Energy-Efficient Cooperative Spectrum Sensing Using Machine Learning Algorithm.

Cognitive Radio (CR) is a practical technique for overcoming spectrum inefficiencies by sensing and utilizing spectrum holes over a wide spectrum. In particular, cooperative spectrum sensing (CSS) determines the state of primary users (PUs) by cooperating with multiple secondary users (SUs) distributed around a Cognitive Radio Network (CRN), further overcoming various noise and fading issues in the radio environment. But it's still challenging to balance energy efficiency and good sensing performances in the existing CSS system, especially when the CRN consists of battery-limited sensors. This article investigates the application of machine learning technologies for cooperative spectrum sensing, especially through solving a multi-dimensional optimization that cannot be readily addressed by traditional approaches. Specifically, we develop a neural network, which involves parameters that are integral to the CSS performance, including a device sleeping rate for each sensor and thresholds used in the energy detection method, and a customized loss function based on the energy consumption of the CSS system and multiple penalty terms reflecting the system requirements. Using this formulation, energy consumption is to be minimized with the guarantee of reaching a certain probability of false alarm and detection in the CSS system. With the proposed method, comparison studies under different hard fusion rules ('OR' and 'AND') demonstrate its effectiveness in improving the CSS system performances, as well as its robustness in the face of changing global requirements. This paper also suggests the combination of the traditional and the proposed scheme to circumvent the respective inherent pitfalls of neural networks and the traditional semi-analytic methods.

Assessing the role of the cadherin/catenin complex at the Schwann cell-axon interface and in the initiation of myelination.

Myelination is dependent on complex reciprocal interactions between the Schwann cell (SC) and axon. Recent evidence suggests that the SC-axon interface represents a membrane specialization essential for myelination; however, the manner in which this polarized-apical domain is generated remains a mystery. The cell adhesion molecule N-cadherin is enriched at the SC-axon interface and colocalizes with the polarity protein Par-3. The asymmetric localization is induced on SC-SC and SC-axon contact. Knockdown of N-cadherin in SCs cocultured with DRG neurons disrupts Par-3 localization and delays the initiation of myelination. However, knockdown or overexpression of neuronal N-cadherin does not influence the distribution of Par-3 or myelination, suggesting that homotypic interactions between SC and axonal N-cadherin are not essential for the events surrounding myelination. To further investigate the role of N-cadherin, mice displaying SC-specific gene ablation of N-cadherin were generated and characterized. Surprisingly, myelination is only slightly delayed, and mice are viable without any detectable myelination defects. ß-Catenin, a downstream effector of N-cadherin, colocalizes and coimmunoprecipitates with N-cadherin on the initiation of myelination. To determine whether ß-catenin mediates compensation on N-cadherin deletion, SC-specific gene ablation of ß-catenin was generated and characterized. Consistent with our hypothesis, myelination is more severely delayed than when manipulating N-cadherin alone, but without any defect to the myelin sheath. Together, our results suggest that N-cadherin interacts with ß-catenin in establishing SC polarity and the timely initiation of myelination, but they are nonessential components for the formation and maturation of the myelin sheath.

Anterograde transport and secretion of brain-derived neurotrophic factor along sensory axons promote Schwann cell myelination.

The neurotrophin brain-derived neurotrophic factor (BDNF) inhibits Schwann cell (SC) migration and promotes myelination via the p75 neurotrophin receptor (NTR). Despite these recent findings, the expression, localization, and mechanism of BDNF action has yet to be determined. Here we demonstrate that the sensory neurons of the dorsal root ganglion (DRG) are a major source of BDNF during postnatal development. The expression of BDNF is initially elevated before myelination and decreases dramatically after the onset of myelination. BDNF expression is controlled in part by transcriptional regulation and the increased expression of the truncated TrkB receptor on SCs. To investigate the possible mechanism of BDNF transport and release, multicompartment Campenot chambers were used. DRG neurons transported and secreted endogenous BDNF along the surface of axons in anterograde fashion. In an attempt to enhance myelination by SCs, DRG neurons were transduced with an adenovirus to overexpress BDNF. BDNF was transported and secreted along the axons and enhanced myelination when compared with control cocultures. Together, the events surrounding the expression, localization, and mechanism of BDNF action in DRG neurons may hint at potential therapeutic implications to efficiently promote remyelination.

The quest for remyelination: a new role for neurotrophins and their receptors.

The formation of myelin is dependent on a reciprocal and intimate relationship between neurons and the myelin-forming glia. Recently, the neurotrophin family of growth factors has been shown to regulate the complex cell-cell interactions that control myelination. Neurotrophins and their receptors influence myelin formation via two distinct mechanisms, either by acting on the neurons, changing the axonal signals that control myelination, or by acting directly on the myelin-forming glia. In this review, we will discuss research highlighting the ability of neurotrophins to both promote and inhibit the myelination process. As reflected in the work presented here, these effects are dependent on a delicate balance of which neurotrophins are expressed, and what receptors are activated. Additionally, we examine an emerging model in which the growth factors that promote the early survival and differentiation of particular sets of neurons later play important roles as key regulators in glial development. Characterizing the temporal expression and the cellular targets of neurotrophins, both during development and after injury, represents a pivotal step in developing a greater understanding of the myelination process, contributing to the development of effective treatments for demyelinating conditions. We conclude this review by discussing the potential for neurotrophins as therapeutics in the quest for remyelination.

The polarity protein Par-3 directly interacts with p75NTR to regulate myelination.

Cell polarity is critical in various cellular processes ranging from cell migration to asymmetric cell division and axon and dendrite specification. Similarly, myelination by Schwann cells is polarized, but the mechanisms involved remain unclear. Here, we show that the polarity protein Par-3 localizes asymmetrically in Schwann cells at the axon-glial junction and that disruption of Par-3 localization, by overexpression and knockdown, inhibits myelination. Additionally, we show that Par-3 directly associates and recruits the p75 neurotrophin receptor to the axon-glial junction, forming a complex necessary for myelination. Together, these results point to a critical role in the establishment of cell polarity for myelination.

Caveolin scaffolding region and the membrane binding region of SRC form lateral membrane domains.

Formation of domains by the membrane binding motifs of caveolin and src were studied in large unilamellar vesicles using fluorescence digital imaging microscopy. Caveolin, a major structural protein of caveolae, contains a scaffolding region (residues 82-101) that contributes to the binding of the protein to the plasma membrane. A caveolin peptide (82-101) corresponding to this scaffolding region induced the formation of membrane domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol-4,5-bisphosphate. Cholesterol, another predominant component of caveolae, was also enriched in these domains. Caveolae also contain many different signaling molecules including src family tyrosine kinases. Src proteins bind to the plasma membrane via a N-terminal myristate chain and a cluster of basic residues that can interact electrostatically with negatively charged lipids. A peptide corresponding to the src membrane binding motifs (residues myr-2-19) sequestered acidic lipids into lateral membrane domains. Both the src and the caveolin peptides colocalized together with acidic lipids in the domains. Control experiments show the domains are not the result of vesicle aggregation. Two-photon fluorescence correlation spectroscopy experiments suggest diffusion in the domains was slower, but the domains were dynamic. Protein kinase C phosphorylated src in its N-terminal membrane binding region; however, the caveolin scaffolding peptide inhibited this activity. Consequently, protein-induced membrane domains may affect cell signaling by organizing signal transduction components within the membrane and changing reaction rates.

Steroid hormone signaling between Schwann cells and neurons regulates the rate of myelin synthesis.

Fluorescence digital imaging microscopy was used to develop a method that allows the continuous monitoring and quantitative measurement of a single myelin internode throughout its development. Using this technique, steroid hormones such as progesterone and dexamethasone were shown to reduce the time required for the initiation and to regulate the rate of myelin synthesis. Progesterone was capable of increasing the rate of myelin synthesis in Schwann cell/neuronal co-cultures in a dose-dependent manner. RT-PCR and in situ hydridization studies revealed that the mRNAs for P450scc and 3beta-hydroxysteroid dehydrogenase, the enzymes involved in progesterone biosynthesis, were induced at the onset of myelin synthesis. The progesterone receptor protein translocated into the nucleus of the neurons during myelin synthesis, suggesting that progesterone could also be affecting neuronal gene expression. Changes in gene expression caused by progesterone are being examined to identify additional factors that may control myelin formation.