Laatusuositukset ympäristöhallinnon vedenlaaturekistereihin vietävälle tiedolle: vesistä tehtävien analyyttien määritysrajat, mittausepävarmuudet sekä säilytysajat ja -tavat

Ohjeesta on julkaistu päivitetty painos (2., uudistettu painos) toukokuussa 2016 Suomen ympäristökeskuksen raportteja -sarjassa (SYKEra 22/2016) osoitteessa: https://helda.helsinki.fi/handle/10138/163532Suomen ympäristökeskus (SYKE) julkaisee laatusuositukset vedenlaaturekistereihin vietävälle tiedolle edistääkseen ympäristömittausten laatutason ja jäljitettävyyden parantamista. Rekisteritiedon laatuongelmia on havaittu muun muassa seurantojen EU-raportointien yhteydessä. Laatusuosituksilla pyritään edistämään eri toimijoiden rekistereihin tuottaman tiedon vertailukelpoisuutta. Suositusten taustalla ovat säädösten edellyttämät menettelytavat ja käytössä olevat standardimenetelmät. Ohjeessa on suosituksia vesistä tehtävien analyyttien menetelmien akkreditoinnille, määritysrajoille, mittausepävarmuuksille sekä näytteiden säilytysajoille ja -tavoille. Lisäksi on huomioitu sekä seurantatiedon raportoinnin tarpeita että Suomen ympäristön erityispiirteitä, kuten vesien luontaisesti pienet taustapitoisuudet. Suositusten laadintaa varten järjestettiin kysely rekisteriin tietoa tuottaville laboratorioille. Kyselyssä kartoitettiin nykyisiä käytäntöjä määritysrajan, mittausepävarmuuden ja näytteiden säilyttämisen osalta ja pyydettiin kommentteja suositusten luonnoksesta. Muun muassa jätevesistä tehtäville analyyteille ja orgaanisten haitta-aineiden analyyteille toivottiin laatusuosituksia. Jätevesien ominaisuudet ja ainepitoisuudet vaihtelevat suuresti kuormituslähteestä johtuen. Ohjeessa on annettu joitakin jätevesiä koskevia suosituksia, mutta ei yhtä kattavasti kuin luonnonvesille. Orgaanisten haitta-aineiden laatusuosituksia on käsitelty tässä ohjeessa vain yleisellä tasolla. Suositukset julkaistaan vain verkkoversiona ja ne tullaan päivittämään tarvittaessa, koska vesistöjen seurantatarpeet ja -vaatimukset muuttuvat. Lisäksi analytiikka kehittyy koko ajan ja menetelmästandardien päivitys on jatkuvaa

CIP2A expression is increased in prostate cancer

Abstract Background The CIP2A protein is a recently characterized oncoprotein which inhibits protein phosphatase 2A activity. Expression of CIP2A has been detected in several carcinomas, but its expression and significance in prostate cancer has not been examined so far. Methods Expression of the CIP2A protein was studied using immunohistochemistry in prostate cancer (n = 59) and in benign prostatic hyperplasia (n = 20) specimens. The CIP2A staining scores were compared with several clinicopathological parameters. Results Expression of CIP2A was increased in prostate cancer epithelium as compared with the benign hyperplastic epithelium (p Conclusions Expression of the CIP2A protein is increased in prostate cancer specimens and its expression is associated with poorly differentiated and high-risk tumors.</p

Newly discovered KI, WU, and Merkel cell polyomaviruses: No evidence of mother-to-fetus transmission

Peer reviewe

The shed ectodomain of type XIII collagen affects cell behaviour in a matrix-dependent manner.

Transmembrane type XIII collagen resides in adhesive structures of cells and tissues, and has therefore been implicated in cell adhesion and in adhesion-dependent cell functions. This collagen also exists as a soluble protein in the pericellular matrix, as the ectodomain is released from the plasma membrane by proteolytic cleavage. Analysis with various protease inhibitors led to confirmation of the furin family of proprotein convertases as the protease group responsible for the shedding of the ectodomain, cleaving at a site conforming to the consensus sequence for the proprotein convertases at the stem of the ectodomain. Both the trans -Golgi network and the plasma membrane were used as cleavage locations. Mammalian cells employed various intracellular mechanisms to modulate shedding of the ectodomain, all resulting in a similar cleavage event. Cell detachment from the underlying substratum was also found to augment the excision. The released ectodomain rendered the pericellular surroundings less supportive of cell adhesion, migration and proliferation, as seen specifically on a vitronectin substratum. Type XIII collagen ectodomain shedding thus resulted in the formation of a soluble, biologically active molecule, which eventually modulated cell behaviour in a reciprocal and substratum-specific manner. The dual existence of membrane-bound and soluble variants widens our biological understanding of type XIII collagen

Type XIII collagen:characterization of ectodomain shedding and its biological implications in mammalian cells, characterization of type XIII collagen expression in human cancers

Abstract Type XIII collagen is an integral membrane protein in type II orientation. In cells and tissues type XIII collagen has been located in various adhesive structures, like focal adhesions. Due to this, its biological role has been implicated in cell adhesion. This collagen also exists as a soluble protein due to the release of the ectodomain from the plasma membrane. In this thesis, ectodomain shedding, i.e. enzymatic release of the extracellular domain, was studied in detail, focusing on the phenomenon as it occurs in mammalian cells. It was found that the ectodomain is released by members of the mammalian proprotein convertase family, e.g. furin. Shedding was shown to take place at the cell surface, but based on additional observations, this cleavage may also take place intracellularly in the Golgi apparatus. Various intracellular mechanisms, depending on cell type, were found to be involved in the regulation of ectodomain shedding. Apparently, due to the liberation of the ectodomain, the level of type XIII collagen on the plasma membrane is maintained at a relatively even amount. The released ectodomain was shown to retain biological activity. It showed distinct matrix-specificity so that on vitronectin its influence on cell functions was anti-adhesive, anti-migratory, anti-proliferative and non-supportive of cell spreading. It was also demonstrated to affect the fibronectin matrix assembly in a manner that resulted in reduced amounts of the fibrillar fibronectin matrix. A large collection of human epithelial and mesenchymal cancer samples were screened for type XIII collagen mRNA expression and compared to the expression levels of pre-malignant and normal samples. It was discovered that malignant transformation upregulates the expression of type XIII collagen in mesenchymal cancers and particularly in the stroma of epithelial cancers, more so than in cancer epithelia. TGF-β1 was demonstrated as one factor contributing to the stimulation of expression. Based on cell culture experiments in this study, it was also deduced that the upregulated expression of type XIII collagen and the concomitant shedding of the ectodomain can remodel the tumour stroma, making it inauspicious for adhesion-dependent cell functions, particularly in vitronectin-rich milieu

Targeting collagen XVIII improves the efficiency of ErbB inhibitors in breast cancer models

The tumor extracellular matrix (ECM) critically regulates cancer progression and treatment response. Expression of the basement membrane component collagen XVIII (ColXVIII) is induced in solid tumors, but its involvement in tumorigenesis has remained elusive. We show here that ColXVIII was markedly upregulated in human breast cancer (BC) and was closely associated with a poor prognosis in high-grade BCs. We discovered a role for ColXVIII as a modulator of epidermal growth factor receptor tyrosine kinase (ErbB) signaling and show that it forms a complex with ErbB1 and -2 (also known as EGFR and human epidermal growth factor receptor 2 [HER2]) and α6-integrin to promote cancer cell proliferation in a pathway involving its N-terminal portion and the MAPK/ERK1/2 and PI3K/AKT cascades. Studies using Col18a1 mouse models crossed with the mouse mammary tumor virus-polyoma virus middle T antigen (MMTV-PyMT) mammary carcinogenesis model showed that ColXVIII promoted BC growth and metastasis in a tumor cell-autonomous manner. Moreover, the number of mammary cancer stem cells was significantly reduced in the MMTV-PyMT and human cell models upon ColXVIII inhibition. Finally, ablation of ColXVIII substantially improved the efficacy of ErbB-targeting therapies in both preclinical models. In summary, ColXVIII was found to sustain the stemness properties of BC cells and tumor progression and metastasis through ErbB signaling, suggesting that targeting ColXVIII in the tumor milieu may have important therapeutic potential