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(Circulation Research. 2008;102:392.)
© 2008 American Heart Association, Inc.

Editorials

Disrupted Intercalated Discs

Is Kindlin-2 Required?

Cathy J. Hatcher, Craig T. Basson

From the Center for Molecular Cardiology, Greenberg Division of Cardiology, Weill Medical College of Cornell University, New York.

Correspondence to Craig T. Basson, MD, PhD, Director, Cardiovascular Research, Center for Molecular Cardiology, Greenberg Division of Cardiology, Weill Medical College of Cornell University, 1300 York Ave, New York, NY 10021. E-mail ctbasson@med. cornell.edu

See related article, pages 423–431

Key Words: intercalated discs • kindlin-2 • cardiomyopathy • integrin • cardiac development

An extract of the first 250 words of the full text is provided, because this article has no abstract.

Intermediate filaments are cytoskeletal structures that maintain the structural and mechanical integrity of cells, tissues, and organs. These filaments are associated with the nuclear surface but extend out into the cytoplasm and interact with other cytoskeletal elements and cytoplasmic organelles. Eventually, their impingement on the plasma membrane in certain tissues allows them to be tethered by specialized membrane structures, such as hemidesmosomes in epithelial cells, costameres in striated muscle, and intercalated discs in cardiac muscle.¹ At an intercalated disc, the cell membranes of 2 adjacent cardiomyocytes are extensively intertwined and bound together by gap junctions and desmosomes. These connections help stabilize the positions of the cells relative to each other and also help maintain the 3D structural integrity of the tissue. Thus, the intercalated discs ensure proper function of the heart with efficient ejection of blood with each contraction.

Kindlin-2, a member of the kindlin family of focal adhesion proteins, is expressed in cardiac muscle and is enriched at intercalated discs and costameres.² Kindlin-1 and kindlin-2 have been shown to play an essential role in integrin-mediated adhesion and spreading. Kindlin-2 can interact with integrin-linked kinase (ILK) and is also able to bind migfilin, a LIM domain–containing protein capable of binding Filamin.³ In this issue of Circulation Research, Dowling et al demonstrate a novel role for kindlin-2 in embryonic development as well as cardiac development and function.⁴ Complete loss of murine kindlin-2 produces embryonic lethality by embryonic day 7.5. These findings demonstrate the essential role of kindlin-2 in early embryogenesis, . . . [Full Text of this Article]

Related Article:

Kindlin-2 Is an Essential Component of Intercalated Discs and Is Required for Vertebrate Cardiac Structure and Function

James J. Dowling, Elizabeth Gibbs, Mark Russell, Daniel Goldman, Jeremy Minarcik, Jeffrey A. Golden, and Eva L. Feldman
Circ. Res. 2008 102: 423-431. [Abstract] [Full Text] [PDF]