Isolation of Extracellular Vesicles of Holothuria (Sea Cucumber ).

Extracellular vesicles (EVs), carriers of molecular signals, are considered a critical link in maintaining homeostasis in mammals. Currently, there is growing interest in studying the role of EVs, including exosomes (subpopulation of EVs), in animals of other evolutionary levels, including marine invertebrates. We have studied the possibility of obtaining appropriate preparations of EVs from whole-body extract of holothuria using a standard combination of centrifugation and ultracentrifugation.

Protease and DNase Activities of a Very Stable High-Molecular-Mass Multiprotein Complex from Sea Cucumber .

Only some human organs, including the liver, are capable of very weak self-regeneration. Some marine echinoderms are very useful for studying the self-regeneration processes of organs and tissues. For example, sea cucumbers Eupentacta fraudatrix (holothurians) demonstrate complete restoration of all organs and the body within several weeks after their division into two parts.

Comparison of the Content of Several Elements in Seawater, Sea Cucumber and Its High-Molecular-Mass Multiprotein Complex.

Metal ions and other elements play many different critical roles in all biological processes. They can be especially important in high concentrations for the functioning of organisms living in seawater. It is important to understand how much the concentrations of different trace elements in such organisms can be higher than in seawater.

Very Stable Two Mega Dalton High-Molecular-Mass Multiprotein Complex from Sea Cucumber .

In contrast to many human organs, only the human liver can self-regenerate, to some degree. Some marine echinoderms are convenient objects for studying the processes of regenerations of organs and tissues. For example, sea cucumbers can completely restore within several weeks, the internal organs and the whole body after their division into two or three parts.

Twenty Element Concentrations in Human Organs Determined by Two-Jet Plasma Atomic Emission Spectrometry.

In this paper, we have performed determination of the concentration of twenty elements in seven human organs (spleen, liver, kidney, muscle, heart, lungs, and brain) using two-jet plasma atomic emission spectrometry. The method allows multielemental analysis of solid samples without wet acid digestion. Before analysis, all human organs were first dried, ground to powders, and carbonized.

Comparison of Trace Elements in High-Molecular-Mass Multiprotein Complex and in Female Milk from Which It Was Obtained.

Background: Many biological processes are performed by different protein complexes. During the association of proteins and enzymes forming specific complexes, the latter can include ions of various metal ions, which may be important for their formation and biological function.

Objective Of The Studies: However, to date in the literature there are no data on metal ions that are part of any protein complexes.

Cow Milk Lactoferrin Possesses Several Catalytic Activities.

Lactoferrin (LF) is a Fe-binding glycoprotein, that was first recognized in milk and then in other epithelial secretions and barrier body fluids to which many different functions have been attributed to LF including protection from iron-induced lipid peroxidation, immunomodulation, cell growth regulation, DNA and RNA binding, as well as transcriptional activation, еtс. The polyfunctional physiological role of LF is still unclear, but it has been suggested to be responsible for primary defense against microbial and viral infections. It was shown previously that human milk LF possesses several enzymatic activities: DNase, RNase, ATPase, phosphatase, and amylase.

DNase and RNase activities of fresh cow milk lactoferrin.

Lactoferrin (LF) is an Fe -binding glycoprotein first recognized in milk and then in other epithelial secretions and barrier body fluids to which many different functions have been attributed to LF, including protection from iron-induced lipid peroxidation, immunomodulation, cell growth regulation, DNA and RNA binding, as well as transcriptional activation, еtс. The polyfunctional physiological role of LF is still unclear, but it has been suggested to be responsible for primary defense against microbial and viral infections. Here, we present the first evidence that LF preparations isolated from milk of 18 cows of different breeds possess various levels of metal-dependent DNase and metal-independent RNase activities.

Extremely stable high molecular mass soluble multiprotein complex from eggs of sea urchin Strongylocentrotus intermedius with phosphatase activity.

It was proposed that most biological processes are performed by different protein complexes. In contrast to individual proteins and enzymes, their complexes usually have other biological functions, and their formation may be important system process for the expansion of diversity and biological functions of different molecules. Identification and characterization of embryonic components including proteins and their multiprotein complexes seem to be very important for an understanding of embryo function.

Human serum and milk albumins are metal-dependent DNases.

It is known that that human serum albumin (HSA) and alpha-lactalbumin (LA) possess DNA-binding sites. Electrophoretically homogeneous HSA and LA containing no canonical enzymes were isolated from human sera and milk. Here we have analyzed for the first time the possibility of DNA hydrolysis by these proteins.

How human serum albumin recognizes DNA and RNA.

We show here for the first time that HSA possesses two nucleic acid-(NA) binding sites and we estimated the relative contributions of the nucleotide links of (pN)n to their total affinity for these binding sites with higher and lower affinity for NAs. The minimal ligands of these binding sites are orthophosphate (Kd=3.0 and 20.

Very stable high molecular mass multiprotein complex with DNase and amylase activities in human milk.

For breastfed infants, human milk is more than a source of nutrients; it furnishes a wide array of proteins, peptides, antibodies, and other components promoting neonatal growth and protecting infants from viral and bacterial infection. It has been proposed that most biological processes are performed by protein complexes. Therefore, identification and characterization of human milk components including protein complexes is important for understanding the function of milk.

Extremely stable soluble high molecular mass multi-protein complex with DNase activity in human placental tissue.

Human placenta is an organ which protects, feeds, and regulates the grooving of the embryo. Therefore, identification and characterization of placental components including proteins and their multi-protein complexes is an important step to understanding the placenta function. We have obtained and analyzed for the first time an extremely stable multi-protein complex (SPC, ∼ 1000 kDa) from the soluble fraction of three human placentas.

Recognition of specific and nonspecific DNA by human lactoferrin.

The general principles of recognition of nucleic acids by proteins are among the most exciting problems of molecular biology. Human lactoferrin (LF) is a remarkable protein possessing many independent biological functions, including interaction with DNA. In human milk, LF is a major DNase featuring two DNA-binding sites with different affinities for DNA.

DNA, oligosaccharides, and mononucleotides stimulate oligomerization of human lactoferrin.

Using small-angle X-ray scattering (SAXS), light scattering (LS), and soft laser ablation we have shown that lactoferrin (LF) in solution at neutral pH is oligomerized in the absence of salt or at physiological salt concentrations. The level of oligomerization depends on the concentration of LF, KCl or NaCl, and on the duration of the protein storage in solution. At the concentrations comparable with those in human milk (1-6 mg/ml), the average radius of gyration (R(g)) values of LF can attain 400-480 A, while fresh solution of previously lyophylized LF demonstrate a lower average R(g) (50-100 A), and R(g) value characterizing the LF monomer formed at 1 M NaCl is 26.