[Effect of modification of been venom components on its hemolytic activity and ability to decrease the volume of the human erythrocyte].

T A Parchenko; S V Rudenko

PubMed · 10609324

[Effect of modification of been venom components on its hemolytic activity and ability to decrease the volume of the human erythrocyte].

Abstract

The crude bee venom was modified by different chemical substances. The inverse correlation was established between increase of the hemolytic activity and decrease of the contractive one under modification of the bee venom by NaOH and KOH. The negligible decrease of the contractive activity occurs in the acid conditions (pH 1,0), while hemolytic one is stationary. Dithiothreitol, mercaptoethanol, urea and high temperature (60-90 degrees C) did not affect activity of the bee venom.

Explore related subjects

Bee Venoms Dithiothreitol Erythrocyte Volume Hemolysis Hot Temperature Humans Hydroxides In Vitro Techniques Mercaptoethanol Potassium Compounds Sodium Hydroxide English Abstract Journal Article

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

T A Parchenko, S V Rudenko. [Effect of modification of been venom components on its hemolytic activity and ability to decrease the volume of the human erythrocyte].. https://pubmed.ncbi.nlm.nih.gov/10609324/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2000

Shift from Th2 to Th1 response in immunotherapy with venoms.

Cytokines released from T lymphocytes regulate antibody production by B lymphocytes and releasability of mast cells and basophils. Immune tolerance in specific allergen (Ag) immunotherapy (SIT) might be a consequence of decreased Th2 or increased Th1 response of Ag specific T lymphocytes. We compared function of T lymphocytes in 11 patients with Hymenoptera venom allergy and in 7 healthy volunteers. We followed function of T lymphocytes in 6 patients during SIT. We measured released IL-2, IFN-gamma, IL-4 and IL-5 from Ag and mitogens (either with phorbol-myristate-acetate (PMA) and ionomycin or anti-CD3 antibodies) stimulated peripheral blood mononuclear cells (PBMC). After stimulation with Ag PBMC of patients released 86 +/- 133 pg/ml IFN-gamma and 19.7 +/- 20.1 pg/ml IL-4 (Th2 response), PBMCs of healthy controls released 184 +/- 116 pg/ml IFN-gamma and 4.8 +/- 8 pg/ml IL-4 (Th1 response). Spontaneous release of IFN-gamma in cultures of PBMC of patients increased after rush SIT (before: 25 +/- 31 pg/ml, after 241 +/- 281 pg/ml, p<0.05). After 6 months of SIT response of PBMCs of patients became similar to response of PBMCs of healthy controls. Time pattern of cytokines secreted from PBMCs after stimulation with PMA and ionomycin was different than after stimulation through T-cell receptor/CD3 complex.

Bee Venoms↗

PubMed1999

Ultraviolet Raman examination of the environmental dependence of bombolitin I and bombolitin III secondary structure.

Bombolitin I and III (BI and BIII) are small amphiphilic peptides isolated from bumblebee venom. Although they exist in predominately nonhelical conformations in dilute aqueous solutions, we demonstrate, using UV Raman spectroscopy, that they become predominately alpha-helical in solution at pH > 10, in high ionic strength solutions, and in the presence of trifluoroethanol (TFE) and dodecylphosphocholine (DPC) micelles. In this paper, we examine the effects of electrostatic and hydrophobic interactions that control folding of BI and BIII by systematically monitoring their secondary structures as a function of solution conditions. We determine the BI and BIII secondary structure contents by using the quantitative UV Raman methodology of Chi et al. (1998. Biochemistry. 37:2854-2864). Our findings suggest that the alpha-helix turn in BIII at neutral pH is stabilized by a salt bridge between residues Asp2 and Lys5. This initial alpha-helical turn results in different BI and BIII alpha-helical folding mechanisms observed in high pH and high salt concentrations: BIII folds from its single alpha-helix turn close to its N-terminal, whereas the BI alpha-helix probably nucleates within the C-terminal half. We also used quasielastic light scattering to demonstrate that the BI and BIII alpha-helix formation in 0.2 M Ca(ClO4)2 is accompanied by formation of trimers and hexamers, respectively.

Bee Venoms↗

PubMed1999

IL-10-induced anergy in peripheral T cell and reactivation by microenvironmental cytokines: two key steps in specific immunotherapy.

Specific immunotherapy (SIT) is widely used for treatment of allergic diseases and could potentially be applied in other immunological disorders. Induction of specific unresponsiveness (anergy) in peripheral T cells and recovery by cytokines from the tissue microenvironment represent two key steps in SIT with whole allergen or antigenic T cell peptides (PIT). The anergy is directed against the T cell epitopes of the respective antigen and characterized by suppressed proliferative and cytokine responses. It is initiated by autocrine action of IL-10, which is increasingly produced by the antigen-specific T cells. Later in therapy, B cells and monocytes also produce IL-10. The anergic T cells can be reactivated by different cytokines. Whereas IL-15 and IL-2 generate Th1 cytokine profile and an IgG4 antibody response, IL-4 reactivates a Th2 cytokine pattern and IgE antibodies. Increased IL-10 suppresses IgE and enhances IgG4 synthesis, resulting in a decreased antigen-specific IgE:IgG4 ratio, as observed normally in patients after SIT or PIT. The same state of anergy against the major bee venom allergen, phospholipase A2, can be observed in subjects naturally anergized after multiple bee stings. Together, these data demonstrate the pivotal role of autocrine IL-10 in induction of specific T cell anergy and the important participation of the cytokine microenvironment in SIT. Furthermore, knowledge of the mechanisms explaining reasons for success or failure of SIT may enable possible predictive measures of the treatment.

Bee Venoms↗