This Article Full Text Alert me when this article is cited Alert me if a correction is posted Citation Map 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 Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Beggs, A. H. Search for Related Content PubMed PubMed Citation Articles by Beggs, A. H.

(Circulation. 1997;95:2344-2347.)
© 1997 American Heart Association, Inc.

Articles

Dystrophinopathy, The Expanding Phenotype

Dystrophin Abnormalities in X-Linked Dilated Cardiomyopathy

Alan H. Beggs, PhD

the Division of Genetics, Children's Hospital and Department of Pediatrics, Harvard Medical School, Boston, Mass.

Correspondence to Alan H. Beggs, PhD, Genetics Division, Children's Hospital, 300 Longwood Ave, Boston, MA 02115. E-mail beggs@rascal.med.harvard.edu

Key Words: Editorials • genes • cardiomyopathy • dystrophin

	Introduction

 
Advances in diagnostic methodologies are constantly changing our definitions of disease entities. In particular, the nosology of the muscular dystrophies has been subject to much change as molecular genetics has provided us with the tools to define these disorders on the basis of their underlying molecular defects. Identification of dystrophin as the protein mutated in DMD has led to the appreciation of a wide range of clinical presentations associated with dystrophin gene mutations.¹ The term "dystrophinopathy" is now commonly used to describe these allelic disorders that can range from classic DMD to clinically silent cases of elevated serum CK. Most recently, it has become clear that a significant proportion of cases of XLDCM may be caused by underlying dystrophin gene defects, thus further expanding the spectrum of dystrophin-related phenotypes.

Idiopathic dilated cardiomyopathy generally presents with congestive heart failure secondary to an increase in ventricular size and impairment of ventricular function. It is a leading cause of cardiovascular morbidity and mortality, with an estimated prevalence of 36.5/100 000 in the United States.² Traditionally, most cases have been considered to be sporadic, but recent studies³ have demonstrated that up to 20% of cases may be familial in nature, suggesting a strong genetic component for this group of diseases. Inheritance patterns vary and may be X-linked, autosomal dominant, or autosomal recessive. One remarkable pedigree with XLDCM was reported by Berko and Swift in 1987.⁴ Affected males presented in their late teens to early 20s with syncope and rapidly progressive congestive heart failure, leading . . . [Full Text of this Article]

This article has been cited by other articles:

				N. H. Robin, P. B. Tabereaux, R. Benza, and B. R. Korf Genetic Testing in Cardiovascular Disease J. Am. Coll. Cardiol., August 21, 2007; 50(8): 727 - 737. [Abstract] [Full Text] [PDF]

				W. Burke Genomics as a Probe for Disease Biology N. Engl. J. Med., September 4, 2003; 349(10): 969 - 974. [Full Text] [PDF]

				J. A. Towbin A noninvasive means of detecting preclinical cardiomyopathy in Duchenne muscular dystrophy? J. Am. Coll. Cardiol., July 16, 2003; 42(2): 317 - 318. [Full Text] [PDF]

				C.A. MacRae Genetics and dilated cardiomyopathy: limitations of candidate gene strategies Eur. Heart J., November 2, 2000; 21(22): 1817 - 1819. [PDF]

				C. Badorff, B. Fichtlscherer, R. E. Rhoads, A. M. Zeiher, A. Muelsch, S. Dimmeler, and K. U. Knowlton Nitric Oxide Inhibits Dystrophin Proteolysis by Coxsackieviral Protease 2A Through S-Nitrosylation : A Protective Mechanism Against Enteroviral Cardiomyopathy Circulation, October 31, 2000; 102(18): 2276 - 2281. [Abstract] [Full Text] [PDF]

				G.-H. Lee, C. Badorff, and K. U. Knowlton Dissociation of Sarcoglycans and the Dystrophin Carboxyl Terminus From the Sarcolemma in Enteroviral Cardiomyopathy Circ. Res., September 15, 2000; 87(6): 489 - 495. [Abstract] [Full Text] [PDF]

				C. Badorff, N. Berkely, S. Mehrotra, J. W. Talhouk, R. E. Rhoads, and K. U. Knowlton Enteroviral Protease 2A Directly Cleaves Dystrophin and Is Inhibited by a Dystrophin-based Substrate Analogue J. Biol. Chem., April 6, 2000; 275(15): 11191 - 11197. [Abstract] [Full Text] [PDF]