{"title":"Effect of tumour promoting agents on protein phosphorylation in human placenta","authors":"D. Bischof, K.D. Hammond","doi":"10.1016/0020-711X(94)90086-8","DOIUrl":"10.1016/0020-711X(94)90086-8","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The effects of okadaic acid (OA) and phorbol-12-myristate-13-acetate (PMA) on protein phosphorylation were studied in human term placentas.</p></span></li><li><span>2.</span><span><p>2. When samples treated with tumour promoters were compared with untreated samples, the phosphorylation of a 135 kDa protein was significantly decreased; OA also produced a decrease in phosphorylation of a 24 kDa protein.</p></span></li><li><span>3.</span><span><p>3. Both substances produced an alteration in the proportions of bands of masses 170, 65 and 24 kDa, relative to total phosphorylation: PMA treatment also affected the band of mass 135 kDa.</p></span></li><li><span>4.</span><span><p>4. Placental cell extracts were also subjected to Western blotting with a protein kinase C (PKC) antibody, reportedly specific for the α- and β-isoforms.</p></span></li><li><span>5.</span><span><p>5. Two immunoreactive proteins were detected; an 80 kDa band, presumably corresponding to the α- or β-PK.C, and a 64 kDa protein, which could be a degradation production of the 80 kDa protein or it could correspond to another form of the enzyme. The expression of PKC did not change on treatment with PMA.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 7","pages":"Pages 923-931"},"PeriodicalIF":0.0,"publicationDate":"1994-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90086-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19056682","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Juhani Jänne, Juha-Matti Hyttinen, Teija Peura, Minna Tolvanen, Leena Alhonen, Rlitta Sinervirta, Maria Halmekytö
{"title":"Transgenic bioreactors","authors":"Juhani Jänne, Juha-Matti Hyttinen, Teija Peura, Minna Tolvanen, Leena Alhonen, Rlitta Sinervirta, Maria Halmekytö","doi":"10.1016/0020-711X(94)90078-7","DOIUrl":"10.1016/0020-711X(94)90078-7","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Although many human therapeutic proteins are currently produced in microbial fermentors using recombinant DNA techniques, it is obvious that microbial processing is not suitable for a large number of bioactive proteins owing to the inability of bacteria to carry out postsynthetic modification reactions required for full biological activity.</p></span></li><li><span>2.</span><span><p>2. This disadvantage does not apply to animal cell bioreactors that can generate biologically fully active entities, yet the use of large-scale animal cell cultures for production purposes is prohibitively expensive.</p></span></li><li><span>3.</span><span><p>3. With the advent of transgenic technology, the production of valuable human pharmaceuticals in large farm animals (pig, sheep, goat and dairy cattle) has become more and more attractive as a high-quantity, low-cost alternative. By employing targeted gene transfer, e.g. using mammary gland-specific regulatory sequences fused with the desired production genes, it is possible to govern the expression to occur exclusively in the mammary gland and hence the gene product is being ultimately secreted into the milk.</p></span></li><li><span>4.</span><span><p>4. While reviewing the remarkable progress in this field that has even led to commercial exploitations, we will outline in somewhat greater detail our strategy for the use of dairy cattle as a bioreactor for valuable proteins of pharmaceutical interest.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 7","pages":"Pages 859-870"},"PeriodicalIF":0.0,"publicationDate":"1994-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90078-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19056676","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Cysteine protease activity in arils of Thaumatococcus daniellii: Relationship between the sweet protein thaumatin and cysteine protease activity","authors":"Andrew G. Stephen , Roy Powls , Robert J. Beynon","doi":"10.1016/0020-711X(94)90080-9","DOIUrl":"https://doi.org/10.1016/0020-711X(94)90080-9","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The intensely sweet protein thaumatin was originally reported to possess autolytic activity, manifest only in the presence of reducing agents. We have shown that the proteolytic activity in partially purified thaumatin preparations is attributable to a cysteine proteinase, thaumatopain, that can be separated from thaumatin by cation exchange chromatography.</p></span></li><li><span>2.</span><span><p>2. Lesser peaks of proteolytic activity coeluted with thaumatin variants, which did not completely exclude the possibility of a weak but inherent proteolytic activity in the thaumatins.</p></span></li><li><span>3.</span><span><p>3. The minor proteolytic peaks were resolved from thaumatins by hydrophobic interaction chromalography, and are probably due to minor charge variants of the thaumatopains. Thaumatin has no intrinsic proteolytic activity.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 7","pages":"Pages 879-884"},"PeriodicalIF":0.0,"publicationDate":"1994-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90080-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72220694","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Oded Zamir , William O'Brien , Robert Thompson , Duane C. Bloedow , Josef E. Fischer , Per-Olof Hasselgren
{"title":"Reduced muscle protein breakdown in septic rats following treatment with interleukin-1 receptor antagonist","authors":"Oded Zamir , William O'Brien , Robert Thompson , Duane C. Bloedow , Josef E. Fischer , Per-Olof Hasselgren","doi":"10.1016/0020-711X(94)90088-4","DOIUrl":"10.1016/0020-711X(94)90088-4","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The role ofinterleukin-1 (IL-1) in sepsis-induced muscle proteolysis was assessed by treating septic rats with recombinant IL-1 receptor antagonist (rIL-Ira).</p></span></li><li><span>2.</span><span><p>2. In initial experiments, we tested the effectiveness of IL-Ira in preventing muscle proteolysis induced by administration of IL-1.</p></span></li><li><span>3.</span><span><p>3. When normal rats were treated with rIL-α (three intraperitoneal doses of 100 μ g/kg body weight each over 16 hr), total and myofibrillar muscle protein breakdown rates, measured as release oftyrosine and 3-methylhistidine, respectively, by incubated extensor digitorum longus muscles, were significantly increased.</p></span></li><li><span>4.</span><span><p>4. This metabolic response to IL-α was completely abolished by rIL-Ira, administered as three intraperitoneal doses of 3 mg/kg body weight each over 16hr.</p></span></li><li><span>5.</span><span><p>5. In subsequent experiments, sepsis was induced in rats by cecal ligation and puncture (CLP); non-septic rats were sham-operated.</p></span></li><li><span>6.</span><span><p>6. Treatment of septic rats over 16hr with a total dose of 25mg/kg body weight of rIL-Ira reduced, but did not normalize, the increased muscle protein breakdown rates seen during sepsis.</p></span></li><li><span>7.</span><span><p>7. When the dose of rIL-Ira was more than doubled and given as a constant infusion at a rate of 4.2 mg/kg body weight/hr for 16 hr, the increased rate of muscle proteolysis in septic rats was normalized.</p></span></li><li><span>8.</span><span><p>8. The present study offers the first direct evidence that IL-1 is involved in the regulation of muscle proteolysis during sepsis.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 7","pages":"Pages 943-950"},"PeriodicalIF":0.0,"publicationDate":"1994-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90088-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19056587","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The possibility that Ca2+-ATPase from the plasma membrane-rich fraction of bovine parotid gland is ecto-Ca2+-dependent nucleoside triphosphatase","authors":"Junko Sato, Ritsuko Matsukawa , Hisashi Takiguchi","doi":"10.1016/0020-711X(94)90084-1","DOIUrl":"10.1016/0020-711X(94)90084-1","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Parotid plasma membrane nonpump low-affinity Ca<sup>2+</sup>-ATPase, which possesses high-affinity (Ca<sup>2+</sup> + Mg<sup>2+</sup> )-ATPase activity, was characterized.</p></span></li><li><span>2.</span><span><p>2. Purified Ca<sup>2+</sup>-ATPase hydrolyzed the nucleoside triphosphates, GTP, ITP, CTP, UTP, TTP (67–93% of ATP) and nucleoside diphosphates, ADP. GDP, IDP, CDP, TDP (12–40% of ATP) but not AMP and <em>p</em>-NPP.</p></span></li><li><span>3.</span><span><p>3. The maximum activities of Ca<sup>2+</sup>- and (Ca<sup>2+</sup> +Mg<sup>2+</sup> )-ATPases were obtained in the presence of 1 mM and 0.13 μ M Ca<sup>2+</sup>, respectively.</p></span></li><li><span>4.</span><span><p>4. The <em>K</em><sub><em>m</em></sub> values for Ca<sup>2+</sup> in Ca<sup>2+</sup>- and (Ca<sup>2+</sup>+ Mg<sup>2+</sup> )-ATPases were 0.2 mM and 22 nM. respectively.</p></span></li><li><span>5.</span><span><p>5. The activities of both Ca<sup>2+</sup>- and (Ca<sup>2+</sup> + Mg<sup>2+</sup> )-ATPases were found in the right-side-out-vesicles obtained from the plasma membrane-rich fraction.</p></span></li><li><span>6.</span><span><p>6. These features suggest that Ca<sup>2+</sup>-ATPase is an ecto-Ca<sup>2+</sup>-dependent nucleoside triphosphatase.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 7","pages":"Pages 905-911"},"PeriodicalIF":0.0,"publicationDate":"1994-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90084-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19056681","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Changes in oxidative capacity and fatigue resistance in skeletal muscle","authors":"H. Degens, J.H. Veerkamp","doi":"10.1016/0020-711X(94)90079-5","DOIUrl":"10.1016/0020-711X(94)90079-5","url":null,"abstract":"","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 7","pages":"Pages 871-878"},"PeriodicalIF":0.0,"publicationDate":"1994-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90079-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19056677","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The anti-proliferative action of transforming growth factor-β1 on a rat intestinal epithelial cell line (rie-1) is dependent on cell population density and culture passage number","authors":"Roger D. Smith","doi":"10.1016/0020-711X(94)90083-3","DOIUrl":"10.1016/0020-711X(94)90083-3","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The proliferation of RIE-1 rat intestinal epithelial cells was potently but reversibly inhibited by transforming growth factor-β<sub>1</sub> (TGF-β<sub>1</sub>). In early-passage cultures, complete growth arrest was observed when sparse cultures were treated with TGF-β<sub>1</sub> (1 ng/ml).</p></span></li><li><span>2.</span><span><p>2. However, increasing the initial cell culture density resulted in decreased TGF-β<sub>1</sub>-mediated inhibition of cell proliferation.</p></span></li><li><span>3.</span><span><p>3. Independent of this population density effect, RIE-1 cells also exhibit a marked phenotypic transition around passage-8 to -10, such that later-passage cells were less responsive to growth inhibition by TGF-β<sub>1</sub>].</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 7","pages":"Pages 899-903"},"PeriodicalIF":0.0,"publicationDate":"1994-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90083-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19056680","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
S. Blachowski , T. Motyl , Katarzyna Grzelkowska , Maria Kasterka , A. Orzechowski , Boźena Interewicz
{"title":"Involvement of polyamines in epidermal growth factor (EGF), transforming growth factor (TGF)-α and -β1 action on culture of L6 and fetal bovine myoblasts","authors":"S. Blachowski , T. Motyl , Katarzyna Grzelkowska , Maria Kasterka , A. Orzechowski , Boźena Interewicz","doi":"10.1016/0020-711X(94)90082-5","DOIUrl":"https://doi.org/10.1016/0020-711X(94)90082-5","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. α-Difluoromethylornithine, an irreversible inhibitor of ornithine decarboxylase significantly abolished stimulation of protein synthesis evoked by EGF, TGF-α or -β 1 in L6 and fetal bovine myoblasts.</p></span></li><li><span>2.</span><span><p>2. The participation of polyamines in early events evoked by growth factors was shown by a significant stimulation of ornithine decarboxylase and <em>S</em>denosylmethionine decarboxylase activity as well as increased concentration of spermidine and spermine in L6 cells exposed to TGF-α and EGF.</p></span></li><li><span>3.</span><span><p>3. TGF-β 1 at a high concentration (1 ng/ml) increased protein synthesis in L6 myoblasts but inhibited it in fetal bovine myoblasts. Metabolic effects of TGF-β 1 in L6 cells was associated with an enhancement of decarboxylase activities, however there were no significant changes in cellular polyamine concentrations. Presented data suggest that polyamines are involved in the signal transduction pathway of EGF, TGF-α, and -β 1 in L6 and fetal bovine myoblasts.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 7","pages":"Pages 891-897"},"PeriodicalIF":0.0,"publicationDate":"1994-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90082-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72220693","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
F. Panara, A. Angiolillo, I. Di Rosa, A. Fagotti, S. Contenti, F. Simoncelli, S. Lorvik, R. Pascolini
{"title":"Purification and some properties of a Mg2+-activated acid phosphatase from rat testis","authors":"F. Panara, A. Angiolillo, I. Di Rosa, A. Fagotti, S. Contenti, F. Simoncelli, S. Lorvik, R. Pascolini","doi":"10.1016/0020-711X(94)90081-7","DOIUrl":"10.1016/0020-711X(94)90081-7","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The acid phosphatase (AcPase, EC 3.1.3.2) IV from rat testicular tissue was purified to apparent homogeneity.</p></span></li><li><span>2.</span><span><p>2. The enzyme displays a native molecular weight of 70 kDa determined on gel permeation chromatography on a Sephadex G-100 column and 68 kDa using linear 5–20% sucrose density gradient centrifugation. The subunit molecular weight on SDS-PAGE analysis is 67 kDa, suggesting that the enzyme is a monomeric protein.</p></span></li><li><span>3.</span><span><p>3. The enzyme does not bind to Concanavaline A-Sepharose 4B column, indicating that it is not a glycoprotein.</p></span></li><li><span>4.</span><span><p>4. The rat testis AcPase IV is a metal activated enzyme in which Mg<sup>2+</sup> is the metal activating agent with a <em>K</em><sub>a</sub>, = 0.88 × 10<sup>−3</sup> M. The Michaelis constant for <em>p</em>-nitrophenylphosphate, in the presence of saturating concentrations of Mg<sup>2+</sup> ions, is 0.23 × 10<sup>−3</sup> M.</p></span></li><li><span>5.</span><span><p>5. The enzyme preferentially hydrolizes <em>p</em>-nitrophenylphosphate, phenylphosphate and ATP.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 7","pages":"Pages 885-890"},"PeriodicalIF":0.0,"publicationDate":"1994-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90081-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19056678","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The interaction of human serum albumin in the native and fully reduced states with apolipoprotein E, serum amiloid protein and very low density lipoproteins from human plasma","authors":"Alexander D. Dergunov, Yliya Y. Vorotnikova","doi":"10.1016/0020-711X(94)90087-6","DOIUrl":"10.1016/0020-711X(94)90087-6","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Complex formation in a solution of apolipoprotein E (apoE) isolated from human plasma very low density lipoproteins (VLDL) and human serum albumin (HSA) in both native and fully reduced states was studied. The existence of a kinetically unstable complex of apoE and native albumin was shown. The complex became more stable with the reduction of the S—S links in the albumin molecules capable of forming aggregates under these conditions.</p></span></li><li><span>2.</span><span><p>2. The interaction between native HSA as opposed to a fully reduced one and isolated VLDL particles was more pronounced, probably, due to the existence of amphipathic alpha-helical regions.</p></span></li><li><span>3.</span><span><p>3. Dissociation of the serum amyloid protein (SAP) oligomeric form in solution and the interaction of the protein with fully reduced HSA owing to the provision with the additional hydrophobic surface was shown. ApoE displaced SAP from the complex with fully reduced albumin.</p></span></li><li><span>4.</span><span><p>4. It is suggested that the ability of the apolipoprotein to interact with albumin is determined by internal stability of the molecular structure of the latter and the complexes detected <em>in vitro</em> may be a new transport form of apolipoproteins in lipid-free form in serum. It is assumed that competitive interactions in the HSA-SAP-apoE system may be involved in the development of secondary amyloidosis.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 7","pages":"Pages 933-942"},"PeriodicalIF":0.0,"publicationDate":"1994-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90087-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19056586","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}