Fackförbund på tvären - en studie över tre fackförbund och det inkomstpolitiska avtalet för åren 1992-1993

Only abstract. Paper copies of master’s theses are listed in the Helka database (http://www.helsinki.fi/helka). Electronic copies of master’s theses are either available as open access or only on thesis terminals in the Helsinki University Library.Vain tiivistelmä. Sidottujen gradujen saatavuuden voit tarkistaa Helka-tietokannasta (http://www.helsinki.fi/helka). Digitaaliset gradut voivat olla luettavissa avoimesti verkossa tai rajoitetusti kirjaston opinnäytekioskeilla.Endast sammandrag. Inbundna avhandlingar kan sökas i Helka-databasen (http://www.helsinki.fi/helka). Elektroniska kopior av avhandlingar finns antingen öppet på nätet eller endast tillgängliga i bibliotekets avhandlingsterminaler.Studien har två syften. För det första att ta reda på varför fackförbund väljer att inte godta det av centralförbunden och regeringen överenskomna inkomstpolitiska avtalet. För det andra att bedöma om denna strategi som kallas friåkning leder till ett för fackförbundet fördelaktigare kollektivavtal. Fackförbunden i denna studie är Elbranschens fackförbund som valde friåkandet för telebranschen, Byggnadsförbundet för husbyggnadsbranschens del och Gummi- och läderarbetarnas förbund i fråga om bildäcks- och gummiindustrin. Det inkomstpolitiska avtal förbunden hade att ta ställning till gällde åren 1992–1993. Studiens referensram har inspirerats av Leif Lewins teorier om den rationella aktören som han presenterat i bland annat Ideologi och strategi. Svensk politik under 100 år. Jag har också presenterat det systemteoretiska perspektivet. De tre friåkarförbunden förenas ideologiskt genom att de alla tre enligt sina stadgar strävar efter att förvandla produktionssystemet till socialistiskt. Men när det gäller de specifika motiveringarna just denna gång skiljer de sig åt. Gummi- och läderarbetarnas fackförbunds syn på löneutvecklingen i sina branscher var den att inga löneglidningar förekommer, alltså var det viktigt att avtala om löneförhöjningarna. Byggnadsförbundet uppgav en förnyelse av förtroendemannaavtalet som orsak till friåkandet och Elbranschens fackförbund ansåg att telebranschen hamnat på efterkälken i avlöningen jämfört med övriga löntagare. År 1991 såg de sin chans att korrigera detta då omsättningen i telebranschen ökat. Samhällsekonomin i övrigt upplevde samtidigt en dramatisk konjunkturnedgång. Lyckades fackförbunden förbättra sina kollektivavtal genom friåkandet? Även här skiljer sig fackförbunden från varandra. Elbranschens fackförbund uppnådde de största framgångarna och det är inget tvivel om att friåkandet lönade sig för förbundet och dess medlemmar. Gummi- och läderarbetarnas förbund lyckades höja vissa tillägg i båda branscherna och inom gummiidustrin gavs huvudförtroendemännen rätt att ägna all arbetstid för förtroendeuppdraget. Byggnadsförbundets resultat är däremot svårare att bedöma. Visserligen nåddes ett nytt förtroendemannaavtal för husbyggnadsbranschen. Men snarast var det väl en avvärjningsseger där facket lyckades förhindra de av arbetsgivarna tänkta försämringarna. Eftersom friåkandet inte medförde några direkta kostnader för fackförbundens medlemmar annat än i telebranschen där övertidsförbud rådde i tio dagar kan man konstatera att det lönade sig att friåka inför avtalen år 1992–1993

Lihasdystrofiaproteiini myotiliinin molekulaariset sidokset ja hajoamiseen liittyvät mekanismit

The striated muscle sarcomere is a force generating and transducing unit as well as an important sensor of extracellular cues and a coordinator of cellular signals. The borders of individual sarcomeres are formed by the Z-disks. The Z-disk component myotilin interacts with Z-disk core structural proteins and with regulators of signaling cascades. Missense mutations in the gene encoding myotilin cause dominantly inherited muscle disorders, myotilinopathies, by an unknown mechanism. In this thesis the functions of myotilin were further characterized to clarify the molecular biological basis and the pathogenetic mechanisms of inherited muscle disorders, mainly caused by mutated myotilin. Myotilin has an important function in the assembly and maintenance of the Z-disks probably through its actin-organizing properties. Our results show that the Ig-domains of myotilin are needed for both binding and bundling actin and define the Ig domains as actin-binding modules. The disease-causing mutations appear not to change the interplay between actin and myotilin. Interactions between Z-disk proteins regulate muscle functions and disruption of these interactions results in muscle disorders. Mutations in Z-disk components myotilin, ZASP/Cypher and FATZ-2 (calsarcin-1/myozenin-2) are associated with myopathies. We showed that proteins from the myotilin and FATZ families interact via a novel and unique type of class III PDZ binding motif with the PDZ domains of ZASP and other Enigma family members and that the interactions can be modulated by phosphorylation. The morphological findings typical of myotilinopathies include Z-disk alterations and aggregation of dense filamentous material. The causes and mechanisms of protein aggregation in myotilinopathy patients are unknown, but impaired degradation might explain in part the abnormal protein accumulation. We showed that myotilin is degraded by the calcium-dependent, non-lysosomal cysteine protease calpain and by the proteasome pathway, and that wild type and mutant myotilin differ in their sensitivity to degradation. These studies identify the first functional difference between mutated and wild type myotilin. Furthermore, if degradation of myotilin is disturbed, it accumulates in cells in a manner resembling that seen in myotilinopathy patients. Based on the results, we propose a model where mutant myotilin escapes proteolytic breakdown and forms protein aggregates, leading to disruption of myofibrils and muscular dystrophy. In conclusion, the main results of this study demonstrate that myotilin is a Z-disk structural protein interacting with several Z-disk components. The turnover of myotilin is regulated by calpain and the ubiquitin proteasome system and mutations in myotilin seem to affect the degradation of myotilin, leading to protein accumulations in cells. These findings are important for understanding myotilin-linked muscle diseases and designing treatments for these disorders.Lihaksen rakennetta ja toimintaa säätelevät useat valkuaisaineet, joiden avulla aktiini- ja myosiinisäikeiden tuottama supistusvoima synkronoidaan ja siirretään tukikudoksiin. Myotiliini on lihaksen rakenneproteiini ja osa lihaksen supistusyksikköä, sarkomeeriä. Myotiliinin perityt pistemutaatiot aikaansaavat luuranko- ja sydänlihaksen häiriöitä, eli myotilinopatioita. Vaikka myotilinopatian perinnöllinen tausta tunnetaan, on vielä selvittämättä, kuinka myotiliinin muutokset johtavat lihasten surkastumiseen. Solutasolla tiedämme, että myotilinopatiapotilailla on vakavia sarkomeerin rakennehäiriöitä, ja että viallisen myotiliinin ilmentäminen lihassoluissa johtaa sarkomeerirakenteen hajoamiseen. Tässä tutkimuksessa selvitettiin myotiliinin toimintamekanismeja. Myotiliinin päätehtävänä lienee aktiinisäikeiden yhteenliittäminen sarkomeerin Z-levyssä. Osoitimme, että myotiliinin immunoglobuliinin (Ig) kaltaisia rakenneyksiköitä eli domeeneja tarvitaan aktiinin säätelyyn. Nämä Ig domeenit ovat yhtenäisiä rakenneosia muiden myotiliiniperheen jäsenten kanssa. Tauteja aiheuttavat geenivirheet eivät kuitenkaan vaikuttane myotiliinin ja aktiinin väliseen vuorovaikutukseen. Lihasmassaa säädellään tarpeen mukaan ja esimerkiksi fyysinen harjoittelu kasvattaa lihaksia. Rasitusvastetta ja siihen liittyvää geenien luentaa säätelevät Z-levyn rakenneproteiinit. Häiriö proteiinien, kuten myotiliinin, vuorovaikutuksissa voi johtaa lihastauteihin. Selvitimme sydän- ja lihastaudeissa mutatoituneiden myotiliinin- ja FATZ-perheen proteiinien vuorovaikutusta Z-levyssä sijaitsevien Enigma proteiiniperheen jäsenten kanssa. Osoitimme, että myotiliini- ja FATZ-perheiden jäsenet sitovat Enigma proteiinien PDZ-domeenia uuden ja ainutlaatuisen luokka III:n PDZ:tä sitovan motiivin avulla. Näitä proteiinien vuorovaikutuksia voidaan säädellä fosforylaation avulla. Vuorovaikutukset ovat osa mekanismia, jolla lihassolun sisäinen viestintä tapahtuu. Myotilinopatioille tyypillisiä lihaksen rakennevirheitä ovat Z-levyn muutokset ja tiheän säiemäisen materiaalin keräytyminen. Kertymien syytä ja mekanismia ei tunneta, mutta yksi syy tähän voisi olla proteiinien puutteellinen hajoaminen. Osoitimme, että kalpaiini-proteaasi pilkkoo myotiliinin lihassoluissa ja että myotiliini hajoaa pienempiin rakenneosiin proteasomireitin välityksellä. Määritimme myös ensimmäisen toiminnallisen eron normaalin ja mutatoituneen myotiliinin välillä, sillä myotilinopatioissa mutatoitunut myotiliini hajoaa huomattavasti normaalia hitaammin. Lisäksi näytimme, että mikäli myotiliinin hajoamista estetään kemikaaleilla, seurauksena on proteiinikertymiä, jotka muistuttavat potilasnäytteissä nähtäviä muutoksia. Näiden tulosten perusteella ehdotamme taudin syntymekanismiksi mallia, jossa mutatoitunut myotiliini ei hajoa normaalisti vaan muodostaa kertymiä, jotka johtavat lihaksen rakenneosien hajoamiseen ja lihastautiin. Tulokset edesauttavat myotiliiniin liittyvien lihassairauksien ymmärtämistä ja lihassairauksien hoitoon tarkoitettujen lääkkeiden kehittämistä

Työntekijöiden altistuminen tukiasemien radiotaajuisille kentille

Matkapuhelinten käytön ja langattoman viestinnän tiedonsiirtotarpeiden kasvu edellyttää samanaikaista tukiasemaverkoston tihentymistä. Tukiasemien antennit pyritään sijoittamaan siten, että ns. suuri yleisö ei pääse antennien lähelle. Työntekijöiden on kuitenkin joissakin työtehtävissä ja -tilanteissa työskenneltävä antennien lähellä, vaikka turvallinen etäisyys antenneista on epäselvä. Tämän tutkimusprojektin tarkoituksena oli tutkia radiotaajuisia sähkömagneettisia kenttiä kolmen eri matkapuhelinverkon tukiasema-antennien läheisyydessä. Tutkitut tukiasemat kuuluivat GSM-, UMTS- tai TETRA-verkkoon

Liprin-alpha 1 modulates cancer cell signaling by transmembrane protein CD82 in adhesive membrane domains linked to cytoskeleton

Background: PPFIA1 is located at the 11q13 region commonly amplified in cancer. The protein liprin-alpha 1 encoded by PPFIA1 contributes to the adhesive and invasive structures of cytoskeletal elements and is located at the invadosomes in cancer cells. However, the precise mechanism of liprin-alpha 1 function in cancer progression has remained elusive. Methods: Invasion regulating activity of liprin-alpha 1 was examined by analyzing the functions of squamous cell carcinoma of head and neck (HNSCC) cell lines in three-dimensional collagen I after RNAi mediated gene knockdown. Transcriptome profiling and Gene Set Enrichment Analysis from HNSCC and breast cancer cells were used to identify expression changes relevant to specific cellular localizations, biological processes and signaling pathways after PPFIA1 knockdown. The significance of the results was assessed by relevant statistical methods (Wald and Benjamini-Hochberg). Localization of proteins associated to liprin-alpha 1 was studied by immunofluorescence in 2D and 3D conditions. The association of PPFIA1 amplification to HNSCC patient survival was explored using The Cancer Genome Atlas data. Results: In this study, we show that liprin-alpha 1 regulates biological processes related to membrane microdomains in breast carcinoma, as well as protein trafficking, cell-cell and cell-substrate contacts in HNSCC cell lines cultured in three-dimensional matrix. Importantly, we show that in all these cancer cells liprin-alpha 1 knockdown leads to the upregulation of transmembrane protein CD82, which is a suppressor of metastasis in several solid tumors. Conclusions: Our results provide novel information regarding the function of liprin-alpha 1 in biological processes essential in cancer progression. The results reveal liprin-alpha 1 as a novel regulator of CD82, linking liprin-alpha 1 to the cancer cell invasion and metastasis pathways.Peer reviewe

Liprin-α1 modulates cancer cell signaling by transmembrane protein CD82 in adhesive membrane domains linked to cytoskeleton

Abstract Background PPFIA1 is located at the 11q13 region commonly amplified in cancer. The protein liprin-α1 encoded by PPF1A1 contributes to the adhesive and invasive structures of cytoskeletal elements and is located at the invadosomes in cancer cells. However, the precise mechanism of liprin-α1 function in cancer progression has remained elusive. Methods Invasion regulating activity of liprin-α1 was examined by analyzing the functions of squamous cell carcinoma of head and neck (HNSCC) cell lines in three-dimensional collagen I after RNAi mediated gene knockdown. Transcriptome profiling and Gene Set Enrichment Analysis from HNSCC and breast cancer cells were used to identify expression changes relevant to specific cellular localizations, biological processes and signaling pathways after PPFIA1 knockdown. The significance of the results was assessed by relevant statistical methods (Wald and Benjamini-Hochberg). Localization of proteins associated to liprin-α1 was studied by immunofluorescence in 2D and 3D conditions. The association of PPFIA1 amplification to HNSCC patient survival was explored using The Cancer Genome Atlas data. Results In this study, we show that liprin-α1 regulates biological processes related to membrane microdomains in breast carcinoma, as well as protein trafficking, cell-cell and cell-substrate contacts in HNSCC cell lines cultured in three-dimensional matrix. Importantly, we show that in all these cancer cells liprin-α1 knockdown leads to the upregulation of transmembrane protein CD82, which is a suppressor of metastasis in several solid tumors. Conclusions Our results provide novel information regarding the function of liprin-α1 in biological processes essential in cancer progression. The results reveal liprin-α1 as a novel regulator of CD82, linking liprin-α1 to the cancer cell invasion and metastasis pathways

Gremlin-1 is a key regulator of the invasive cell phenotype in mesothelioma

Peer reviewe

Loss of ATRX/DAXX expression and alternative lengthening of telomeres in uterine leiomyomas

Background Uterine leiomyomas (ULs) are the most common gynecologic tumors and affect 3 of every 4 women by the age of 50 years. The majority of ULs are classified as conventional tumors, whereas 10% represent various histopathological subtypes with features that mimic malignancy. These subtypes include cellular and mitotically active ULs and ULs with bizarre nuclei. Uterine leiomyosarcoma (ULMS), the malignant counterpart of UL, is an aggressive cancer with poor overall survival. The early diagnosis and preoperative differentiation of ULMS from UL are often challenging because their symptoms and morphology resemble one another. Recent studies have shown frequent loss of alpha-thalassemia/mental retardation syndrome X-linked (ATRX) or death domain-associated protein (DAXX) expression in ULMS, and this is often associated with an alternative lengthening of telomeres (ALT) phenotype. Methods To investigate ATRX and DAXX expression and the presence of ALT in UL subtypes, immunohistochemical and telomere-specific fluorescence in situ hybridization analyses were performed. The study material consisted of 142 formalin-fixed, paraffin-embedded tissue samples representing various UL subtypes and 64 conventional ULs. Results A loss of ATRX or DAXX and/or ALT was detected in 6.3% of the histopathological UL subtype samples (9 of 142). Two patients whose ULs showed either ATRX loss or ALT were later diagnosed with a pulmonary smooth muscle tumor. Pulmonary tumors displayed molecular alterations found in the corresponding uterine tumors, which indicated metastasis to the lungs. All conventional ULs displayed normal ATRX, DAXX, and telomeres. Conclusions These results highlight the differences between conventional and histopathologically atypical ULs and indicate that some UL subtype tumors may harbor long-term malignant potential. Cancer 2018;124:4650-4656. (C) 2018 American Cancer Society.Peer reviewe

Liprin-α1 modulates cancer cell signaling by transmembrane protein CD82 in adhesive membrane domains linked to cytoskeleton

BackgroundPPFIA1 is located at the 11q13 region commonly amplified in cancer. The protein liprin-α1 encoded by PPF1A1 contributes to the adhesive and invasive structures of cytoskeletal elements and is located at the invadosomes in cancer cells. However, the precise mechanism of liprin-α1 function in cancer progression has remained elusive.MethodsInvasion regulating activity of liprin-α1 was examined by analyzing the functions of squamous cell carcinoma of head and neck (HNSCC) cell lines in three-dimensional collagen I after RNAi mediated gene knockdown. Transcriptome profiling and Gene Set Enrichment Analysis from HNSCC and breast cancer cells were used to identify expression changes relevant to specific cellular localizations, biological processes and signaling pathways after PPFIA1knockdown. The significance of the results was assessed by relevant statistical methods (Wald and Benjamini-Hochberg). Localization of proteins associated to liprin-α1 was studied by immunofluorescence in 2D and 3D conditions. The association of PPFIA1 amplification to HNSCC patient survival was explored using The Cancer Genome Atlas data.ResultsIn this study, we show that liprin-α1 regulates biological processes related to membrane microdomains in breast carcinoma, as well as protein trafficking, cell-cell and cell-substrate contacts in HNSCC cell lines cultured in three-dimensional matrix. Importantly, we show that in all these cancer cells liprin-α1 knockdown leads to the upregulation of transmembrane protein CD82, which is a suppressor of metastasis in several solid tumors.ConclusionsOur results provide novel information regarding the function of liprin-α1 in biological processes essential in cancer progression. The results reveal liprin-α1 as a novel regulator of CD82, linking liprin-α1 to the cancer cell invasion and metastasis pathways.</div

Liprin-alpha 1 is a regulator of vimentin intermediate filament network in the cancer cell adhesion machinery

PPFIA1 is located at the 11q13 region, which is one of the most commonly amplified regions in several epithelial cancers including head and neck squamous cell carcinoma and breast carcinoma. Considering the location of PPFIA1 in this amplicon, we examined whether protein encoded by PPFIA1, liprin-alpha 1, possesses oncogenic properties in relevant carcinoma cell lines. Our results indicate that liprin-alpha 1 localizes to different adhesion and cytoskeletal structures to regulate vimentin intermediate filament network, thereby altering the invasion and growth properties of the cancer cells. In non-invasive cells liprin-alpha 1 promotes expansive growth behavior with limited invasive capacity, whereas in invasive cells liprin-alpha 1 has significant impact on mesenchymal cancer cell invasion in three-dimensional collagen. Current results identify liprin-a1 as a novel regulator of the tumor cell intermediate filaments with differential oncogenic properties in actively proliferating or motile cells.Peer reviewe