scholarly journals Dynamic patterns of expression of BMP isoforms 2, 4, 5, 6, and 7 during chicken heart development

2004 ◽  
Vol 279A (1) ◽  
pp. 636-651 ◽  
Author(s):  
Semir Somi ◽  
Anita A.M. Buffing ◽  
Antoon F.M. Moorman ◽  
Maurice J.B. Van Den Hoff
Keyword(s):  
Heart Development ◽  
Chicken Heart ◽  
Dynamic Patterns

scholarly journals Detection of a ventricular-specific myosin heavy chain in adult and developing chicken heart.

1986 ◽  
Vol 102 (4) ◽  
pp. 1480-1484 ◽  
Author(s):  
Y Zhang ◽  
S A Shafiq ◽  
D Bader
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Heart Development ◽  
In Ovo ◽  
Specific Expression ◽  
Adult Chicken ◽  
Chicken Heart ◽  
Developing Heart ◽  
Caudal Portion ◽  
Atrial Myosin

In the present study, a monoclonal antibody (McAb), ALD19, generated against myosin of slow tonic muscle, was shown to react with the heavy chain of ventricular myosin in the adult chicken heart. With this antibody, it was possible to detect a ventricular-specific myosin during myocardial differentiation and to show that the epitope recognized by ALD19 was present from the earliest stages of ventricular differentiation and maintained throughout development only in the ventricle. A second McAb, specific for atrial myosin heavy chain (MHC) (Gonzalez-Sanchez, A., and D. Bader, 1984, Dev. Biol., 103:151-158), was used as a control to detect an atrial-specific myosin in the caudal portion of the developing heart at Hamburger-Hamilton stage 15. It was found that the appearance of ventricular MHC predated the expression of atrial MHC by approximately 1 d in ovo and that specific MHCs were always differentially distributed. While a common primordial MHC may be present in the early heart, this study showed the tissue-specific expression of a ventricular MHC during the initial stages of heart development and its differential accumulation throughout development.

Isomyosin expression patterns in tubular stages of chicken heart development: a 3-D immunohistochemical analysis

1987 ◽  
Vol 177 (1) ◽  
pp. 81-90 ◽  
Author(s):  
F. Jong ◽  
W. J. C. Geerts ◽  
W. H. Lamers ◽  
J. A. Los ◽  
A. F. M. Moorman
Keyword(s):  
Heart Development ◽  
Expression Patterns ◽  
Immunohistochemical Analysis ◽  
Chicken Heart

Changes in force and calcium sensitivity in the developing avian heart

1991 ◽  
Vol 69 (11) ◽  
pp. 1692-1697 ◽  
Author(s):  
R. E. Godt ◽  
R. T. H. Fogaça ◽  
T. M. Nosek
Keyword(s):  
Young Adult ◽  
Heart Development ◽  
Troponin I ◽  
Calcium Sensitivity ◽  
Extracellular Calcium ◽  
Contractile Apparatus ◽  
Chicken Heart ◽  
Twitch Force ◽  
Adult Heart ◽  
Isoform Switching

The aim of this study was to characterize the development of the contractile properties of intact and chemically skinned muscle from chicken heart and to compare these characteristics with those of developing mammalian heart reported by others. Small trabeculae were dissected from left ventricles of Arbor Acre chickens between embryonic day 7 and young adulthood (7 weeks post-hatching). At all ages, increasing extracellular calcium (0.45–3.6 mM) progressively increased twitch force of electrically stimulated trabeculae. Twitch force at 1.8 mM extracellular calcium, normalized to cross-sectional area, increased to a maximum at 1 day post-hatching, remained constant through 3 weeks post-hatching, but then decreased at 7 weeks post-hatching. The maximal calcium-activated force of trabeculae chemically skinned with Triton X-100 detergent increased to a maximum 2 days before the time of hatching and was not significantly changed up to 7 weeks post-hatching. Over the ages studied, average twitch force in 1.8 mM calcium was between 26 and 66% of maximal calcium-activated force after skinning, suggesting that the contractile apparatus is not fully activated during the twitch in normal Ringer. In skinned trabeculae, the calcium sensitivity of the contractile apparatus was higher in the embryo than in the young adult. These age-dependent changes in calcium sensitivity are correlated with isoform switching in troponin T. A decrease in pH from 7.0 to 6.5 decreased the calcium sensitivity of the contractile apparatus to a greater degree in skinned trabeculae from young adult hearts than in those from embryonic hearts. This change in susceptibility to acidosis is temporally associated with isoform switching in troponin I. Moreover, the decrease in maximal calcium-activated force with pH was also greater in trabeculae from young adult heart. Thus the contractile apparatus of embryonic chicken heart is less sensitive to the depressant effects of acidosis than that of the adult heart. These developmental changes in calcium sensitivity are analogous to those reported by others in mammalian heart.Key words: muscle contraction, heart development, acidosis, chicken, contractile proteins.

scholarly journals Dynamic patterns of apoptosis in the developing chicken heart

2004 ◽  
Vol 229 (3) ◽  
pp. 489-499 ◽  
Author(s):  
Katherine S. Schaefer ◽  
Yong Qiu Doughman ◽  
Steven A. Fisher ◽  
Michiko Watanabe
Keyword(s):  
Chicken Heart ◽  
Dynamic Patterns

scholarly journals Expression Analysis of CITED2 mRNA During Chicken Heart Development

2007 ◽  
Vol 21 (5) ◽  
Author(s):  
Ke Yang ◽  
Yong‐Qiu Doughman ◽  
Syed Zaidi ◽  
Thomas Brand ◽  
Yu‐chung Yang ◽  
...  
Keyword(s):  
Expression Analysis ◽  
Heart Development ◽  
Chicken Heart

scholarly journals Expression of bone morphogenetic protein-10 mRNA during chicken heart development

2004 ◽  
Vol 279A (1) ◽  
pp. 579-582 ◽  
Author(s):  
Semir Somi ◽  
Anita A.M. Buffing ◽  
Antoon F.M. Moorman ◽  
Maurice J.B. Van Den Hoff
Keyword(s):  
Bone Morphogenetic Protein ◽  
Heart Development ◽  
Chicken Heart ◽  
Morphogenetic Protein

scholarly journals Patterns of Expression of the Follistatin and Follistatin-Like1 Genes During Chicken Heart Development: A Potential Role in Valvulogenesis and Late Heart Muscle Cell Formation

2007 ◽  
Vol 290 (7) ◽  
pp. 783-787 ◽  
Author(s):  
Gert Van Den Berg ◽  
Semir Somi ◽  
Anita A.M. Buffing ◽  
Antoon F.M. Moorman ◽  
Maurice J.B. Van Den Hoff
Keyword(s):  
Muscle Cell ◽  
Heart Development ◽  
Heart Muscle ◽  
Potential Role ◽  
Cell Formation ◽  
Heart Muscle Cell ◽  
Chicken Heart

scholarly journals Direct and Indirect Effects of Pseudoephedrine on the Intrinsic Conduction System of the Embryonic Chicken Heart

2015 ◽  
Vol 12 (3) ◽  
Author(s):  
Samely Gonzalez ◽  
Fatima Afzal ◽  
Jacqueline McLaughlin
Keyword(s):  
Heart Rate ◽  
Indirect Effects ◽  
Heart Development ◽  
Adrenergic Receptors ◽  
Nasal Congestion ◽  
Conduction System ◽  
Direct And Indirect Effects ◽  
Over The Counter ◽  
Chicken Heart ◽  
Intrinsic Conduction

Pseudoephedrine (PSE) is an over the counter (OTC) medication used to temporarily relieve nasal congestion, hay fever or other upper respiratory allergies by shrinking blood vessels in the nasal passages. Aside from its vasoconstriction properties it is also known to elevate heart rate, and blood pressure, thus being a sympathomimetic drug. There are two hypotheses on how this drug increases heart rate (HR): (1) a direct mechanism wherein PSE works by binding to adrenergic receptors in the heart’s intrinsic conduction system; and, (2) an indirect mechanism wherein PSE causes the release of norepinephrine from sympathetic nerves to activate adrenergic receptors. This research utilized the chick embryonic heart as a model system to examine the chronotropic effects and mechanisms of PSE on the developing vertebrate heart. Research suggests that this drug has both direct and indirect effects, and induces dangerous heart arrhythmias such as atrial flutter, in high doses. KEYWORDS: Pseudophedrine, Sympathomimetic Drugs, Pseudophedrine and Pregnancy, Pseudophedrine and Norepinephrine, Pseudophedrine Related Arrhythmias, Over–the-counter Drugs; Chick Heart Development

Forced expression of the homeodomain protein Gax inhibits cardiomyocyte proliferation and perturbs heart morphogenesis

Development ◽  
1997 ◽  
Vol 124 (21) ◽  
pp. 4405-4413 ◽  
Author(s):  
S.A. Fisher ◽  
E. Siwik ◽  
D. Branellec ◽  
K. Walsh ◽  
M. Watanabe
Keyword(s):  
Cell Cycle ◽  
Heart Development ◽  
Negative Regulator ◽  
Homeodomain Protein ◽  
Cardiomyocyte Proliferation ◽  
Heart Morphogenesis ◽  
Chicken Heart ◽  
Nuclear Expression ◽  
Compact Zone ◽  
Myocyte Proliferation

The development of the tubular heart into a complex four-chambered organ requires precise temporal and region-specific regulation of cell proliferation, migration, death and differentiation. While the regulatory mechanisms in heart morphogenesis are not well understood, increasing attention has focused on the homeodomain proteins, which are generally linked to morphogenetic processes. The homeodomain containing gene Gax has been shown to be expressed in heart and smooth muscle tissues. In this study, the Gax protein was detected in the nuclei of myocardial cells relatively late in chicken heart development, at a time when myocyte proliferation is declining. To test the hypothesis that the Gax protein functions as a negative regulator of cardiomyocyte proliferation, a replication-defective adenovirus was used to force its precocious nuclear expression during chicken heart morphogenesis. In experiments in which Gax- and beta-galactosidase-expressing adenoviruses were co-injected, clonal expansion of myocytes was reduced, consistent with inhibition of myocyte proliferation. This effect on proliferation was corroborated by the finding that the percentage of exogenous Gax-expressing myocytes that were positive for the cell cycle marker PCNA decreased over time and was lower than in control myocytes. The precocious nuclear expression of Gax in tubular hearts resulted in abnormal heart morphology, including small ventricles with rounded apices, a thinned compact zone and coarse trabeculae. These results suggest a role for the Gax protein in heart morphogenesis causing proliferating cardiomyocytes to withdraw from the cell cycle, thus influencing the size and shape that the heart ultimately attains.

scholarly journals NCAM polypeptides in heart development: association with Z discs of forms that contain the muscle-specific domain.

1995 ◽  
Vol 128 (1) ◽  
pp. 209-221 ◽  
Author(s):  
M K Byeon ◽  
Y Sugi ◽  
R R Markwald ◽  
S Hoffman
Keyword(s):  
Heart Development ◽  
Early Stage ◽  
Cytoplasmic Domain ◽  
Cell Contact ◽  
Isolated Cells ◽  
Specific Domain ◽  
Small Surface ◽  
Chicken Heart ◽  
Stage Of Development

Previous studies of neural cell adhesion molecule (NCAM) cDNAs have revealed an alternatively spliced set of small exons (12A, 12B, 12C, and 12D) that encode a region in the extracellular portion of the molecule known as the muscle-specific domain (MSD). The entire MSD region can be expressed in skeletal muscle, heart, and skin; only exons 12A and 12D have been found in brain. These studies did not reveal which NCAM polypeptides contain the MSD region or the immunohistochemical distribution of these NCAM molecules. To address these questions, we prepared antibodies against the oligopeptides encoded by exons 12A and 12B and by exons 12C and 12D, and we used these antibodies to study the forms of NCAM containing the MSD region expressed during embryonic chicken heart development. These antibodies recognize certain forms of NCAM found in the heart, but they do not recognize brain NCAM. In the heart, each of the splice variants of NCAM (large cytoplasmic domain, small cytoplasmic domain, and small surface domain) that differ in their mode of attachment to the plasma membrane or in the size of their cytoplasmic domain is expressed in a form that contains and in a form that lacks the MSD region. No microheterogeneity is observed in the size of NCAM molecules containing the MSD region, even at the level of cyanogen bromide fragments, suggesting that exons 12A-D are expressed as a single unit. Depending on the site and the stage of development, the percent of NCAM molecules containing the MSD region can vary from nearly 0 to 100%. In general, this percentage increases during development. In immunohistochemical studies of hearts from stage 18 embryos, forms of NCAM containing the MSD region colocalized with Z discs. No other adhesion molecules were found in this distribution at this early stage of development. Studies on isolated cells in vitro demonstrate that the colocalization with Z discs of NCAM molecules containing the MSD region does not depend on cell-cell contact, and they raise the possibility that this form of NCAM is involved in cell-extracellular matrix interactions. The association of NCAM molecules containing the MSD region with Z discs suggests that this form of NCAM is involved in early myofibrillogenesis.

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