fasudil Protein protein interaction networks are an

Protein–protein interaction networks are an important ingredient for the system-level understanding of cellular processes. Such networks can be used for filtering and assessing functional genomics data and for providing an instinctive platform for annotating structural, functional and evolutionary properties of proteins (Schwartz et al., 2009). For a full description of a protein's function, knowledge about its specific interaction partners is an important pre-requisite. The concept of protein ‘function’ is somewhat hierarchical (Ashburner et al., 2000, Bairoch and Boeckmann, 1994, Lee et al., 2007, Ouzounis et al., 2003), and at all levels in this hierarchy, interactions among proteins help to describe and narrow down a protein's function. In this research, partners and pathways of P-ATPase enzyme fasudil in insects were determined based on the B. terrestris species in each protein family (Table 7). Surprisingly these two proteins were involved in six similar pathways including: Metabolic pathways, Alanine, aspartate and glutamate metabolism, Aminoacyl-tRNA biosynthesis, Endocytosis, Wnt signaling pathway and Pyrimidine metabolism. These results may lead us to find new understanding about P-ATPase family functions. Since phylogenetic analyses can be the basis of molecular and biochemical analyses of protein families, the protein research was performed on the P-ATPase protein families in insects. In Phylogenetic analysis two groups were identified among insect species so that each family of P-ATPases was separated in a group. Group 1 which consisted of all P-ATPase 13A1 members were divided into 11 subgroups. In this group, all the members of subgroups 13A1-I to 13A1-IV were from Formicidae family while all the members of subgroups 13A1-V to 13A1-VIII were other families of Hymenoptera order. Also all the members of 13A1-VIII were just from Braconidae family. Subgroup 13A1-XI contained different species of Diptera. Groups IX and X consisted of different orders, so that all the Hemipteran species were in subgroup 13A1-IX with one species from Pediculidae. It can show the similarity of the species Pediculus humanus corporis to Hemiptera P-ATPase 13A1 protein. Subgroup 13A1-X consisted of all Lepidopteran insect species with one Coleopteran. Group 2 included all the P-ATPase 13A3 proteins in 7 subgroups. According to the tree subgroup 13A3-VII consisted of all the species of Formicidae, also subgroups 13A3-V and 13A3-VI were Hymenopteran species. Subgroup 13A3 consisted of just Lepidopteran insects but other subgroups of 13A3 had different members of different insect orders. These results suggested that, in insects, P-ATPases are very similar to each other and are almost certainly inherited from a common ancestor. Based on Fagan and Saier (1994) research a common ancestry for all P-ATPases has been recognized. These results and observations in this study suggest that some additional families of P-ATPases with novel specificities are likely to be found. Bioinformatics can play a crucial role in the analysis and interpretation of genomic and proteomic data. It uses methods and technologies from mathematics, statistics, computer sciences, physics, biology, and medicine (Romano et al., 2011). In this research, bioinformatic analyses of P-ATPases in insects exhibited similarities of this protein in different P-ATPase families. So that it was shown by obtained data from six similar pathways and seventeen similar domains between these two protein families. Also these results provide background of bioinformatic studies for the function and evolution of this enzyme in insects.
Aluminum is one of the most abundant elements in the Earth's crust. The relationship between aluminum exposure and neurodegenerative diseases, including dialysis encephalopathy syndrome, amyotrophic lateral sclerosis, Parkinsonism dementia and Alzheimer's disease has been extensively reported []. The oxidation state of aluminum is +3, and its effective ionic radius in sixfold coordination is 0.54 Å. The primary interaction of Al with ligands is electrostatic and has a slow dissociation rate []. In aqueous solution, aluminum is solvated with water molecules. This form is known as free aluminum (Al(HO) (or simply, Al) and is abundant at acidic pH. When the pH rises, aluminum is complexed with OH from deprotonation of water molecules (Al(OH)). Among others, Al binds strongly to ATP and phosphate groups and displaces both Mg and Ca from their enzyme's binding sites []. Hence, changes in the Ca homeostasis and protein phosphorylation/dephosphorylation would explain aluminum cellular toxicity [].