Structural requirements of human salivary peptides, histatins fgr histamine releasing activity.
نویسندگان
چکیده
منابع مشابه
Anti-tumoral activity of human salivary peptides.
Chemotherapy continues to be the standard treatment for advanced or metastasized cancer. However, commonly used chemotherapeutic agents may induce damage in healthy cells and tissues. Thus, in recent years, there has been an increased focus on the development of new, efficient anticancer drugs exhibiting low toxicity and that are not affected by mechanisms of chemoresistance. In the present wor...
متن کاملHistamine and its Releasing Agents
Spontaneous histamine release from isolarted Mastcells was found to be independent of calcium in the concentration range up to 1 m. mole/lit. Phosphatidyl serine do not change the effect of calcium on spontaneous release. The activation of anaphyla.ctic histamine release by calcium is potentiated by phosphatidyl serine but the laitter can't do so w1th strontium. Mastcells, pretreated with AT...
متن کاملSynthetic peptides comprising sequences of the human immunoglobulin E heavy chain capable of releasing histamine.
On the basis of previous studies on the structure-activity relationship of model polypeptide histamine liberators, a site within the Fc region of immunoglobulin E antibody molecules has been proposed as that responsible for the direct triggering of target mast cells after antigen challenge. Peptides comprising this region of the epsilon-chain have now been synthesized and shown to induce histam...
متن کاملSalivary histatins in human deep posterior lingual glands (of von Ebner).
OBJECTIVE Human saliva contains a family of low molecular weight histidine-rich proteins, named histatins, characterised by bactericidal and fungicidal activities in vitro against several microbial pathogens, such as Streptococcus mutans and Candida albicans. They represent a major component of an innate host non-immune defense system. In an earlier study we described the distribution of histat...
متن کاملInhibitory effects of human salivary histatins and lysozyme on coaggregation between Porphyromonas gingivalis and Streptococcus mitis.
The effects of histatins on coaggregation between Porphyromonas gingivalis 381 and Streptococcus mitis ATCC 9811 were investigated by using a turbidimetric assay. The coaggregation activity was significantly inhibited by histatins 5 and 8 and strongly by lysozyme. Tritium-labeled histatin 8 bound to P. gingivalis cells but not to S. mitis cells.
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ژورنال
عنوان ژورنال: Japanese Journal of Pharmacology
سال: 1991
ISSN: 0021-5198
DOI: 10.1016/s0021-5198(19)38379-9