scholarly journals Role of Calcium in Signal Transduction of Commelina Guard Cells.

1991 ◽  
pp. 333-344 ◽  
Author(s):  
S. Gilroy ◽  
M. D. Fricker ◽  
N. D. Read ◽  
A. J. Trewavas
Keyword(s):  
Signal Transduction ◽  
Guard Cells

Ca2+ signalling in stomatal guard cells

2000 ◽  
Vol 28 (4) ◽  
pp. 476-481 ◽  
Author(s):  
M. R. McAinsh ◽  
J. E. Gray ◽  
A. M. Hetherington ◽  
C. P. Leckie ◽  
C. Ng
Keyword(s):  
Signal Transduction ◽  
Guard Cell ◽  
Signal Transduction Pathway ◽  
Guard Cells ◽  
Stomatal Opening ◽  
Cell Turgor ◽  
Stomatal Guard Cells ◽  
External Stimuli ◽  
Spatial And Temporal Characteristics

Ca2+ is a ubiquitous second messenger in the signal transduction pathway(s) by which stomatal guard cells respond to external stimuli. Increases in guard-cell cytosolic free Ca2+ concentration ([Ca2+]cyt) have been observed in response to stimuli that cause both stomatal opening and closure. In addition, several important components of Ca2+-based signalling pathways have been identified in guard cells, including the cADP-ribose and phospholipase C/Ins(1,4,5)P3-mediated Ca2+-mobilizing pathways. The central role of stimulus-induced increases in [Ca2+]cyt in guard-cell signal transduction has been clearly demonstrated in experiments examining the effects of modulating increases in [Ca2+]cyt on alterations in guard-cell turgor or the activity of ion channels that act as effectors in the guard-cell turgor response. In addition, the paradox that Ca2+ is involved in the transduction of signals that result in opposite end responses (stomatal opening and closure) might be accounted for by the generation of stimulus-specific Ca2+ signatures, such that increases in [Ca2+]cyt exhibit unique spatial and temporal characteristics.

Role of Calcium in Signal Transduction of Commelina Guard Cells

1991 ◽  
Vol 3 (4) ◽  
pp. 333 ◽  
Author(s):  
Simon Gilroy ◽  
Mark D. Fricker ◽  
Nick D. Read ◽  
Anthony J. Trewavas
Keyword(s):  
Signal Transduction ◽  
Guard Cells

scholarly journals cROStalk for Life: Uncovering ROS Signaling in Plants and Animal Systems, from Gametogenesis to Early Embryonic Development

Genes ◽  
2021 ◽  
Vol 12 (4) ◽  
pp. 525
Author(s):  
Valentina Lodde ◽  
Piero Morandini ◽  
Alex Costa ◽  
Irene Murgia ◽  
Ignacio Ezquer
Keyword(s):  
Signal Transduction ◽  
Signaling Pathways ◽  
Analytical Techniques ◽  
Antioxidant Systems ◽  
Developmental Studies ◽  
Science Field ◽  
Ros Signaling ◽  
Reproductive Processes

This review explores the role of reactive oxygen species (ROS)/Ca2+ in communication within reproductive structures in plants and animals. Many concepts have been described during the last years regarding how biosynthesis, generation products, antioxidant systems, and signal transduction involve ROS signaling, as well as its possible link with developmental processes and response to biotic and abiotic stresses. In this review, we first addressed classic key concepts in ROS and Ca2+ signaling in plants, both at the subcellular, cellular, and organ level. In the plant science field, during the last decades, new techniques have facilitated the in vivo monitoring of ROS signaling cascades. We will describe these powerful techniques in plants and compare them to those existing in animals. Development of new analytical techniques will facilitate the understanding of ROS signaling and their signal transduction pathways in plants and mammals. Many among those signaling pathways already have been studied in animals; therefore, a specific effort should be made to integrate this knowledge into plant biology. We here discuss examples of how changes in the ROS and Ca2+ signaling pathways can affect differentiation processes in plants, focusing specifically on reproductive processes where the ROS and Ca2+ signaling pathways influence the gametophyte functioning, sexual reproduction, and embryo formation in plants and animals. The study field regarding the role of ROS and Ca2+ in signal transduction is evolving continuously, which is why we reviewed the recent literature and propose here the potential targets affecting ROS in reproductive processes. We discuss the opportunities to integrate comparative developmental studies and experimental approaches into studies on the role of ROS/ Ca2+ in both plant and animal developmental biology studies, to further elucidate these crucial signaling pathways.

scholarly journals Critical role of the membrane-proximal, proline-rich motif of the interleukin-2 receptor γc chain in the Jak3-independent signal transduction

1999 ◽  
Vol 4 (6) ◽  
pp. 363-373 ◽  
Author(s):  
Shiho Tsujino ◽  
Tadaaki Miyazaki ◽  
Atsuo Kawahara ◽  
Michiyuki Maeda ◽  
Tadatsugu Taniguchi ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Critical Role ◽  
Interleukin 2 ◽  
Interleukin 2 Receptor

scholarly journals Direct evidence for a key role of protein kinase C in the development of vasospasm after subarachnoid hemorrhage

1992 ◽  
Vol 76 (4) ◽  
pp. 635-639 ◽  
Author(s):  
Shigeru Nishizawa ◽  
Nobukazu Nezu ◽  
Kenichi Uemura
Keyword(s):  
Signal Transduction ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Direct Evidence ◽  
Control Group ◽  
Content Type ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Fine Print

✓ Vascular contraction is induced by the activation of intracellular contractile proteins mediated through signal transduction from the outside to the inside of cells. Protein kinase C plays a crucial role in this signal transduction. It is hypothesized that protein kinase C plays a causative part in the development of vasospasm after subarachnoid hemorrhage (SAH). To verify this directly, the authors measured protein kinase C activity in canine basilar arteries in an SAH model with (γ-32P)adenosine triphosphate and the data were compared to those in a control group. Protein kinase C is translocated to the membrane from the cytosol when it is activated, and the translocation is an index of the activation; thus, protein kinase C activity was measured both in the cytosol and in the membrane fractions. Protein kinase C activity in the membrane in the SAH model was remarkably enhanced compared to that in the control group. The percentage of membrane activity to the total was also significantly greater in the SAH vessels than in the control group, and the percentage of cytosol activity in the SAH group was decreased compared to that in the control arteries. The results indicate that protein kinase C in the vascular smooth muscle was translocated to the membrane from the cytosol and was activated when SAH occurred. It is concluded that this is direct evidence for a key role of protein kinase C in the development of vasospasm.

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