Penerapan Metode Logika Fuzzy dalam Perhitungan Status Gizi dan Pola Konsumsi Ibu Hamil pada Smartphone Android

Status gizi adalah suatu keadaan yang diakibatkan oleh status keseimbangan antara antara jumlah asupan gizi dan jumlah yang dibutuhkan oleh tubuh untuk berbagai fungsi biologis seperti pertumbuhan fisik, perkembangan, aktivitas, pemeliharan kesehatan, dan lainnya. Agar memudahkan ibu hamil memantau status gizi dan pola konsumsi maka perlu adanya suatu sistem yang dapat memudahkan ibu hamil untuk menggunakan maka sistem dibuat pada smartphone android. Hasil uji program dilakukan selama 20 pengujian untuk status gizi, dimana pengujian tersebut menggunakan metode logika fuzzy, sembilan belas diantaranya sesuai dengan perhitungan rumus Indeks Massa Tubuh dengan nilai validasi = 95%. Hasil uji program dilakukan selama 15 pengujian untuk pola konsumsi, dimana pengujian tersebut menggunakan metode logika fuzzy, 8 diantaranya sesuai dengan perhitungan rumus Angka Kecukupan Gizi Individu dengan nilai validasi = 53%. Sehingga dapat disimpulkan bahwa system dapat digunakan untuk perhitungan status gizi, sedangkan untuk perhitungan pola konsumsi ibu hamil sistem belum layak digunakan

Agonist-induced PIP(2) Hydrolysis Inhibits Cortical Actin Dynamics: Regulation at a Global but not at a Micrometer Scale

Phosphatidylinositol 4, 5-bisphosphate (PIP(2)) at the inner leaflet of the plasma membrane has been proposed to locally regulate the actin cytoskeleton. Indeed, recent studies that use GFP-tagged pleckstrin homology domains (GFP-PH) as fluorescent PIP(2) sensors suggest that this lipid is enriched in membrane microdomains. Here we report that this concept needs revision. Using three distinct fluorescent GFP-tagged pleckstrin homology domains, we show that highly mobile GFP-PH patches colocalize perfectly with various lipophilic membrane dyes and, hence, represent increased lipid content rather than PIP(2)-enriched microdomains. We show that bright patches are caused by submicroscopical folds and ruffles in the membrane that can be directly visualized at ∼15 nm axial resolution with a novel numerically enhanced imaging method. F-actin motility is inhibited significantly by agonist-induced PIP(2) breakdown, and it resumes as soon as PIP(2) levels are back to normal. Thus, our data support a role for PIP(2) in the regulation of cortical actin, but they challenge a model in which spatial differences in PIP(2) regulation of the cytoskeleton exist at a micrometer scale

Clostridium difficile toxin B differentially affects GPCR-stimulated Ca^(2+) responses in macrophages: independent roles for Rho and PLA_2

Clostridium difficile toxins cause acute colitis by disrupting the enterocyte barrier and promoting inflammation. ToxB from C. difficile inactivates Rho family GTPases and causes release of cytokines and eicosanoids by macrophages. We studied the effects of ToxB on GPCR signaling in murine RAW264.7 macrophages and found that ToxB elevated Ca^(2+) responses to Gαi-linked receptors, including the C5aR, but reduced responses to Gαq-linked receptors, including the UDP receptors. Other Rho inhibitors also reduced UDP Ca^(2+) responses, but they did not affect C5a responses, suggesting that ToxB inhibited UDP responses by inhibiting Rho but enhanced C5a responses by other mechanisms. By using PLCβ isoform-deficient BMDM, we found that ToxB inhibited Ca^(2+) signaling through PLCβ4 but enhanced signaling through PLCβ3. Effects of ToxB on GPCR Ca^(2+) responses correlated with GPCR use of PLCβ3 versus PLCβ4. ToxB inhibited UDP Ca^(2+) signaling without reducing InsP3 production or the sensitivity of cellular Ca^(2+) stores to exogenous InsP3, suggesting that ToxB impairs UDP signaling at the level of InsP3/Ca^(2+) coupling. In contrast, ToxB elevated InsP3 production by C5a, and the enhancement of Ca^(2+) signaling by C5a was prevented by inhibition of PLA2 or 5-LOX but not COX, implicating LTs but not prostanoids in the mechanism. In sum, ToxB has opposing, independently regulated effects on Ca^(2+) signaling by different GPCR-linked PLCβ isoforms in macrophages