A frequency-domain receiver for asynchronous systems employing CP-assisted DS-CDMA schemes

In this paper we consider the uplink transmission within CP-assisted (Cyclic Pre¯x) DS-CDMA (Direct Sequence Code Division Multiple Access) systems and we present a frequency-domain MUD (MultiUser Detection) receiver with iterative estimation and compensation of residual frequency errors. The proposed receiver is suitable for broadband wireless systems, with performances that can be close to the single-user MFB (Matched Filter Bound), even for fully loaded systems and/or in the presence of strong interfering signals. The receiver is powerful enough for typical asynchronous scenarios, requiring only a coarse synchronization between users.

Frequency- domain multiuser detection for highly overloaded DS-CDMA systems

A DS-CDMA (Direct Sequence-Coded Division Multiple Access) system has maximum spectral efficiency if the system is fully loaded (i.e., the number of users is equal to the spreading factor) and we employ signals with bandwidth equal to the chip rate. However, due to implementation constraints we need to employ signals with higher bandwidth, decreasing the system’s spectral efficiency. In this paper we consider prefixassisted DS-CDMA systems with bandwidth that can be significantly above the chip rate. To allow high spectral efficiency we consider highly overloaded systems where the number of users can be twice the spreading factor or even more. To cope with the strong interference levels we present an iterative frequencydomain receiver that takes full advantage of the total bandwidth of the transmitted signals. Our performance results show that the proposed receiver can have excellent performance, even for highly overloaded systems. Moreover, the overall system performance can be close to the maximum theoretical spectral efficiency, even with transmitted signals that have bandwidth significantly above the chip rate.

Ligand binding and signalling pathways of PTH receptors in sea bream (Sparus auratus) enterocytes

Whole animal studies have indicated that Ca2+ uptake by the gastrointestinal tract is regulated by the action of parathyroid hormone-related peptide (PTHrP) in teleost fish. We have characterised PTH receptors (PTHR) in piscine enterocytes and established, by using aminoterminal PTHrP peptides, the amino acid residues important for receptor activation and for stabilising the ligand/receptor complex. Ligand binding of 125I-(1–35tyr) PTHrP to the membrane fraction of isolated sea bream enterocytes revealed the existence of a single saturable high-affinity receptor (KD=2.59 nM; Bmax=71 fmol/mg protein). Reverse transcription/polymerase chain reaction with specific primers for sea bream PTH1R and PTH3R confirmed the mRNA expression of only the later receptor. Fugu (1–34) PTHrP increased cAMP levels in enterocytes but had no effect on total inositol phosphate accumulation. The aminoterminal peptides (2–34)PTHrP, (3–34)PTHrP and (7–34) PTHrP bound efficiently to the receptor but were severely defective in stimulating cAMP in enterocyte cells indicating that the first six residues of piscine (1–34)PTHrP, although not important for receptor binding, are essential for activation of the adenylate cyclase/phosphokinase A (AC-PKA)-receptor-coupled intracellular signalling pathway. Therefore, PTHrP in teleosts acts on the gastrointestinal tract through PTH3R and the AC-PKA intracellular signalling pathway and might regulate Ca2+ uptake at this site. Ligand-receptor binding and activity throughout the vertebrates appears to be allocated to the same amino acid residues of the amino-terminal domain of the PTHrP molecule.