Faktor-Faktor yang Berhubungan dengan Kejadian Wound Dehiscence pada Pasien Post Laparatomi

Wound dehiscence sering terjadi setelah pembedahan mayor abdomen menimbulkan tingkat morbiditas dan mortalitas yang tinggi. Wound dehiscence dapat menimbulkan stress, eviserasi, reoperasi, gangguan citra tubuh, meningkatnya lama rawat dan biaya rawat, menurunkan kualitas hidup pasien serta kematian sehingga perlu menangani faktor yang mempengaruhi kejadian wound dehiscence. Tujuan dari penelitian ini adalah untuk menganalisis faktor-faktor yang berhubungan dengan kejadian wound dehiscence pada pasien dewasa post laparatomi di RSUP Dr Hasan Sadikin Bandung. Metode penelitian menggunakan analitik korelasi dengan pendekatan cross sectional. Sampel yang digunakan berjumlah 40 orang yang diambil dengan menggunakan consecutive sampling. Pengumpulan data dengan cara wawancara, observasi dan studi dokumentasi. Analisis univariat menggunakan distribusi frekuensi dan analisis bivariat menggunakan uji Chi Square. Hasil penelitian menunjukkan kejadian wound dehiscence terjadi ketika perawatan di rumah (35%). Hasil analisis bivariat menunjukkan adanya hubungan yang signifikan antara infeksi luka (p=0,0001), operasi emergensi (p = 0,020), hipoalbumin (p=0,037), anemia (p = 0,028), status nutrisi (0,010), dan adanya penyakit penyerta (p = 0,008) dengan kejadian wound dehiscence, serta tidak ada hubungan yang signifikan antara faktor usia (p = 0,581) dan jenis kelamin (p= 0,604) dengan kejadian wound dehiscence. Penting bagi perawat untuk mengidentifikasi potensial faktor risiko wound dehiscence pada pasien yang dilakukan operasi laparatomi dan segera melakukan intervensi yang diperlukan untuk mencegah terjadinya komplikasi wound dehiscence, diantaranya dengan melakukan discharge planning terkait perawatan luka dan pentingnya asupan protein yang adekuat supaya bisa dikenali ditahab mana terjadinya wound dehiscence.Kata kunci: Pasien, post laparatomi, wound dehiscence. Factors correlating of Wound Dehiscence in Patients after Laparatomi at Dr Hasan Sadikin General Hospital BandungAbsractWound dehiscence is often occurred after major abdominal surgery which impacts on morbidity and mortality rates and significantly contributes to prolonged hospital stays, implicit and explicit costs, associate with psychosocial stressor on patients, evisceration re-surgical operation, and may affect to quality of life patients. It is therefore necessary to identify factors affecting wound dehiscence. The aims of the study was to analyze factors correlating of post-operative wound dehiscence in adult patients at Dr Hasan Sadikin general hospital. Correlational analytic with cross sectional approach was used in this study. 40 patients were selected to be participated in this study by using consecutive sampling. Observations, interviews and study documents were conducted in data collection process. Univariate and Bivariate analysis with Chi Square were performed to analyze the data. Results of the study identified than wound dehiscence were occurred during patients at home (35%). Result of analysis bivariate showed that there was a significance correlation between wound infection (p=0, 0001), surgical emergency (p = 0,020), hypo albumin (p=0,037), anemia (p = 0,028), nutrition status (0,010), and other illness (p = 0,008) with wound dehiscence. Whereas, there was no correlation significantly between age factor (p = 0,581) and gender (p= 0,604) with wound dehiscence. It is important for nurses to identify potential risk factors of wound dehiscence in patients after post-operative laparotomy and prevent complication of wound dehiscence by doing discharge planning especially in term of wound care and the need of taking protein consumption adequately to avoid wound dehiscence

Defective ribosomal products challenge nuclear function by impairing nuclear condensate dynamics and immobilizing ubiquitin

Nuclear protein aggregation has been linked to genome instability and disease. The main source of aggregation-prone proteins in cells is defective ribosomal products (DRiPs), which are generated by translating ribosomes in the cytoplasm. Here, we report that DRiPs rapidly diffuse into the nucleus and accumulate in nucleoli and PML bodies, two membraneless organelles formed by liquid\u2013liquid phase separation. We show that nucleoli and PML bodies act as dynamic overflow compartments that recruit protein quality control factors and store DRiPs for later clearance. Whereas nucleoli serve as constitutive overflow compartments, PML bodies are stress-inducible overflow compartments for DRiPs. If DRiPs are not properly cleared by chaperones and proteasomes due to proteostasis impairment, nucleoli undergo amyloidogenesis and PML bodies solidify. Solid PML bodies immobilize 20S proteasomes and limit the recycling of free ubiquitin. Ubiquitin depletion, in turn, compromises the formation of DNA repair compartments at fragile chromosomal sites, ultimately threatening cell survival

Small heat-shock protein HSPB3 promotes myogenesis by regulating the lamin B receptor

One of the critical events that regulates muscle cell differentiation is the replacement of the lamin B receptor (LBR)-tether with the lamin A/C (LMNA)-tether to remodel transcription and induce differentiation-specific genes. Here, we report that localization and activity of the LBR-tether are crucially dependent on the muscle-specific chaperone HSPB3 and that depletion of HSPB3 prevents muscle cell differentiation. We further show that HSPB3 binds to LBR in the nucleoplasm and maintains it in a dynamic state, thus promoting the transcription of myogenic genes, including the genes to remodel the extracellular matrix. Remarkably, HSPB3 overexpression alone is sufficient to induce the differentiation of two human muscle cell lines, LHCNM2 cells, and rhabdomyosarcoma cells. We also show that mutant R116P-HSPB3 from a myopathy patient with chromatin alterations and muscle fiber disorganization, forms nuclear aggregates that immobilize LBR. We find that R116P-HSPB3 is unable to induce myoblast differentiation and instead activates the unfolded protein response. We propose that HSPB3 is a specialized chaperone engaged in muscle cell differentiation and that dysfunctional HSPB3 causes neuromuscular disease by deregulating LBR

Effect of Dengue Hemorrhagic Fever Health Education on Knowledge and Attitudes, in Elementary School Children in West Java, Indonesia

Background: Flooding due to Citarum river overflowing is a natural phenomenon that is almost common every year, especially for the area around Citarum Dayeuhkolot. Floods cause various health problems, such as Dengue Haemorogic Fever (DHF). The high incidence of environmental-based infectious diseases in flood-prone villages in Dayeuhkolot is caused by problems in the health determinant factor which is associated with the still low awareness of the community that supports clean and healthy lifestyle behaviors (PHBS). Objective: To determine the effect of DHF prevention education on elementary school students' knowledge and attitudes. Methods: Quasi-experimental research design with pre-test and post-test design. The study was conducted at Bojong Asih Elementary School, Pasawahan Elementary School, Cangkuang Elementary School, and Leuwi Bandung Elementary School in 2017. The samples in this study were all students in grades 4- 6 totaling 323 people. All students were given a questionnaire before the intervention and then given counseling about the prevention of DHF and given a questionnaire again to measure the level of knowledge and attitudes. Data analysis uses descriptive univariate analysis and bivariate t test. The approach method in this research uses the Integrated UKS method.&nbsp

BAG3 and BAG6 differentially affect the dynamics of stress granules by targeting distinct subsets of defective polypeptides released from ribosomes.

Stress granules (SGs) are dynamic ribonucleoprotein granules induced by environmental stresses. They play an important role in the stress response by integrating mRNA stability, translation, and signaling pathways. Recent work has connected SG dysfunction to neurodegenerative diseases. In these diseases, SG dynamics are impaired because of mutations in SG proteins or protein quality control factors. Impaired SG dynamics and delayed SG dissolution have also been observed for SGs that accumulate misfolding-prone defective ribosomal products (DRiPs). DRiP accumulation inside SGs is controlled by a surveillance system referred to as granulostasis and encompasses the molecular chaperones VCP and the HSPB8-BAG3-HSP70 complex. BAG3 is a member of the BAG family of proteins, which includes five additional members. One of these proteins, BAG6, is functionally related to BAG3 and able to assist degradation of DRiPs. However, whether BAG6 is involved in granulostasis is unknown. We report that BAG6 is not recruited into SGs induced by different types of stress, nor does it affect SG dynamics. BAG6 also does not replace BAG3's function in SG granulostasis. We show that BAG3 and BAG6 target different subsets of DRiPs, and BAG3 binding to DRiPs is mediated by HSPB8 and HSP70. Our data support the idea that SGs are sensitive to BAG3-HSP70-bound DRiPs but not to BAG6-bound DRiPs. Additionally, only BAG3 is strongly upregulated in the stress recovery phase, when SGs dissolve. These data exclude a role for BAG6 in granulostasis and point to a more specialized function in the clearance of a specific subset of DRiPs