Dynamic Scheduling of Contextually Categorised Internet of Things Services in Fog Computing Environment.

Fog computing emerged as a concept that responds to the requirements of upcoming solutions requiring optimizations primarily in the context of the following QoS parameters: latency, throughput, reliability, security, and network traffic reduction. The rapid development of local computing devices and container-based virtualization enabled the application of fog computing within the IoT environment. However, it is necessary to utilize algorithm-based service scheduling that considers the targeted QoS parameters to optimize the service performance and reach the potential of the fog computing concept.

Enzymatic and chemical modifications of lipoprotein(a) selectively alter its lysine-binding functions.

The pathogenicity of lipoprotein(a) [Lp(a)] as a risk factor for cardiovascular disease may depend upon its lysine binding sites (LBS) which impart unique functions to Lp(a) not shared with low density lipoprotein. Biologically relevant modifications of Lp(a) were tested for alterations of LBS activity using two previously described functional assays, a LBS-Lp(a) immunoassay and a lysine-Sepharose bead assay. In the LBS-Lp(a) immunoassay, minimal changes in the LBS activity of Lp(a) were observed after modification with lipoprotein lipase, sphingomyelinase, or phospholipase C.

A quantitative immunoassay for the lysine-binding function of lipoprotein(a). Application to recombinant apo(a) and lipoprotein(a) in plasma.

Apo(a), the unique apoprotein of lipoprotein(a) (Lp[a]), can express lysine-binding sites(s) (LBS). However, the LBS activity of Lp(a) is variable, and this heterogeneity may influence its pathogenetic properties. An LBS-Lp(a) immunoassay has been developed to quantitatively assess the LBS function of Lp(a).

Interaction of Lp(a) with plasminogen binding sites on cells.

Lp(a) competes with plasminogen for binding to cells but it is not known whether this competition is due to the ability of Lp(a) to interact directly with plasminogen receptors. In the present study, we demonstrate that Lp(a) can interact directly with plasminogen binding sites on monocytoid U937 cells and endothelial cells. The interaction of Lp(a) with these sites was time dependent, specific, saturable, divalent ion independent and temperature sensitive, characteristics of plasminogen binding to these sites.