Ompelein tai hakasin suljettu leikkaushaava : kotihoito-ohje potilaalle

TIIVISTELMÄ Nurminen, Anna-Maria & Marjokari, Elisa. Ompelein tai hakasin suljettu leikkaushaava, Kotihoito-ohje potilaalle. Kevät 2014, 44s., 3 liitettä. Diakonia-ammattikorkeakoulu, Hoitotyön koulutusohjelma, Hoitotyön suuntautumisvaihtoehto, Sairaanhoitaja (AMK) / Terveydenhoitotyön suuntautumisvaihtoehto, Terveydenhoitaja (AMK). Opinnäytetyön tarkoituksena oli tehdä kirjallisuuskatsaus ompelein tai hakasin suljetun leikkaushaavan hoidosta, sekä kirjallisuuskatsauksen perusteella laatia aiheesta kotihoito-ohje potilaalle. Tämän opinnäytetyön sisältämä leikkaushaavan kotihoito-ohje on tehty yhteistyössä Suomen Haavanhoitoyhdistyksen kanssa. Potilasohje perustuu kirjallisuushakuun ja sen tuloksiin, joista muokattiin potilasohje suljetun leikkaushaavan hoidosta. Kirjallisuuskatsauksen tekemiseen käytettiin neljää tietokantaa: Medic, Cinahl (full text), Ebsco (full text) ja The Cochrane. Osa hauista suoritettiin lisäksi manuaalisesti kirjastohaulla sekä Googlen avulla. Kirjallisuuskatsauksessa käytettiin yhteensä 15 tutkimusta. Osa käytetyistä tutkimuksista antoi nykyisiin leikkaushaavan hoito-ohjeisiin nähden ristiriitaisen käsityksen leikkaushaavan hoidossa käytettävistä menetelmistä. Esimerkiksi haavan kastelun ja sidosten poiston ensimmäisen 12 tunnin aikana ei todettu vaikuttavan haavainfektioiden määrään, vaikka suurin osa sairaaloista ohjeistaa pitämään haavan kuivana ja ottamaan sidokset pois vasta aikaisintaan 24h leikkauksen jälkeen. Osa tutkimuksista kuitenkin tuki nykyisiä ohjeita. Kotihoito-ohjeen sisältö perustuu kirjallisuuskatsaukseen ja koostuu seuraavista asioista: milloin haavan saa kastella, milloin haavasidokset saa poistaa, miten haavakipua hoidetaan, mitä tarvitsee tietää haavan puhdistamisesta ja käsihygieniasta, mitä vaikutuksia ravitsemuksella ja tupakoinnilla on haavan paranemisen kannalta. Asiasanat: haavat, hoito, leikkaushoito, potilasohjeet, kvalitatiivinen tutkimus, kirjallisuuskatsauksetABSTRACT Nurminen, Anna-Maria and Marjokari, Elisa. A literature review of general practices of suture or staple closed clean surgical wound. Language: Finnish. Helsinki, Spring 2014. 44p., 3 appendices. Diaconia University of Applied Sciences. Degree Programme in Nursing, Option in Nursing. Degree: Nurse / Option in Health care. Degree: Public Health Nurse. Aim of the thesis was to make a review of the literature and develop an integrated patient education handout of assessment and management of surgical wound. This patient education handout is produced together with The Finnish Wound Care Society. This patient education handout is based on literature search and its results. Four different databases were used in this thesis: Medic, Cinahl (full text), Ebsco (full text) and The Cochrane. Also manual search was used by Google and library search. Latest evidence-based research data which affects healing of surgical wound was searched. 15 studies were used in this thesis. Some of the used studies in this literature review were different than the current instructions. For example wound showering and dressing removal in the first 12 hours was not seen to affect the number of wound infections even though the majority of hospitals instruct to keep the wound dry and covered at least 24 hours after surgery. Some of the researches, however, support the current instructions. The evidence suggests that the patient education handout should instruct patients about wound showering, dressing removal, pain management, wound cleansing, hand hygiene, nutrition and the effects of smoking. There is no national evidence-based treatment recommendations about surgical wound care. Key words: surgical wound, wound care, surgical-site infection, wound healing, wound-related pain, dressings

Molecular mechanism of T-cell protein tyrosine phosphatase (TCPTP) activation by mitoxantrone

T-cell protein tyrosine phosphatase (TCPTP) is a ubiquitously expressed non-receptor protein tyrosine phosphatase. It is involved in the negative regulation of many cellular signaling pathways. Thus, activation of TCPTP could have important therapeutic applications in diseases such as cancer and inflammation. We have previously shown that the α-cytoplasmic tail of integrin α1β1 directly binds and activates TCPTP. In addition, we have identified in a large-scale high-throughput screen six small molecules that activate TCPTP. These small molecule activators include mitoxantrone and spermidine. In this study, we have investigated the molecular mechanism behind agonist-induced TCPTP activation. By combining several molecular modeling and biochemical techniques, we demonstrate that α1-peptide and mitoxantrone activate TCPTP via direct binding to the catalytic domain, whereas spermidine does not interact with the catalytic domain of TCPTP in vitro. Furthermore, we have identified a hydrophobic groove surrounded by negatively charged residues on the surface of TCPTP as a putative binding site for the α1-peptide and mitoxantrone. Importantly, these data have allowed us to identify a new molecule that binds to TCPTP, but interestingly cannot activate its phosphatase activity. Accordingly, we describe here mechanism of TCPTP activation by mitoxantrone, the cytoplasmic tail of α1-integrin, and a mitoxantrone-like molecule at the atomic level. These data provide invaluable insight into the development of novel TCPTP activators, and may facilitate the rational discovery of small-molecule cancer therapeutics

Cystic Fibrosis Transmembrane Conductance Regulator Interacts with Multiple Immunoglobulin Domains of Filamin A*

Mutations of the chloride channel cystic fibrosis transmembrane conductance regulator (CFTR) that impair its apical localization and function cause cystic fibrosis. A previous report has shown that filamin A (FLNa), an actin-cross-linking and -scaffolding protein, interacts directly with the cytoplasmic N terminus of CFTR and that this interaction is necessary for stability and confinement of the channel to apical membranes. Here, we report that the CFTR N terminus has sequence similarity to known FLNa-binding partner-binding sites. FLNa has 24 Ig (IgFLNa) repeats, and a CFTR peptide pulled down repeats 9, 12, 17, 19, 21, and 23, which share sequence similarity yet differ from the other FLNa Ig domains. Using known structures of IgFLNa·partner complexes as templates, we generated in silico models of IgFLNa·CFTR peptide complexes. Point and deletion mutants of IgFLNa and CFTR informed by the models, including disease-causing mutations L15P and W19C, disrupted the binding interaction. The model predicted that a P5L CFTR mutation should not affect binding, but a synthetic P5L mutant peptide had reduced solubility, suggesting a different disease-causing mechanism. Taken together with the fact that FLNa dimers are elongated (∼160 nm) strands, whereas CFTR is compact (6∼8 nm), we propose that a single FLNa molecule can scaffold multiple CFTR partners. Unlike previously defined dimeric FLNa·partner complexes, the FLNa-monomeric CFTR interaction is relatively weak, presumptively facilitating dynamic clustering of CFTR at cell membranes. Finally, we show that deletion of all CFTR interacting domains from FLNa suppresses the surface expression of CFTR on baby hamster kidney cells