or 141. The crystal structure of porcine cytosolic AK was used as a molecular model to investigate how these mutations may affect enzyme structure and function. (Blood. 2003;102:353-356) CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: Y.-W. Tan, J. A. Hanson, and H. Yang Direct Mg2+ Binding Activates Adenylate Kinase from Escherichia coli J. Biol. Chem., January 30, 2009; 284(5): 3306 - 3313. [Abstract] [Full Text] [PDF]

	Copyright © 2003 by American Society of Hematology         Online ISSN: 1528-0020