{"title":"Electron microscopic studies on the macronuclear development in the ciliate Chilodonella uncinata.","authors":"C K Pyne","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The development of macronuclear anlage in the ciliate Chilodonella uncinata has been studied through electron microscopy. The ultrastructure of macro- and micronuclei is described for comparison. During the first stage of development, when the DNA content of the macronuclear anage increases from 2 C to 32 C, chromosomes are visible as distinct osmiophilic bodies inside the anlage. At the end of the initial polyploidization phase, the chromosomes despiralize, giving rise to long filamentous structures 25 to 50 nm in diameter. The latter show a singular banding pattern, with dense bands 12 to 25 nm thick alternating regularly with less dense interbands. Such an organization has not yet been observed in any other type of nucleus. These filamentous structures have been interpreted as highly despiralized oligotenic chromosomes. During the final stage of macronuclear development, these structures condense into thin chromatin strands and small dense granules; the number of granules increases progressively as the chromatin strands disappear. These small granules very likely fuse amongst themselves to form the chromatin granules of the vegetative macronucleus. No evidence has yet been found for a fragmentation of chromatin in this ciliate, but this problem needs further study. The old macronucleus maintains a normal ultrastructure until a late stage of development of the macronuclear anlage, becoming pycnotic only towards the very end of the latter process.</p>","PeriodicalId":75770,"journal":{"name":"Cytobiologie","volume":"18 1","pages":"145-60"},"PeriodicalIF":0.0,"publicationDate":"1978-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11321335","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":"Chromatin activation in peritoneal exudate leukocytes after fusion with L cell cytoplasts.","authors":"A A Kushch, I A Prudowskii, A V Zelenin","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Cells reconstituted from the L cell cytoplasts and nuclei of mouse peritoneal leukocytes (PL) have been obtained by fusion procedures. The dormant nuclei of leukocytes undergo reactivation after fusion with active L cell cytoplasms. The reactivation is manifested by the swelling of nuclei, the increase of 3H-actinomycin D binding to chromatin in situ and the 3H-uridine incorporation in nuclei in vivo and by the appearance of nucleoli. The data obtained indicate that the process of dormant nuclei reactivation does not require the presence of the nucleus of the active cell partner. Moreover, the process of chromatin reactivation is more rapid in reconstituted cells than in PL + L cell heterokaryons. Some other details of PL chromatin activation in reconstituted cells and heterokaryons are discussed.</p>","PeriodicalId":75770,"journal":{"name":"Cytobiologie","volume":"18 1","pages":"59-66"},"PeriodicalIF":0.0,"publicationDate":"1978-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11911581","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":"Large scale perfusion culture of cells growing on surfaces with automatic gas and medium control.","authors":"E Harms, J Wendenburg","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":75770,"journal":{"name":"Cytobiologie","volume":"18 1","pages":"67-75"},"PeriodicalIF":0.0,"publicationDate":"1978-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11252706","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}
T Ueda, K Götz von Olenhusen, K E Wohlfarth-Bottermann
{"title":"Reaction of the contractile apparatus in Physarum to injected Ca++, ATP, ADP and 5'AMP.","authors":"T Ueda, K Götz von Olenhusen, K E Wohlfarth-Bottermann","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>After replacement of endoplasm by artificial media, the ectoplasmic tube of the plasmodial veins survives and contraction automaticity continues. Motive force generation for plasmodial locomotion is widely independent of the presence of endoplasm, i.e. force generation is located within the ectoplasmic tube. The replacement of endoplasm offers the possibility to study the effects of physiologically active substances upon the contraction activity of cytoplasmic actomyosin under in vivo conditions. Using different methods for measuring the force output as indicator of the effects of injected substances, the influences of free Ca++-ions and different nucleotides were studied. The injection of Ca++ buffers revealed that force output of the veins increased with ascending Ca++ concentrations between 2 x 10(-7) and 10(-6) M. Half maximal response was found to lie in the range of 4 x 10(-7) M, the saturation value at 6 x 10(-7) M Ca++. The injection of adenosine nucleotides induced optimal contraction responses at 0.2 mM ATP, 0.5 mM ADP and 2.5 mM 5'AMP, respectively. The contraction response induced by 0.2 mM ATP depends strongly on the concentration of the available Ca++. From a threshold concentration of 2 x 10(-7) M Ca++, force output increased up to 10(-5) M Ca++. In presence of 0.2 mM ATP, the value for half maximal contraction response to Ca++ was 10(-6) M Ca++. It is concluded that 0.2 mM ATP and 2 to 4 x 10(-7) M Ca++, are the conditions, under which the cytoplasmic actomyosin system of Physarum performs its function in vivo. The implication of the results and the possibilites of the new method for further investigations of the contraction physiology of Physarum as a model system for cytoplasmic actomyosin are discussed.</p>","PeriodicalId":75770,"journal":{"name":"Cytobiologie","volume":"18 1","pages":"76-94"},"PeriodicalIF":0.0,"publicationDate":"1978-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11911582","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 occurrence of enzymes involved in phenylpropanoid metabolism in the tapetum fraction of anthers.","authors":"E Herdt, R Sütfeld, R Wiermann","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The contents of another loculus were separated in a pollen and tapetum fraction. The following enzymes involved in phenylpropanoid metabolism were present in the tapetum fraction: shikimate dehydrogenase; phenylalanine ammonialyase; cinnamic acid 4-hydroxylase; SAM (S-adenosylmethionine): caffeate 3-O-methyltransferase; hydroxycinnamate: CoA ligase; \"flavanone synthase\"; chalcone-flavanone isomerase; SAM: 3',4'-dihydroxyflavonoid 3'-O-methyltransferase; O-glucosyltransferase. It is postulated, that these enzymes derived from the tapetum catalyze the different steps of phenylpropanoid metabolism at or in cavities of the exine after their transfer into the loculus.</p>","PeriodicalId":75770,"journal":{"name":"Cytobiologie","volume":"17 2","pages":"433-41"},"PeriodicalIF":0.0,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11890254","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":"Spatio-temporal relationships between protoplasmic streaming and contraction activities in plasmodial veins of Physarum polycephalum.","authors":"N Hülsmann, K E Wohlfarth-Bottermann","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Plasmodial veins of Physarum polycephalum were investigated by combining cinematographical, morphological, and tensiometrical techniques. Translucent and nontranslucent (thicker) strands remaining in their original position on filter paper were analyzed in respect to their radial contraction cycles and the resulting streaming activity of the endoplasm. A new technique for measuring the flow intensity by a microbalance method allowed testing of the influence of radial contraction on actual streaming processes within a strand. Stationary ectoplasm and flowing endoplasm are involved in a mutual transformation process: thereia an exchange of ectoplasm and endoplasm in the form of protoplasmic streamlets crossing the borderline between the endoplasmic stream and the ectoplasmic tube. Radial contraction cycles show the same time periodicity as the endoplasmic shuttle streaming. Relationships between radial contractions, streaming rates of endoplasm and streamlets between ectoplasm and endoplasm were analyzed. The participation of the ectoplasmic walls in motive force generation and their function in control of streaming throughput is discussed.</p>","PeriodicalId":75770,"journal":{"name":"Cytobiologie","volume":"17 2","pages":"317-34"},"PeriodicalIF":0.0,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11890250","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}
T Guillot-Salomon, C Tuquet, M De Lubac, M F Hallais, M Signol
{"title":"[Comparative analysis of ultrastructure and lipid composition of plastids from sun and shade plants (author's transl)].","authors":"T Guillot-Salomon, C Tuquet, M De Lubac, M F Hallais, M Signol","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The ultrastructure and lipid composition of chloroplasts, isolated from various shade and sun plants, were compared. Depending on the origin of the plastid, significant differences were observed in the percentage of appressed thylakoids. Accordingly, plastids could be classified into three different types: Type I chloroplasts, from mesophyll cells of sun plants (barley, corn, spinach, bean), display well-developed grana and intergrana thylakoid membranes. Type II chloroplasts, typical of shade plant (Arum), show giant grana stacks with few interconnecting thylakoids. Type III chloroplasts, from bundle sheath cells of leaves from C4-plants (corn), are characterized by an extensive development of stroma thylakoids with only occasional rudimentary grana. The percentages of appressed membranes are in the ranges of 50 to 60%, 80% and 2% for type I, II and III plastids respectively. Striking differences are observed in the fatty acid composition of phosphatidylglycerol molecules. Trans-delta3-hexadecenoic acid is found only in this phospholipid and amounts to 30 to 40%, 50% and less than 8% of total fatty acids in type I, II and III plastids respectively. The comparison of ultrastructural and biochemical data suggests a strong correlation between the amounts of phosphatidylglycerol molecules containing trans-delta3-hexadecenoic acid and the percentages of appressed membranes (grana stacks) within plastid stroma.</p>","PeriodicalId":75770,"journal":{"name":"Cytobiologie","volume":"17 2","pages":"442-52"},"PeriodicalIF":0.0,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11890255","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":"Cell multiplication following partial enzymatic removal of surface coat.","authors":"E Wyroba","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Treatment of Paramecium aurelia with trypsin or pronase (1 mg per 10(5) cells, at 0 to 4 degrees C) partially removes the surface coat and modifies significantly multiplication of cells. The division rate after 24 hours of cultivation is diminished approximately twice in the case of pronase-treated cells and 1.5 for tyrpsin-digested ciliates as compared with the control. On the second day the division rate increases rapidly and number of cell divisions exceeds the values observed in the control. After 72 hours of cultivation the division rate in both untreated and enzyme-treated cells is almost the same. It is concluded that the observed inhibition of cell fission results from the enzymatic removal of the surface coat--the integrity of this surface coat seems to be necessary in the process of cell division. The influence of environmental factors on the rate of growth is presented.</p>","PeriodicalId":75770,"journal":{"name":"Cytobiologie","volume":"17 2","pages":"412-20"},"PeriodicalIF":0.0,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11890253","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":"Localization of concanavalin A binding sites on the cell membrane of Herpetomonas samuelpessoai: influence of growth conditions.","authors":"J L Sixel, M J Esteves, J Angluster, W De Souza","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Herpetomonas samuelpessoai agglutinates when incubated with concanavalin A (Con A). Agglutination involved binding of Con A to specific receptors as it was inhibited by alpha-methyl-D-mannoside. The pattern and the intensity of the agglutination as well as the localization of Con A-binding sites were influenced by the composition of the growth medium, growth temperature and time of incubation. Con A-binding sites were detected by using the Con A-horseradish peroxidase-diaminobenzidine technique.</p>","PeriodicalId":75770,"journal":{"name":"Cytobiologie","volume":"17 2","pages":"421-32"},"PeriodicalIF":0.0,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11771287","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 intermediate-sized filaments in rat kangaroo PtK2 cells. II. Structure and composition of isolated filaments.","authors":"W W Franke, E Schmid, M Osborn, K Weber","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>When cultured cells of the rat kangaroo cell line PtK2 grown on plastic or glass surfaces are lysed and extracted with combinations of low and high salt buffers and the non-ionic detergent Triton X-100 cytoskeletal preparations are obtained that show an enrichment of 6 to 11 nm thick filaments. The arrays of these filaments have been examined by various light and electron microscopic techniques, including ultrathin sectioning, whole mount transmission electron microscopy, negative staining, and indirect immunofluorescence microscopy. In addition, 6 to 11 nm filaments isolated from these cells with similar extraction procedures and with centrifugation techniques have been examined by electron microscopy. The arrays of these isolated intermediate-sized filaments, their ultrastructure and their specific decoration by certain antibodies present in normal rabbit sera as well as by guinea pig antibodies against purified bovine prekeratin is demonstrated. When preparations enriched in these intermediate-sized filaments are examined by SDS-polyacrylamide gel electrophoresis a corresponding enrichment of three polypeptide bands with apparent molecular weights of about 45 000, 52 000 and 58 000 (the latter component sometimes appears split into two bands) is observed, besides some residual actin and a few high molecular weight bands. The morphology of the isolated filaments, their immunological reaction with antibodies decorating prekeratin-containing structures, and the sizes of their constitutive polypeptides suggest that these filaments are closely related to prekeratin-containing filaments observed in a variety of epithelial cells.</p>","PeriodicalId":75770,"journal":{"name":"Cytobiologie","volume":"17 2","pages":"392-411"},"PeriodicalIF":0.0,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11567557","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}