CTF1

Case Study 1: Mohammad Abdul-Ghani, 2017

The post-natal heart adapts to stress and overload through hypertrophic growth, a process that may be pathologic or beneficial (physiologic hypertrophy). Physiologic hypertrophy improves cardiac performance in both healthy and diseased individuals, yet the mechanisms that propagate this favorable adaptation remain poorly defined. The researchers identify the cytokine cardiotrophin 1 (CT1) as a factor capable of recapitulating the key features of physiologic growth of the heart including transient and reversible hypertrophy of the myocardium, and stimulation of cardiomyocyte-derived angiogenic signals leading to increased vascularity. The capacity of CT1 to induce physiologic hypertrophy originates from a CK2-mediated restraining of caspase activation, preventing the transition to unrestrained pathologic growth. Exogenous CT1 protein delivery attenuated pathology and restored contractile function in a severe model of right heart failure, suggesting a novel treatment option for this intractable cardiac disease.

Fig1. Primary neonatal cardiomyocytes were stimulated for 24 h with hCT1 (0.5 nM), PE (100 μM), hCT1 and PE, or control serum-free medium (Ctrl, SF) followed by morphometric analysis.

Fig2. Significant differences were observed between the PAH-induced SUHx rat groups (hCT1 or PBS) and the control rat group.

Case Study 2: Darren H Freed, 2011

Chemotactic movement of myofibroblasts is recognized as a common means for their sequestration to the site of tissue injury. Following myocardial infarction (MI), recruitment of cardiac myofibroblasts to the infarct scar is a critical step in wound healing. Contractile myofibroblasts express embryonic smooth muscle myosin, α-smooth muscle actin, as well as collagens I and III. The researchers examined the effects of cardiotrophin-1 (CT-1) in the induction of primary rat ventricular myofibroblast motility. Changes in membrane potential (E(m)) and Ca(2+) entry were studied to reveal the mechanisms for induction of myofibroblast migration. CT-1-induced cardiac myofibroblast cell migration, which was attenuated through the inhibition of JAK2 (25 μM AG490), and myosin light chain kinase (20 μM ML-7). Inhibition of K(+) channels (1 mM tetraethylammonium or 100 μM 4-aminopyridine) and nonselective cation channels by 10 μM gadolinium (Gd(3+)) significantly reduced migration in the presence of CT-1. CT-1 treatment caused a significant increase in myosin light chain phosphorylation, which could be inhibited by incubation in Ca(2+)-free conditions or by application of AG490, ML-7, and W7 (100 μM; calmodulin inhibitor).

Fig3. CT-1 induces phosphorylation of MLC. Cardiac ventricular myofibroblasts were stimulated with CT-1 (10 ng/ml = 0.37 nM).

Fig4. Effect of CT-1 on membrane potential.

Fig1. Proposed model of hCT1-mediated physiologic cardiac hypertrophy. (Mohammad Abdul-Ghani, 2017)

Fig2. Schematic representation of the production and actions of cardiotrophin-1 (CT-1) in the myocardium. (Arantxa González, 2012)

CTF1 involved in several pathways and played different roles in them. We selected most pathways CTF1 participated on our site, such as Cytokine-cytokine receptor interaction, Jak-STAT signaling pathway, MicroRNAs in cardiomyocyte hypertrophy, which may be useful for your reference. Also, other proteins which involved in the same pathway with CTF1 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

CTF1 has several biochemical functions, for example, cytokine activity, leukemia inhibitory factor receptor binding, protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by CTF1 itself. We selected most functions CTF1 had, and list some proteins which have the same functions with CTF1. You can find most of the proteins on our site.

CTF1 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with CTF1 here. Most of them are supplied by our site. Hope this information will be useful for your research of CTF1.

MAGEA6