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  • Maackia amurensis haemagglutinin  (1)
  • TNFα  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Cloning and sequence analysis of theMaackia amurensis haemagglutinin cDNA (1994)
    Springer
    Glycoconjugate journal 11 (1994), S. 572-575 
    Details
    ISSN: 1573-4986
    Keywords: Maackia amurensis haemagglutinin ; cDNA cloning, amino acid sequence ; carbohydrate recognition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Maackia amurensis haemagglutinin (MAH) is a leguminous lectin which preferentially binds to a cluster of sialylatedO-linked carbohydrate chains (Konami Y, Yamamoto K, Osawa T, Irimura T (1994)FEBS Lett 342:334–38). In the present study a 950 bp cDNA clone encoding MAH was isolated from a cDNA library constructed from germinatedMaackia amurensis seeds. From the nucleotide sequence, MAH was predicted to consist of 285 amino acid residues containing a signal peptide of 29 amino acids. The results also confirmed our previous findings from the amino acid sequence analysis, which indicated that two highly conserved amino acid residues in all other well-known leguminous lectins were replaced in MAH. These residues were lysine-105 and aspartic acid-135. The corresponding amino acid residues in other leguminous lectins were glycine and asparagine, respectively. These differences were due to the presence of nucleotides AAA and GAT in place of AAT/C and GGA/T.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731308
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Antitumor effects of liposomal IL1α and TNFα against the pulmonary metastases of the B16F10 murine melanoma in syngeneic mice (1995)
    Springer
    Clinical & experimental metastasis 13 (1995), S. 249-259 
    Details
    ISSN: 1573-7276
    Keywords: antitumor activity ; IL1α ; liposomes ; pulmonary metastasis ; TNFα
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Interleukin 1 alpha (IL1α) and tumor necrosis factor alpha (TNFα) have been successfully incorporated into specific phosphatidylcholine (PC) and phosphatidylserine (PS) multilamellar vesicle (MLV) liposomes by modifying the concentration of calcium ion and pH of the encapsulation buffer. Under these conditions, some of the cytokines may attach to the exterior surface of the MLV and therefore be readily accessible to target cells for receptor binding and signal transduction. These cytokine-associated liposomes are stable for up to 2 weeks in serum-free buffer, and leakage of cytokines into medium containing 10% fetal bovine serum was about 50% at the end of a 3-day incubation period at 37°C. The biological activities mediated by liposomal IL1α and TNFα were specific: the stimulation of thymidine uptake in T-helper D10 lymphocytes and the cytolysis of TNFα-sensitive L929 target cells could be blocked by specific neutralizing antibodies in a dose-dependent fashion. When administered intravenously into C57BL/6 mice bearing the syngeneic B16F10 murine melanoma cells, dual entrapment of liposomal IL1α and TNFα significantly reduced the number of metastatic tumor nodules in the lungs and prolonged the life span of the animals. Thus, liposomal IL1α and TNFα displayed significant in vivo antitumor activity against the IL1α- and TNFα-resistant B16F10 metastatic murine melanoma.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00133480
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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