Tunable transform-limited pulse generation using self-injection locking of an FP laser

Wavelength-tunable, near transform-limited pulses have been generated using a Fabry-Perot laser diode coupled to a fiber loop containing a fiber Fabry-Perot resonator (FFPR) and a polarization controller. The ratio of transmitted to reflected light from the loop can be adjusted using the polarization controller. Single-mode operation of the gain-switched laser is achieved by self-injection locking, which is induced by light reflected from the fiber loop. The resulting output pulse has a time-bandwidth product of 0.4 and is tunable over about 15 nm by varying the tuning voltage of the FFPR

A high-speed optical star network using TDMA and all-optical demultiplexing techniques

The authors demonstrate the use of time-division multiplexing (TDM) to realize a high capacity optical star network. The fundamental element of the demonstration network is a 10 ps, wavelength tunable, low jitter, pulse source. Electrical data is encoded onto three optical pulse trains, and the resultant low duty cycle optical data channels are multiplexed together using 25 ps fiber delay lines. This gives an overall network capacity of 40 Gb/s. A nonlinear optical loop mirror (NOLM) is used to carry out the demultiplexing at the station receiver. The channel to be switched out can be selected by adjusting the phase of the electrical signal used to generate the control pulses for the NOLM. By using external injection into a gain-switched distributed feedback (DFB) laser we are able to obtain very low jitter control pulses of 4-ps duration (RMS jitter <1 ps) after compression of the highly chirped gain switched pulses in a normal dispersive fiber. This enables us to achieve excellent eye openings for the three demultiplexed channels. The difficulty in obtaining complete switching of the signal pulses is presented. This is shown to be due to the deformation of the control pulse in the NOLM (caused by the soliton effect compression). The use of optical time-division multiplexing (OTDM) with all-optical switching devices is shown to be an excellent method to allow us to exploit as efficiently as possible the available fiber bandwidth, and to achieve very high bit-rate optical networks

The two-pore channel TPCN2 mediates NAADP-dependent Ca2+-release from lysosomal stores

Second messenger-induced Ca2+-release from intracellular stores plays a key role in a multitude of physiological processes. In addition to 1,4,5-inositol trisphosphate (IP3), Ca2+, and cyclic ADP ribose (cADPR) that trigger Ca2+-release from the endoplasmatic reticulum (ER), nicotinic acid adenine dinucleotide phosphate (NAADP) has been identified as a cellular metabolite that mediates Ca2+-release from lysosomal stores. While NAADP-induced Ca2+-release has been found in many tissues and cell types, the molecular identity of the channel(s) conferring this release remained elusive so far. Here, we show that TPCN2, a novel member of the two-pore cation channel family, displays the basic properties of native NAADP-dependent Ca2+-release channels. TPCN2 transcripts are widely expressed in the body and encode a lysosomal protein forming homomers. TPCN2 mediates intracellular Ca2+-release after activation with low-nanomolar concentrations of NAADP while it is desensitized by micromolar concentrations of this second messenger and is insensitive to the NAADP analog nicotinamide adenine dinucleotide phosphate (NADP). Furthermore, TPCN2-mediated Ca2+-release is almost completely abolished when the capacity of lysosomes for storing Ca2+ is pharmacologically blocked. By contrast, TPCN2-specific Ca2+-release is unaffected by emptying ER-based Ca2+ stores. In conclusion, these findings indicate that TPCN2 is a major component of the long-sought lysosomal NAADP-dependent Ca2+-release channel

The acid test: the discovery of two-pore channels (TPCs) as NAADP-gated endolysosomal Ca2+ release channels

In this review, we describe the background and implications of our recent discovery that two-pore channels (TPCs) comprise a novel class of calcium release channels gated by the intracellular messenger nicotinic acid adenine dinucleotide phosphate (NAADP). Their localisation to the endolysosomal system highlights a new function for these organelles as targets for NAADP-mediated Ca(2+) mobilisation. In addition, we describe how TPCs may also trigger further Ca(2+) release by coupling to the endoplasmic reticular stores through activation of IP(3) receptors and ryanodine receptors

Calcium mobilization via intracellular ion channels, store organization and mitochondria in smooth muscle

In smooth muscle, Ca2+ release from the internal store into the cytoplasm occurs via inositol trisphosphate (IP3R) and ryanodine receptors (RyR). The internal Ca2+ stores containing IP3R and RyR may be arranged as multiple separate compartments with various IP3R and RyR arrangements, or there may be a single structure containing both receptors. The existence of multiple stores is proposed to explain several physiological responses which include the progression of Ca2+ waves, graded Ca2+ release from the store and various local responses and sensitivities. We suggest that, rather than multiple stores, a single luminally-continuous store exists in which Ca2+ is in free diffusional equilibrium throughout. Regulation of Ca2+ release via IP3R and RyR by the local Ca2+ concentration within the stores explains the apparent existence of multiple stores and physiological processes such as graded Ca2+ release and Ca2+ waves. Close positioning of IP3R on the store with mitochondria or with receptors on the plasma membrane creates ‘IP3 junctions’ to generate local responses on the luminally-continuous store

NAADP mobilizes calcium from acidic organelles through two-pore channels

Ca2+ mobilization from intracellular stores represents an important cell signalling process that is regulated, in mammalian cells, by inositol-1,4,5-trisphosphate (InsP3), cyclic ADP ribose and nicotinic acid adenine dinucleotide phosphate (NAADP). InsP3 and cyclic ADP ribose cause the release of Ca2+ from sarcoplasmic/endoplasmic reticulum stores by the activation of InsP3 and ryanodine receptors (InsP3Rs and RyRs). In contrast, the nature of the intracellular stores targeted by NAADP and the molecular identity of the NAADP receptors remain controversial, although evidence indicates that NAADP mobilizes Ca2+ from lysosome-related acidic compartments. Here we show that two-pore channels (TPCs) comprise a family of NAADP receptors, with human TPC1 (also known as TPCN1) and chicken TPC3 (TPCN3) being expressed on endosomal membranes, and human TPC2 (TPCN2) on lysosomal membranes when expressed in HEK293 cells. Membranes enriched with TPC2 show high affinity NAADP binding, and TPC2 underpins NAADP-induced Ca2+ release from lysosome-related stores that is subsequently amplified by Ca2+-induced Ca2+ release by InsP3Rs. Responses to NAADP were abolished by disrupting the lysosomal proton gradient and by ablating TPC2 expression, but were only attenuated by depleting endoplasmic reticulum Ca2+ stores or by blocking InsP3Rs. Thus, TPCs form NAADP receptors that release Ca2+ from acidic organelles, which can trigger further Ca2+ signals via sarcoplasmic/endoplasmic reticulum. TPCs therefore provide new insights into the regulation and organization of Ca2+ signals in animal cells, and will advance our understanding of the physiological role of NAADP