ABSTRACT
We performed the matrix-assisted laser desorption/ionisation, time-of-flight mass spectrometry (MALDI-TOF) analysis of the peptides entering into the composition of not yet explored bioregulators derived from the extracellular matrix of the tissues of the various organs of the mammals, and also plants and fungi. The study included 15 different mammalian tissues, 13 species of plants, and 2 species of fungi. Exploring the bioregulators derived from eye tissues, we demonstrated that their composition includes peptide components with the same values of the molecular weight. The composition of the bioregulators derived from the tissues of various organs of mammals or different species of plants and fungi includes the peptides with different values of molecular weight. Obtained data indicate the growing evidence of the assumptions about the major function of the bioregulators of this group--their involvement in the regulation of tissue-organ homeostasis in the biological systems.
Subject(s)
Biological Products/isolation & purification , Extracellular Space/chemistry , Eye Proteins/analysis , Peptides/isolation & purification , Tissue Extracts/chemistry , Animals , Biological Products/chemistry , Bone and Bones/chemistry , Brain Chemistry , Cattle , Female , Fungi/chemistry , Liver/chemistry , Male , Molecular Weight , Myocardium/chemistry , Peptides/chemistry , Plants/chemistry , Rats , Rats, Wistar , Spectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationABSTRACT
Proteins with physicochemical properties and biological activity similar to those of membrano-tropic homeostatic tissue-specific bioregulators that had been found earlier in various animal tissues were discovered in leaves of the common plantain (Plantago major L.). To study the specific activity of these plant proteins, we developed an experimental model for organotypic roller cultivation of newt (Pleurodeles waltl) skin tissue in vitro. We showed that the plant proteins of interest exert the wound-healing effect, which is characteristic of this plant, on the skin of vertebrates both in vitro and in vivo.
Subject(s)
Biological Products/isolation & purification , Plant Leaves/chemistry , Plant Proteins/isolation & purification , Plantago/chemistry , Skin/drug effects , Wounds and Injuries/drug therapy , Animals , Biological Products/chemistry , Biological Products/pharmacology , Culture Media , Electrophoresis, Polyacrylamide Gel , Female , Isoelectric Focusing , Male , Mice , Mice, Inbred C57BL , Mice, Inbred CBA , Plant Extracts/chemistry , Plant Proteins/chemistry , Plant Proteins/pharmacology , Salamandridae , Skin/injuries , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization , Tissue Culture Techniques , Wound Healing/drug effects , Wounds and Injuries/pathologyABSTRACT
A protein with a molecular weight of 70 kDa was isolated from bovine blood serum and purified to a homogenous state. This protein inhibited reversibly the adhesive serum glycoprotein with a molecular weight of 12 kDa, which displayed biological activity at ultralow doses. Amino acid analysis showed that the protein inactivator belongs to the group of prealbumins from vertebrate blood serum. The secondary structure of its molecule was characterized by a considerable number of alpha-helices. The conditions for inactivation of serum glycoprotein were studied. The interaction between the serum glycoprotein and the protein inactivator occurred over a long period of time (1 day). It should be emphasized that the presence of calcium ions was a necessary condition for the inactivation of the serum glycoprotein. The data suggest that inactivation of serum glycoprotein results from the formation of a molecular complex consisting of the protein inactivator and the glycoprotein, which is related to the carbon-protein interaction.
Subject(s)
Cell Adhesion Molecules/blood , Glycoproteins/blood , Receptors, Immunologic/blood , Receptors, Peptide/blood , Amino Acids/analysis , Animals , Calcium , Cattle , Cell Adhesion Molecules/antagonists & inhibitors , Cell Adhesion Molecules/chemistry , Glycoproteins/antagonists & inhibitors , Glycoproteins/chemistry , Molecular Weight , Prealbumin/chemistry , Protein Binding , Protein Structure, Secondary , Receptors, Immunologic/chemistry , Receptors, Immunologic/isolation & purification , Receptors, Peptide/chemistry , Receptors, Peptide/isolation & purification , Time FactorsABSTRACT
Amino acid composition, structure, and physicochemical properties of a low-molecular-weight glycoprotein from cattle blood serum (SGP) were studied. The content of carbohydrates (represented by mannose-rich oligosaccharides) amounted to 45-50 wt %. The value of specific partial heat of SGP, measured by differential scanning calorimetry (DSC), equaled 1.8 J/g.K, which is characteristic of unfolded proteins. Circular dichroic (CD) spectra of SGP led us to conclude that it is not highly structured and that it occurs in the shape of a statistical globule. The protein was deglycated using anhydrous trifluoromethane sulfonate (TFMS), after which its amino acid composition and the sequence of a fragment were determined. The results indicate that SGP is a protein not studied previously.