Luigia Santella

Dr. Luigia Santella

Research Director, Stazione Zoologica Anton Dohrn, Napoli, Italy
orcid

Research Focus & Metrics

Academic Career Length

45Years (1982-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 January 2001 in Critical Reviews in Biochemistry and Molecular Biology
Verified
Journal Article
Closed access
ECErnesto Carafoli
Ernesto Carafoli
Luigia SantellaLuigia Santella
Luigia Santella
DBDonata Branca
Donata Branca
MBMarisa Brini
Marisa Brini
In the course of evolution, Ca2+ has emerged as the most versatile intracellular messenger. Its concentration within cells is controlled by reversible binding to specific classes of proteins that act as Ca2+ sensors to decode its information before passing it on to targets. The decoding operation is based on specific conformational changes in the sensor proteins. Other proteins intrinsic to membranes simply control Ca2+ concentration without processing its message, by transporting it across membrane boundaries. They are located in the plasma membrane and in the membranes of the organelles (the endo(sarco)plasmic reticulum, the mitochondria, the nuclear envelope), which play distinctive roles in the cellular homeostasis of Ca2+. Ca2+ is an ambivalent signaling agent. It carries information to virtually all processes important to cell life (e.g., it couples excitation to contraction, secretion, gene transcription, and controls enzyme activity through protein phosphorylation-dephosphorylation), but also transmits signals that promote the programmed demise of cells. When escaping control, Ca2+ also precipitates toxic cell death.

1 November 1997 in The FASEB Journal
Verified
Journal Article
Closed access
Luigia SantellaLuigia Santella
Luigia Santella
ECErnesto Carafoli
Ernesto Carafoli

1 March 1998 in Biochemical and Biophysical Research Communications
Verified
Journal Article
Closed access
Luigia SantellaLuigia Santella
Luigia Santella

1 May 1991 in Molecular Reproduction and Development
Verified
Journal Article
Closed access
PDF file
BDB. Dale
B. Dale
RGR. Gualtieri
R. Gualtieri
RTR. Talevi
R. Talevi
ETE. Tosti
E. Tosti
Luigia SantellaLuigia Santella
Luigia Santella
KEKay Elder
Kay Elder

1 August 2004 in Trends in Biochemical Sciences
Verified
Journal Article
Closed access
Luigia SantellaLuigia Santella
Luigia Santella
DLDmitri Lim
Dmitri Lim
Francesco MocciaFrancesco Moccia
Francesco Moccia

1 March 2000 in Journal of Biological Chemistry
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Journal Article
Open access
PDF file
Luigia SantellaLuigia Santella
Luigia Santella
KKKeiichiro Kyozuka
Keiichiro Kyozuka
AGArmando A. Genazzani
Armando A. Genazzani
LRLaura De Riso
Laura De Riso
ECErnesto Carafoli
Ernesto Carafoli
An intracellular mechanism activated by nicotinic acid adenine dinucleotide phosphate (NAADP+) contributes to intracellular Ca2+ release alongside inositol 1,4,5-trisphosphate (Ins-P3) and ryanodine receptors. The NAADP+-sensitive mechanism has been shown to be operative in sea urchin eggs, ascidian eggs, and pancreatic acinar cells. Furthermore, most mammalian cell types can synthesize NAADP+, with nicotinic acid and NADP+ as precursors. In this contribution, NAADP+-induced Ca2+ release has been investigated in starfish oocytes. Uncaging of injected NAADP+ induced Ca2+mobilization in both immature oocytes and in oocytes matured by the hormone 1-methyladenine (1-MA). The role of extracellular Ca2+ in NAADP+-induced Ca2+mobilization, which was minor in immature oocytes, was instead essential in mature oocytes. Thus, the NAADP+-sensitive Ca2+ pool, which is known to be distinct from those sensitive to inositol 1,4,5-trisphosphate or cyclic ADPribose, apparently migrated closer to (or became part of) the plasma membrane during the maturation process. Inhibition of both Ins-P3and ryanodine receptors, but not of either alone, substantially inhibited NAADP+-induced Ca2+ mobilization in both immature and mature oocytes. The data also suggest that NAADP+-induced Ca2+ mobilization acted as a trigger for Ca2+ release via Ins-P3 and ryanodine receptors.