Library

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
    THE GLUCOSE FATTY ACID CYCLE IN OBESITY AND MATURITY ONSET DIABETES MELLITUS (1965)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 131 (1965), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1965.tb34800.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Assessment of proinsulin's effects on intermediary metabolism using the forearm technique in normal man (1993)
    Springer
    Acta diabetologica 30 (1993), S. 29-35 
    Details
    ISSN: 1432-5233
    Keywords: Forearm ; Lactate ; Man ; Proinsulin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We have compared the effects of human proinsulin and insulin on forearm metabolism. Seven normal, non-obese subjects were infused with 386 pmol/kg per hour of proinsulin and 180 pmol/kg per hour of insulin using the euglycaemic clamp technique. Glucose appearance and utilization rates were quantified using a primed continuous infusion of [6′,6′-2H2]glucose. Mean blood glucose was 4.1±0.1 and 4.1±0.2 mmol/l during proinsulin and insulin infusions respectively. Basal insulin concentrations increased from 0.02±0.01 to 0.25±0.03 nmol/l. The proinsulin infusion was chosen to give steady-state levels approximately 20-fold higher on a molar basis than those of insulin, based on previous findings that proinsulin has only 5% the biological potency of insulin. Basal proinsulin concentrations increased from 0.003 to 5.4±0.3 nmol/l. Hepatic glucose production was suppressed similarly during the last hour of each hormone infusion: 0.07±0.16 (proinsulin, P), and 0.01±0.13 (insulin, I) mg/kg per minute. Glucose disposal, however, was significantly increased during the final hour of the insulin infusion: 4.7±0.4 (I) and 3.4±0.2 (P) mg/kg per minute (P=0.025). Net forearm glucose uptake (FGU) increased by a greater amount during insulin compared with proinsulin infusion: 1.44±0.02 (I) and 0.71±0.01 (P) μmol/100 ml forearm per minute (P〈0.02). There was a small but significant net drop in arterialized blood lactate and pyruvate concentrations during proinsulin compared with insulin infusion: lactate −43±29 (P) and +63±35 (I) μmol/l (P〈0.01); pyruvate −8±3 (P) and +6±2 (I) μmol/l (P〈0.02). Arterialized blood alanine concentrations were similar during both series of hormone infusions. Forearm production and arterialized concentrations of glycerol were suppressed by equal amounts during the last hour of each hormone infusion. Despite greater FGU during insulin infusion, forearm production of lactate, pyruvate and alanine were similar during the last hour of each glucose clamp. These results indicate that in overnight fasted normal man: (1) proinsulin may have a preferential effect on the liver compared with muscle in terms of glucose handling; (2) proinsulin is less effective in stimulating FGU than is insulin; (3) from calculation of carbon flux across the forearm, proportionally less glucose was oxidized or stored during infusion of proinsulin compared with insulin; (4) proinsulin has similar effects on forearm lipolysis compared with insulin; (5) proinsulin may have a differential effect on splanchnic lactate metabolism compared with insulin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00572871
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Regulation of calcium-activated nonselective cation channel activity by cyclic nucleotides in the rat insulinoma cell line, CRI-G1 (1995)
    Springer
    The journal of membrane biology 145 (1995), S. 267-278 
    Details
    ISSN: 1432-1424
    Keywords: Rat insulinoma cell line, CRI-G1 ; Cyclic nucleotide regulation ; Calcium-activated nonselective cation channel ; Patch clamp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The regulation of a calcium-activated nonselective cation (Ca-NS+) channel by analogues of cyclic AMP has been investigated in the rat insulinoma cell line, CRI-G1. The activity of the channel is modulated by cyclic AMP in a complex way. In the majority of patches (83%) tested concentrations of cyclic AMP of 10 μm and above cause an inhibition of channel activity which is immediately reversible on washing. In contrast, lower concentrations of cyclic AMP, between 0.1 and 1.0 μm, produce a transient activation of channel activity in most patches (63%) tested. One group of analogues, including N6-monobutyryl cyclic AMP and N6, 2′-O-dibutyryl cyclic AMP reduced the activity of the Ca-NS+ channel at all concentrations tested and 2′-O-Monobutyryl cyclic AMP produced inhibition in all patches tested except one, at all concentrations. A second group produced dual concentration-dependent effects on Ca-NS+, low concentrations stimulating and high concentrations inhibiting channel activity. 6-Chloropurine cyclic AMP and 8-bromo cyclic AMP produced effects similar to those of cyclic AMP itself. In contrast, 8-[4-chlorophenylthio] cyclic AMP also showed a dual action, but with a high level of activation at all concentrations tested up to 1mm. Ca-NS+ channel activity was also predominantly activated by low concentrations of Sp-cAMPS. The activating effects of both Sp-cAMPS and cyclic AMP are antagonized by Rp-cAMPS, which by itself only produced a weak inhibition of Ca-NS+ channel activity even at concentrations of 10 μm and above. The results are discussed in terms of a model in which cyclic AMP, and other cyclic nucleotides, modulate the activity of the Ca-NS+ channel by binding to two separate sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00232718
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Nucleotide regulation of a calcium-activated cation channel in the rat insulinoma cell line, CRI-G1 (1994)
    Springer
    The journal of membrane biology 141 (1994), S. 101-112 
    Details
    ISSN: 1432-1424
    Keywords: Rat insulinoma cell line ; CRI-G1 ; Nucleotide regulation ; Calcium-activated nonselective cation channel ; Patch clamp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The nucleotide regulation of a calcium-activated nonselective cation (Ca-NS+) channel has been investigated in the rat insulinoma cell line CRI-G1. The activity of the channel is reduced by both AMP and ADP (1–100 μm) in a concentration-dependent manner, with AMP being more potent than ADP. At lower concentrations (0.1–5 μm), both ADP and AMP activate the channel in some patches. Examination of the nucleotide specificity of channel inhibition indicates a high selectivity for AMP over the other nucleotides tested with a rank order of potency of AMP 〉 UMP 〉 CMP ≥GMP. Cyclic nucleotides also modulate channel activity in a complex, concentration-dependent way. Cyclic AMP exhibits a dual effect, predominantly increasing channel activity at low concentrations (0.1–10 μm) and reducing it at higher concentrations (100 μm and 1 mm). Specificity studies indicate that the cyclic nucleotide site mediating inhibition of channel activity exhibits a strong preference for cyclic AMP over cyclic GMP, with cyclic UMP being almost equipotent with cyclic AMP. Cyclic IMP and cyclic CMP are not active at this site. The cyclic nucleotide site mediating activation of the channel shows much less nucleotide specificity than the inhibitory site, with cyclic AMP, cyclic GMP and cyclic IMP being almost equally active.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00238244
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Effects of chemical modification of amino and sulfhydryl groups on KATP channel function and sulfonylurea binding in CRI-G1 insulin-secreting cells (1994)
    Springer
    The journal of membrane biology 139 (1994), S. 167-181 
    Details
    ISSN: 1432-1424
    Keywords: KATP channels ; Chemical modification ; Sulfhydryl group ; Basic amino acids ; Pancreatic β-cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The effects of several group-specific chemical reagents were examined upon the activity of the ATP-sensitive potassium (KATP) channel in the CRI-G1 insulin-secreting cell line. Agents which interact with the sulfhydryl moiety (including 1 mM N-ethylmaleimide (NEM), 1 mM 5,5′-dithio-bis-(2-nitrobenzoic acid) (DNTB) and 1 mm o-iodobenzoate) produced an irreversible inhibition of KATP channel activity when applied to the intracellular surface of excised inside-out patches. This inhibition was substantially reduced when attempts were made to eliminate Mg2+ from the intracellular compartment. ATP 50 μm and 100 μm tolbutamide were each shown to protect against the effects of these reagents. The membrane impermeable DNTB was significantly less effective when applied to the external surface of outside-out patches. Agents which interact with peptide terminal amine groups and ɛ amino groups of lysine [1 mm methyl acetimidate and 1 mm trinitrobenzene sulfonic acid (TNBS)] and also the guanido group of arginine (1 mm methyl glyoxal) produced a Mg2+-dependent irreversible inhibition of KATP channel activity which could be prevented by ATP but not tolbutamide. The irreversible activation of the KATP channel produced by the proteolytic enzyme trypsin was prevented only when methyl glyoxal and methyl acetimidate were used in combination to inhibit channel activity. Radioligand binding studies showed that the binding of 3H glibenclamide was unaffected by any of the above agents with the exception of TNBS which completely inhibited binding with a EC50 of 307 ±6 μm. These results provide evidence for the presence of essential sulfhydryl (possibly cysteine), and basic amino acid (possibly lysine and arginine) residues associated with the normal functioning of the KATP channel. Furthermore, we believe that the sulfhydryl group in question is situated at the internal surface of the membrane, possibly near to the channel pore.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00232621
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    The effects of pyridine nucleotides on the activity of a calcium-activated nonselective cation channel in the rat insulinoma cell line, CRI-G1 (1994)
    Springer
    The journal of membrane biology 142 (1994), S. 299-307 
    Details
    ISSN: 1432-1424
    Keywords: Calcium-activated nonselective channel ; Rat insulinoma cell line ; CRI-G1 ; Pyridine nucleotides β-NAD+-NS+ channel ; Nucleotide regulation ; AMP
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The activity of a calcium-activated nonselective (Ca-NS+) channel in a rat insulinoma cell line (CRI-G1) is inhibited by pyridine nucleotides in excised patches. The effects of all four pyridine nucleotides tested, β-NAD+, β-NADH, β-NADP+ and β-NADPH were very similar when tested at 0.1 mm, and at 1 mm the phosphorylated forms, β-NADP+ and β-NADPH, appeared to be slightly more potent than β-NAD+ and β-NADH. All the pyridine nucleotides tested reduced both the open state probability of the channel and the number of functional channels observed in a single patch. The application of β-NAD+, but not of the other nucleotides tested, to the cytoplasmic surface of isolated inside-out patches from CRI-G1 cells opened a novel nonselective cation channel (the β-NAD+-NS+ channel). The activity of this new channel is calcium sensitive and may also be inhibited by AMP.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00233437
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Adenosine-5′-triphosphate-sensitive ion channels in neonatal rat cultured central neurones (1988)
    Springer
    Pflügers Archiv 412 (1988), S. 297-304 
    Details
    ISSN: 1432-2013
    Keywords: Cultured central neurones ; ATP-sensitive ; Patch-clamp ; Ion channels
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract ATP-sensitive channels were observed in isolated inside-out membrane patches from rat cultured central neurones. Two types of ATP-sensitive K+ channels were present in cortical neurones, one which had its open-state probability increased, the other its open-state probability decreased by application of ATP to the cytoplasmic membrane surface. Another, ATP-sensitive channel differing in ion conductance from all previously reported ATP-sensitive channels was also seen in patches from cortical neurones. This channel was noselective with respect to Na+, K+ and Cl− ions and ATP produced a “flickery” type of block. The non-hydrolysable analogue, AMPPNP, did not mimic ATP and prevented ATP action Preliminary experiments indicate that similar, but not, identical ATP-sensitive channels exist in cerebellar neurones
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00582512
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Human hormones in health and disease (1977)
    [s.l.] : Nature Publishing Group
    Nature 267 (1977), S. 470-470 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] THE editor of this multi-author book, Dr H. N. Antoniades, quotes with approval in his Introduction the 1960 statement of Dr G. W. Thorn in his foreword to Hormones in Human Plasma that it would be impossible "ever again, to contain within one single volume all information pertaining to this ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/267470b0
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Labelled Antibodies and Immunological Assay Systems (1968)
    [s.l.] : Nature Publishing Group
    Nature 219 (1968), S. 186-189 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Some proteins have unique properties which (usually in biological systems) can be measured with great sensitivity, but antibodies are the only reagents known to be capable of reacting specifically and at low concentration with a great many proteins. The use of radioactive isotopes has enabled the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/219186a0
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Measurement of human proinsulin by an indirect two-site immunoradiometric assay (1979)
    Springer
    Diabetologia 17 (1979), S. 229-234 
    Details
    ISSN: 1432-0428
    Keywords: Indirect two-site immunoradiometric assay ; human proinsulin ; insulin ; C-peptide ; diabetes ; insulinoma
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary An indirect two-site immunoradiometric assay is described for the measurement of human proinsulin in plasma. Polyethylene tubes coated with purified guinea-pig antibodies to insulin were used to extract proinsulin and insulin from plasma. Rabbit antibody to human C peptide was then added to react with the C-peptide moiety of the bound proinsulin. The uptake of this antibody was measured by the subsequent binding of125I-sheep antibody to rabbit IgG. The binding of radioactivity to the tubes was a function of the proinsulin concentration in the sample. The sensitivity of the assay was 0.006 pmol/ml. Only 200 μl of plasma was required in the assay and the125I-labelled antibody was produced from readily available reagents. The polyethylene tubes remained stable for at least 5 months after coating. The mean fasting proinsulin level was 0.009 pmol/ml in sixteen normal subjects and 0.025 pmol/ml in twelve maturity onset diabetics. Oral glucose produced an 8 fold increase in proinsulin concentration but a decline in the plasma proinsulin/insulin molar ratio. Four patients with insulinoma had extremely elevated proinsulin levels and proinsulin/insulin ratios.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01235859
    Library Location Call Number Volume/Issue/Year 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...