ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Influence of different culture conditions on sarcoplasmic reticular calcium transport in isolated neonatal rat cardiomyocytes (1998)
    Springer
    Molecular and cellular biochemistry 188 (1998), S. 177-185 
    Details
    ISSN: 1573-4919
    Keywords: neonatal rat cardiomyocyte culture ; sarcoplasmic reticulum ; phospholamban ; calcium ATPase ; calcium transport ; thyroid hormone
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract This study investigates sarcoplasmic reticulum (SR) calcium-(Ca2+) transport ATPase (SERCA2a) and phospholamban (PLB) in cultured spontaneously contracting neonatal rat cardiomyocytes (CM) to ascertain the function of both SR proteins under various culture conditions. The two major SR proteins were readily detectable in cultured CM by immunofluorescent microscopy using specific anti-SERCA2 and anti-PLB antibodies. Double labeling technique revealed that PLB-positive CM also labeled with anti-SERCA2. Coexpression of SERCA2 and PLB in CM was supported by measurement of cell homogenate oxalate-supported Ca2+ uptake which was completely inhibited by thapsigargin and stimulated by protein kinase A-catalyzed phosphorylation. Under serum-free conditions, incubation of CM with the SERCA2a expression modulator 3,3′,5-triiodo-L-thyronine (100 nM, 72 h) resulted in elevated Ca2+ uptake of +33%. Specific Ca2+ uptake activity was not altered if insulin was omitted from the serum-free culture medium but total SR Ca2+ transport activity was reduced under this culture condition. The results indicate that primary culture of spontaneously contracting neonatal rat CM can be employed as a useful model system for investigating both short- and long-term mechanisms determining the Ca2+ re-uptake function of the SR under defined culture conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006850724830
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Immunocytochemical studies of the Gi Protein mediated muscarinic receptor-adenylyl cyclase system (1995)
    Springer
    Molecular and cellular biochemistry 147 (1995), S. 161-168 
    Details
    ISSN: 1573-4919
    Keywords: adenylyl cyclase ; muscarinic receptors ; G-proteins ; immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The localization of three key signal transduction components was indicated in rat heart tissue by immunocytochemical and histochemical experiment. It was shown that: 1. The M2 muscarinic receptors are localized along outer cell membranes and T-tubule membranes of cardiomyocytes but additionally at membranes of endothelial cells and fibroblasts. 2. Giα was found along outer cell membranes of cardiomyocytes and other cells of the heart and also inside the cells of the perinuclear space in close contact to the nuclei envelope and the endoplasmic reticulum membranes. Goα were found to be associated mainly in atrial tissue, especially at the nerval (neuronal) endings located among the cardiac muscle cells. This was shown in parallel incubation with specific neuronal antibody as a marker for these structures. 3. Adenylyl cyclase was localized along the sarcolemma and the T-tubule membranes in normal cardiomyocytes of rat and guinea pig hearts. Under ischemic conditions, the adenylyl cyclase was also seen in junctional sarcoplasmic reticulum membranes. The reasons for this changed localization need further elucidation. Binding of the adenylyl cyclase within the molecular structure of the membrane or variation of the marker penetration remain to be clarified.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00944796
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Renaissance of cytochemical localization of membrane ATPases in the myocardium (1995)
    Springer
    Molecular and cellular biochemistry 147 (1995), S. 169-172 
    Details
    ISSN: 1573-4919
    Keywords: membrane ATPases ; cytochemistry ; myocardium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract ATPases of cardiac cells are known to be among the most important enzymes to maintain the fluxes of vital cations by hydrolysis of the terminal high-energy phosphate of ATP. Biochemically the activities of Ca2+-pump ATPase, Ca2+/Mg2+-ecto ATPase, Na+,K+-ATPase and Mg2+-ATPase are determined in homogenates and isolated membranes as well as in myofibrillar and mitochondrial fractions of various purities. Such techniques permit estimation of enzyme activitiesin vitro under optimal conditions without precise enzyme topography. On the other hand, cytochemical methods demonstrate enzyme activityin situ, but not under optimal conditions. Until recently several cytochemical methods have been employed for each enzyme in order to protect its specific activity and precise localization but the results are difficult to interpret. To obtain more consistent data from biochemical and cytochemical point of view, we modified cytochemical methods in which unified conditions for each ATPase were used. The fixative solution (1% paraformaldehyde −0.2% glutaraldehyde in 0.1 M Tris Base buffer, pH 7.4), the same cationic concentrations of basic components in the incubation medium (0.1 M Tris Base, 2mM Pb(NO2)3, 5 mM MgSO4, 5 mM ATP) and selective stimulators or inhibitors were employed. The results reveal improved localization of Ca2+-pump ATPase, Na+−K+ ATPase and Ca2+/Mg2+-ecto ATPase in the cardiac membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00944797
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Über das Volumenverhältnis von Mitochondrien zu Myofibrillen im chronisch überlasteten, hypertrophierten Herzen (1962)
    Springer
    Naturwissenschaften 49 (1962), S. 161-162 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00640140
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Elektronenmikroskopische Darstellung von ATPase-Aktivität an den Cristae mitochondriales und anderen Membranstrukturen im Herzmuskel (1962)
    Springer
    Naturwissenschaften 49 (1962), S. 376-377 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00629260
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Darstellung der Na+- und K+-abhängigen glykosidempfindlichen Adenosintriphosphatase des Herzmuskels an der Plasmamembran des Sarkolemms (1966)
    Springer
    Naturwissenschaften 53 (1966), S. 134-134 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00643351
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Elektronenmikroskopische Untersuchung zur Frage der Bindegewebsentstehung im embryonalen Herzmuskelverband des Hundes (1961)
    Springer
    Naturwissenschaften 48 (1961), S. 166-166 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00639552
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Localization of α1-adrenoceptors in rat and human hearts by immunocytochemistry (1996)
    Springer
    Molecular and cellular biochemistry 163-164 (1996), S. 159-165 
    Details
    ISSN: 1573-4919
    Keywords: immunocytochemistry ; antipeptide antibodies ; α1-adrenoceptors ; heart cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The localization of the ai adrenoceptors (α1-AR) in the heart tissues from rat and human and in the cultured heart cells from neonatal rats was studied by indirect immunofluorescence and postembedding electronmicroscopical immuno-gold technique. With antipeptide antibodies directed against the second extracellular loop of the human α1-AR (AS sequence 192–218), this receptor was found to be localized along the sarcolemma in both human and rat hearts. Similar localization sites were detected in cultivated rat neonatal cardiomyocytes. Beside the localization in cardiomyocytes, α1-AR were identified in endothelial cells of capillaries and smooth muscle cells of coronary vessels, in neuronal endings, in mast cells of cultivated heart cells but not, or in less amount in fibroblasts. Interestingly, in the right atrium of rat heart the localization of α1-AR was found to be near or on atrial natriuretic factor (ANF) granules, providing the basis for the α-adrenergic influence on ANF release. The immunocytochemical studies further confirm and complete the findings known by using autoradiographic binding studies with specific ligands.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00408653
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Localization of α1,2,3-subunit isoforms of Na,K-ATPase in cultured neonatal and adult rat myocardium: The immunofluorescence and immunocytochemical study (1996)
    Springer
    Molecular and cellular biochemistry 163-164 (1996), S. 39-45 
    Details
    ISSN: 1573-4919
    Keywords: Na,K-ATPase ; localization ; immunofluorescence ; immunoelectron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract By indirect immunofluorescence and preembedding peroxidase-diaminobenzidine technique the localization of polyclonal and monoclonal antibodies against α1, α2 and α3 isoforms of the Na,K-ATPase were studied in rat myocardium. The α1-subunit was identified predominantly on sarcolemma of cultured myocytes, neonatal, as well as adult cardiocytes. The α2 signal was localized around nuclei of cultured cardiocytes, very weak signals were seen in neonatal and more intense signal, were dispersed throughout the adult myocytes. The α3-subunit immunoreactivity was weak and localized in cell processes connecting individual cultured cells, on sarcolemma and intercalated discs of neonatal cells and very weak in adult working myocytes. Cytochemically demonstrated ouabain resistant Na,K-ATPase localized in junctional sarcoplasmic reticulum may represent α1 isoenzyme which is directly involved in modulation of action potential fluxes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00408639
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Cytochemical and immunocytochemical localization of Na,K-ATPase α subunit isoenzymes in the rat heart (1997)
    Springer
    Molecular and cellular biochemistry 176 (1997), S. 107-112 
    Details
    ISSN: 1573-4919
    Keywords: immunogold staining ; adult myocytes ; subsarcolemmal ATPase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract In order to understand the functional significance of Na,K-ATPase subunits as well as their isoenzymes, a precise subcellular localization of these in the myocyte is a crucial prerequisite. Cytochemical, immunofluorescence, preembedding immunogold and horse radish peroxidasediaminobenzidine methods, demonstrated α1 isoenzyme immunoreactivity on the sarcolemma, T-tubules and the subsarcolemmal cisterns of the adult cardiac myocytes. Cytochemically, ouabain resistant Na,K-ATPase precipitate was localized only in the subsarcolemmal cisterns and junctional sarcoplasmic reticulum. For α2 isoenzyme, immunoreactivity was demonstrated on the sarcolemma as well as in all areas of the myocytes in particularly a close proximation to the sarcoplasmic reticulum and microsomes. For α3 isoenzyme, only a weak insignificant signal was noted on the sarcolemma, intercalated disc and sarcoplasm. It is suggested that cytochemical ouabain resistant precipitate present in subsarcolemmal cisterns and junctional sarcoplasmic reticulum represent α1 isoenzyme of Na,K-ATPase. A differential as well as unique localization of α subunit isoenzymes of Na,K-ATPase in specific structures of cardiac myocytes may suggest importance in physiological function at these sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006883130242
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...