Kol nidrei, op. 47

Soitinnus: Sello, ork.

Handling of TDM Connections with Cello Media Gateway

UMTS is a 3rd generation telecommunication system, which introduces new network architecture. The change in the network architecture introduces new logical network nodes and changes the role of existing nodes in the network. This architecture changes the current vertically specialized network into a horizontally layered structure. In practice, the layering means that different levels in network hierarchy are separated, and they communicate over well-specified interfaces. The Connectivity Layer, at the bottom of the UMTS network architecture, contains Media Gateways (MGW). The GSM radio access network and UMTS access network are connected to the connectivity network via a MGW. External networks, e.g. ISDN networks, are accessed via other MGWs. The user plane is transported across the connectivity network between/via MGWs. ATM network is used as the backbone in Ericsson’s UMTS core network release 2.0. The main goal of this thesis is to study how the MGW is used to bridge ATM and TDM networks. The Circuit Emulation Service (CES) for ATM is studied, as the conversion from TDM to ATM is made according it. The transportation is made using AAL2 and the issues that it has with voice traffic are studied. The implementation and usage of TDM switching service in MGW are described in detail.

Novel Players in the Integrin Signaling Orchestra: TCPTP and MDGI

Metastases are the major cause of cancer deaths. Tumor cell dissemination from the primary tumor utilizes dysregulated cellular adhesion and upregulated proteolytic degradation of the extracellular matrix for progeny formation in distant organs. Integrins are transmembrane adhesive receptors mediating cellcell and cellmatrix interactions that are crucial for regulating cell migration, invasion, proliferation, and survival. Consequently, increased integrin activity is associated with augmented migration and invasion capacity in several cancer types. Heterodimeric integrins consist of an alpha - and beta-subunit that are held together in a bent conformation when the receptor is inactive, but extension and separation of subdomains is observed during receptor activation. Either inside-out or outside-in activation of receptors is possible through the intracellular molecule binding to an integrin cytoplasmic domain or extracellular ligand association with an integrin ectodomain, respectively. Several regulatory binding partners have been characterized for integrin cytoplasmic beta-domains, but the regulators interacting with the cytoplasmic alpha-domains have remained elusive. In this study, we performed yeast two-hybrid screens to identify novel binding partners for the cytoplasmic integrin alpha-domains. Further examination of two plausible candidates revealed a significant coregulatory role of an integrin alpha-subunit for cellular signaling processes. T-cell protein tyrosine phosphatase (TCPTP) showed a specific interaction with the cytoplasmic tail of integrin alpha1. This association stimulated TCPTP phosphatase activity, leading to negative regulation of epidermal growth factor receptor (EGFR) signaling and diminished anchorage-independent growth. Another candidate, mammary-derived growth inhibitor (MDGI), exhibited binding to several different integrin cytoplasmic alpha-tails through a conserved GFFKR sequence. MDGI overexpression in breast cancer cells altered EGFR trafficking and caused a remarkable accumulation of EGFR in the cytoplasm. We further demonstrated in vivo that MDGI expression induced a novel form of anti-EGFR therapy resistance. Moreover, MDGI binding to α-tails retained integrin in an inactive conformation attenuating integrin-mediated adhesion, migration, and invasion. In agreement with these results, sustained MDGI expression in breast cancer patients correlated with an increased 10-year distant disease-free survival. Taken together, the integrin signaling network is far from a complete view and future work will doubtless broaden our understanding further.