scholarly journals Sarcolemma instability during mechanical activity in Large myd cardiac myocytes with loss of dystroglycan extracellular matrix receptor function

2011 ◽  
Vol 20 (17) ◽  
pp. 3346-3355 ◽  
Author(s):  
Zhyldyz Kabaeva ◽  
Kailyn E. Meekhof ◽  
Daniel E. Michele
Keyword(s):  
Extracellular Matrix ◽  
Cardiac Myocytes ◽  
Mechanical Activity ◽  
Receptor Function

Cardiac myocytes cultured on a basement membrane extract of the ehs tumor

1986 ◽  
Vol 44 ◽  
pp. 270-271
Author(s):  
L. Terracio ◽  
A. Dewey ◽  
K. Rubin ◽  
T.K. Borg
Keyword(s):  
Extracellular Matrix ◽  
Basement Membrane ◽  
Cardiac Myocytes ◽  
Normal Tissue ◽  
Cell Spreading ◽  
Collagen Iv ◽  
Basement Membrane Extract ◽  
Membrane Extract ◽  
Growth Development ◽  
Multicellular Organisms

The recognition and interaction of cells with the extracellular matrix (ECM) effects the normal physiology as well as the pathology of all multicellular organisms. These interactions have been shown to influence the growth, development, and maintenance of normal tissue function. In previous studies, we have shown that neonatal cardiac myocytes specifically interacts with a variety of ECM components including fibronectin, laminin, and collagens I, III and IV. Culturing neonatal myocytes on laminin and collagen IV induces an increased rate of both cell spreading and sarcomerogenesis.

scholarly journals Cytoskeletal modulation of electrical and mechanical activity in cardiac myocytes

2004 ◽  
Vol 84 (1) ◽  
pp. 29-59 ◽  
Author(s):  
S.C. Calaghan ◽  
J.-Y. Le Guennec ◽  
E. White
Keyword(s):  
Cardiac Myocytes ◽  
Mechanical Activity

Localization of cardiac (alpha)-myosin heavy chain mRNA is regulated by its 3′ untranslated region via mechanical activity and translational block

1997 ◽  
Vol 110 (23) ◽  
pp. 2969-2978 ◽  
Author(s):  
P. Goldspink ◽  
W. Sharp ◽  
B. Russell
Keyword(s):  
Myosin Heavy Chain ◽  
Cardiac Myocytes ◽  
Heavy Chain ◽  
Untranslated Region ◽  
Contractile Activity ◽  
Intracellular Localization ◽  
Mechanical Activity ◽  
Mrna Levels ◽  
Coding Region ◽  
Reporter Protein

We have altered the spontaneous contractile activity of neonatal cardiac myocytes in culture to investigate the re-lationship between mechanical forces, myofibril assembly, and the localization and translation of (alpha)-myosin heavy chain mRNA. Immunofluorescence and in situ hybridization techniques revealed that contracting myocytes display well aligned myofibrils and a diffuse distribution of (alpha)-myosin heavy chain mRNA. Inhibition of contractile activity with the calcium channel blocker verapamil (10 microM) resulted in myofibril disassembly and a perinuclear mRNA distribution within six hours. There was a significant decrease (P<0. 05) of mRNA levels, 5 to 15 micron away from the nucleus following 6 hours of verapamil treatment compared with control cells. Inhibition of protein synthesis with cycloheximide (10 microM) also resulted in perinuclear mRNA localization despite having little effect on contractile activity or myofibril assembly. To determine if the 3′ untranslated region of (alpha)-myosin heavy chain mRNA was sufficient for localizing the entire message, a chimeric construct composed of beta-galactosidase coding region followed by (alpha)-myosin heavy chain 3′ untranslated region sequences was made as a reporter plasmid and transfected into cultured myocytes. A perinuclear accumulation of ss-galactosidase was exhibited in many of the contractile arrested cells (48.3+/−2.4%, n=7). In contrast, significantly fewer (P<0.05) contracting control (29.1+/−3.3%, n=7) and strongly contracting, isoproterenol-treated cells (27.2+/−6.1%, n=3) exhibited a perinuclear localization of protein. The distribution of the reporter protein was not affected by the contractile state in cells transfected with a constitutively translated 3′UTR. We propose that mechanical activity of neonatal cardiac myocytes regulates the intracellular localization of alpha-myosin heavy chain mRNA via the 3′ untranslated region mediated by an initial block in translation.

scholarly journals Adhesive activity of Lu glycoproteins is regulated by interaction with spectrin

Blood ◽  
2008 ◽  
Vol 112 (13) ◽  
pp. 5212-5218 ◽  
Author(s):  
Xiuli An ◽  
Emilie Gauthier ◽  
Xihui Zhang ◽  
Xinhua Guo ◽  
David J. Anstee ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Blood Group ◽  
Molecular Basis ◽  
Functional Role ◽  
Direct Interaction ◽  
Cytoplasmic Tail ◽  
Receptor Function ◽  
Binding Motifs ◽  
Functional Consequences

Abstract The Lutheran (Lu) and Lu(v13) blood group glycoproteins function as receptors for extracellular matrix laminins. Lu and Lu(v13) are linked to the erythrocyte cytoskeleton through a direct interaction with spectrin. However, neither the molecular basis of the interaction nor its functional consequences have previously been delineated. In the present study, we defined the binding motifs of Lu and Lu(v13) on spectrin and identified a functional role for this interaction. We found that the cytoplasmic domains of both Lu and Lu(v13) bound to repeat 4 of the α spectrin chain. The interaction of full-length spectrin dimer to Lu and Lu(v13) was inhibited by repeat 4 of α-spectrin. Further, resealing of this repeat peptide into erythrocytes led to weakened Lu-cytoskeleton interaction as demonstrated by increased detergent extractability of Lu. Importantly, disruption of the Lu-spectrin linkage was accompanied by enhanced cell adhesion to laminin. We conclude that the interaction of the Lu cytoplasmic tail with the cytoskeleton regulates its adhesive receptor function.

The Expression and Role of Protein Kinase C in Neonatal Cardiac Myocyte Attachment, Cell Volume, and Myofibril Formation Is Dependent on the Composition of the Extracellular Matrix

2005 ◽  
Vol 11 (3) ◽  
pp. 224-234 ◽  
Author(s):  
Tara A. Bullard ◽  
Thomas K. Borg ◽  
Robert L. Price
Keyword(s):  
Extracellular Matrix ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Volume ◽  
Cardiac Myocytes ◽  
Cardiac Myocyte ◽  
Dynamic Component ◽  
Laminin 5 ◽  
Kinase C

The extracellular matrix (ECM) is a dynamic component of tissues that influences cellular phenotype and behavior. We sought to determine the role of specific ECM substrates in the regulation of protein kinase C (PKC) isozyme expression and function in cardiac myocyte attachment, cell volume, and myofibril formation. PKC isozyme expression was ECM substrate specific. Increasing concentrations of the PKC δ inhibitor rottlerin attenuated myocyte attachment to randomly organized collagen (1, 5, and 10 μM), laminin (5 and 10 μM), aligned collagen (5 and 10 μM), and fibronectin (10 μM). Rottlerin significantly decreased cell volume on laminin and randomly organized collagen, and inhibited myofibril formation on laminin. The PKC α inhibitor Gö 6976 inhibited attachment to randomly organized collagen at 6 nM but did not affect cell volume. The general PKC inhibitor Bisindolylmalemide I (10 and 30 μM) did not affect myocyte attachment; however, it significantly decreased cell volume on randomly organized collagen. Our data indicate that PKC isozymes are expressed and utilized by neonatal cardiac myocytes during attachment, cell growth, and myofibril formation. Specifically, it appears that PKC δ and/or its downstream effectors play an important role in the interaction between cardiac myocytes and laminin, providing further evidence that the ECM influences cardiac myocyte behavior.

Dense fibrillar collagen matrices to analyse extracellular matrix receptor function

2012 ◽  
Vol 60 (1) ◽  
pp. 7-14 ◽  
Author(s):  
C. Helary ◽  
B. Rodrigues-Sanchez ◽  
S. Vigier ◽  
M.-M. Giraud Guille
Keyword(s):  
Extracellular Matrix ◽  
Fibrillar Collagen ◽  
Receptor Function ◽  
Collagen Matrices
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