Furthermore, examination of changes in the phosphoproteome of rape seeds during the filling stage identified 70 phosphoproteins and 16 non-redundant phosphoproteins, which were verified by mapping the phosphorylation sites. Analysis of vacuolar and cell membranes of rice bud and root revealed 230 membrane and membrane-associated proteins, 20% of which are phosphorylated. In addition, soybean root hairs contain 1625 unique phosphopeptides, including 1659 nonredundant phosphorylation sites, which originate from 1126 phosphoproteins. A recent study identified multiple components of ABA-responsive protein phosphorylation network by integrating genetics with phosphoproteomics. Furthermore, Wang et al. have shown the role of the SnRK2 protein kinases in the ABA signaling pathway by using quantitative phosphopro teomics. To date, only a few plant species have been annotated with protein phosphorylation data and these do not include the economically important plant, cotton. We previously examined the proteome of cotton leaves in response to NO treatment. To follow-up this research, we performed quantitative time-course measurements of the phosphoproteome of cotton leaves treated with sodium nitroprusside, a NO donor. This is the first study to show that NO exposure in leaf tissue alters the phosphorylation states of multiple proteins found in cotton. This information should accelerate research on NO metabolic regulation and will lay a novel, theoretical foundation for further related studies in cotton. The neurotrophins are classically known for their participation in the Staurosporine development, growth, function, and survival of neurons in both the central and peripheral GSI-IX nervous system. Although abundant in the nervous system, BDNF and Ntrk2 are expressed in other cell types and tissues, and BDNF mRNA is found in the majority of the human body organs. In humans, mature BDNF is sequestered in platelets and released upon their degranulation. As such, BDNF has access to all tissues and organs. Motile cells including activated T cells, B cells, and monocytes have been shown to express BDNF in vitro, as have eosinophils, dendritic cells, and endothelial cells. In mice, the visceral epithelium, and airway epithelium are significant sources of BDNF. As for Ntrk2, a comprehensive analysis of Ntrk2 immunoreactivity was assessed and it was found to be expressed mainly in glandular cells of the salivary gland, small intestine, colon, endocrine pancreas, bone marrow hematopoietic cells, monocytes/macrophages of the lymph nodes and spleen, and in the epidermis. Previous studies have shown 
that neurotrophins in the brain are regulated by neuronal activity, and steroid hormones, and that tissue-specific expression is driven by multiple promoters. While BDNF and Ntrk2 expression has been demonstrated in some reproductive tissues including the ovary, and placenta, their uterine expression under physiological conditions has been questionable. BDNF expression was demonstrated by immunohistochemistry in the mouse, and human uterus and by in situ hybridization in the mouse, and rat uterus. While Ntrk2 could not be detected in the mouse and human uterus, others have been successful. To date only one study has looked for the presence of both ligand and receptor simultaneously, in the murine uterus.