The natural biological gift of nature in all BIOCUTIS products : Helix Aspersa Müller Glycoconjugates

It is a complex compound of glycomolecules made of carbohydrate or sulfated sugar chains (glyco = sugar), globular soluble proteins, uronic acids and several oligoelements: copper, zinc calcium and iron with rich biological functions that play a critical role for the sustaining of healthier tissues collected from little creatures of the species Helix Aspersa Müller.

Biochemical investigation of the fluid collected from snails of the aforementioned species proves it contains an heterogeneous compound of glycoconjugates, were we can find glycosaminoglycans, proteoglycans, glycoproteins, copper peptides, co-enzymes and zinc participating in the production of superoxide dismutase antioxidant.

Glycosaminoglycans (GAGs) are relatively large molecules composed of polysaccharide side chains attached to a core backbone of protein, forming a proteoglycan. Each polysaccharide side chain consists of a disaccharide repeat unit composed of hexosamine linked to uronic acids (either iduronic or glucuronic acid). The hexosamine is a glucosamine in heparin, and heparin sulfate and a galactosamine in dermatan sulfate (DS). The disaccharide units are heavily modified and the number of modifications allows for a large structural and functional diversity; it is the composition of the disaccharide side chains that defines the individual GAGs.

The disaccharides are often heavily sulfated and hence strongly negatively charged, and this may explain the pronounced ability of the GAGs to interact with proteins such as growth factors, enzymes, and chemokines. In the body, GAGs are present in mast cells (as heparin), in the extracellular matrix (ECM) and attached to cell surfaces. Clinically, GAGs are widely used for their anti-coagulating effects. Physiologically, the role of the GAGs has still to be fully determined. However, they are known to interact strongly with several growth factors, and therefore, GAGs are assumed to influence growth of normal as well as neoplastic (abnormal and cancer) cells and in the regulation of angiogenesis (growth of blood vessels) .

Order Out of Caos: The Function of Glycoconjugates

Proteoglycans, Glycoproteins and Glycosaminoglycans (GAGs) are active regulators of the cell's functions. They collaborate in cell-matrix communications and take a very important biological role in fibroblasts proliferation and in the differentiation and migration of all cells by effectively modulating the cell's phenotype.

Fibroblasts are the cells in the basal membrane of the skin that give rise to all components of the extracellular matrix, in particular to collagen, elastin, glycosaminoglycans and proteoglycans in the skin matrix.

The basement membrane (BM) is a specialized form of extracellular matrix (ECM) and has recently been recognized as an important regulator of cell behaviour, rather than just a structural feature of tissues. The BM mediates tissue compartmentalization and sends signals to epithelial cells about the external microenvironment.

Proteoglycans are heterogeneous macromolecules consisting of a center protein and one or more covalently attached glycosaminoglycan chain. The biological function of proteoglycans result primarely from the structurally regent glycosaminoglycans emanating from the protein center of the molecule. A large number of different animal species include GAGs and mollusks are a very rich source of these glycomolecules or polysaccharides.

GAGs are often found in the extracellular matrix of vertebrate and invertebrate tissues. Structural investigation shows that GAGs in invertebrate animal species often include unusual variations of sulfate distribution and uronic acids.

The major glycoconjugate of the land snail liquid fluid is a glycosaminoglycan, with a peculiar structure when put next to other recognized glycosaminoglycans. It is secreted from granules inside the snail's structure and is localized on the external surface as a response to exposure of the snail to stress.

What is the importacne of glycosaminoglycans?

Glycosaminoglycans are vital in normal animal development and in the prevention of a lot of diseases; glycans appear to play a role as scaffolds that mediate communications among cells and proteins.

Carbohydrates are indispensable to life. In their simple form, they serve as a main energy source that sustains life. For the most part, nonetheless, carbohydrates do not exist as simple sugars but as intrincated molecular conjugates, or glycans.

Glycans can appear in several shapes and sizes, from linear chains (polysaccharides) to extremely branched molecules bristling with antennae-like arms. And despite proteins and nucleic acids such as DNA have traditionally brought a more scientific care, glycans are also indispensable to life. They are ever-present in nature, forming the heterogeneous sugar cover that surrounds the cells of basically all organism and occupying the spots among these cells. As part of this so-named extracellular matrix, glycans, with their diverse chemical structures, play a very important part in communicating very important biochemical signals into and among the cells. In this way, these sugars command the cellular communication that is essential for normal cell and tissue development and physiological function.

GAGs form a vital component of connective tissues. GAG chains may be covalently attached to a protein to form proteoglycans.

Dermatan sulfate is a glycosaminoglycan found specially in skin, but also can be found blood vessels, heart valves, tendons, and also lungs. Dermatan sulfate may have a role in coagulation, cardiovascular disease, carcinogenesis, infection, wound recovery, and fibrosis.

Chondroitin sulfate is a sulfated glycosaminoglycan (GAG) composed of one chain of alternating sugars (N-acetyl-galactosamine and glucuronic acid). It is normally found united to proteins as part of a proteoglycan. A chondroitin chain can have almost 100 individual sugars, each of which can be sulfated in variable ways and quantities. Comprehending the activities of such diversity in chondroitin sulfate and related glycosaminoglycans is a major aim of glycobiology. Chondroitin sulfate is a big structural ingredient of cartilage and gives a lot of its tolerance to compression.

Complex sugars, or glycans, that are most of the times knitted to proteins, cover the outer parts of cells and fill the spaces among them. Needed in standard animal growing and in the prevention of many diseases, glycans seem to act as scaffolds that mediate communications among cells and proteins.

The Sweet Science of Glycobiology

Intrincated carbohydrates, molecules that are very important for interaction among cells, are coming under systematic study and shed light on the effects of the components of the snail secretions when used for skin care.

The main model of these days’ molecular biology is that biological data flows from DNA to RNA to protein. The strenght of this approach resides not only in its template-driven precision, but also in the capacity to manipulate any one type of molecules based on knowledge of another, and in the diagrams of sequence homology and relatedness that predict function and show evolutionary connections. With the expectedforthcoming finalization of the genomic sequences of humans and several other usually studied model organisms, even more amazing gains in the understanding of biological elements are looked forward to. Nonetheless, there’s often a tendency to take for correct the upcoming extension of the main model: DNA to RNA to PROTEIN to CELL to ORGANISM.

In actual fact, making a cell implies having two other major types of molecules: lipids and carbohydrates. These molecules can act as intermediates in producing energy, as signaling molecules, or as structural elements. The structural papers of carbohydrates become incredibly considerable in constructing heterogeneous multicellular organs and organisms, that needs communication of cells with one another and with the matrix around it. Actually, all cells and a great deal of macromolecules in nature have a compressed and heterogeneous display of covalently united sugar chains (called oligosaccharides or glycans).

In some instances, these glycans can also be free-standing entities. Since most glycans are on the external surface of cellular and secreted macromolecules, they are in a position to modulate or mediate a wide collection of events in cell-cell and cell-matrix communications vital to the development and action of a complex multicellular organism. They also are in a place to control communications between organisms (e.g., between host and parasite).

Plus, simple, highly dynamic protein-bound glycans are abundant in the nucleus and cytoplasm, where they appear to work as regulatory switches.

In the initial section of this century, the chemistry, biochemistry, and biology of carbohydrates were amazingly prominent matters of interest. Nevertheless, when going through the the first phase of the modern revolution in molecular biology, reseach about glycans lagged far behind those of other principal types of molecules. This was largely due to their own structural complexity, the complexity in simply concluding their sequence, and the reality that their biosynthesis could not be directly prognosticated from the DNA template.

The evolution of a variety of new technologies to explore the structures of these sugar chains has opened up a new universe of molecular biology that has been named glycobiology. This word was first spoken in 1988 by Rademacher, Parekh, and Dwek to talk about the coming together of the traditional disciplines of carbohydrate chemistry and biochemistry with modern understanding of the cellular and molecular biology of glycans. The word glycobiology has gainedwide acceptance, with a bigger biomedical journal, a growing scientific society, and a Gordon Research Conference now bearing this name.

Defined in the broadest way, glycobiology is then the study of the morphology, biosynthesis, and biology of saccharides (sugar chains or glycans) that are largely expanded in nature. It is one of the more quickly fields in the biomedical sciences, with importance to basic research, biomedicine, and biotechnology. Actually, many biotechnology, pharmaceutical, and laboratory supply enterprises have invested heavily in the matter.

The area ranges from the chemistry of carbohydrates and the enzymology of glycan-modifying proteins to the functions of glycans in heterogeneous biological systems, and their manipulation by a number of techniques.

Investigation in glycobiology needs a foundation not only in the nomenclature, biosynthesis, morphology, chemical synthesis, and activities of heterogeneous glycans, but also in the general disciplines of molecular genetics, cellular biology, physiology, and protein chemistry. This volume provides an overview of the area of glycobiology, including a special emphasis on the glycans of higher animal groups, about which the greatest quantity is actually known. It isassumed that the reader has a basic knowledge in graduate-level chemistry, biochemistry, and cell biology.

In these passed years, very important studies of a type of linear glycans recognized as glycosaminoglycans (or GAGs for short), and specialy a sub-set known as HSGAGs, that are build up of heparan sulfate and its relative heparin have shed a good deal of light on the action of the snail secretions we use to elaborate the snail skin treatment product.

The complex snail secretions contribute to the proper assembling neccesary for healthy skin repair, skin regeneration and skin renewal.

Building the Proper Configuration of Molecular Chains for Healthier Skin Tissues.

Glycans help the interaction of fibroblast growth factor (FGF) with its receptor at the cell surface. The binding of growth factor to its receptor starts a signaling cascade that finishes in the cell's nucleus, activating genes that modulate cellular proliferation.

An Heparan Sulfate GAG chain (HSGAG) can be characterized as a linear reiteration of approximately 10 to 100 disaccharide building blocks that, when united together, form the basis of each sugar molecule. In its most fundamental form, each disaccharide unit includes two chemically different monosaccharides (a uronic acid and a glucosamine) combined by a glycosidic bond. The chains may alter a great deal in their structural configuration because the disaccharide building blocks may be chemically altered at a number of positions.

These changes include the elimination of the two-carbon acetyl groups at the amino position of the glucosamine portion and the inclusion of sulfate groups at some different positions, along with differentiations in the stereochemical combination of bonds around especial carbons. Different combinations of these diverse chemical adjustments make it possible for even short chains to have an enormous number of structural combinations. Actually, the potential for an enormous quantity of structural information to be embedded in a glycan passes that of nucleic acids or proteins.

Contrary the synthesis of DNA, RNA or proteins, glycan synthesis does not depend on a template that codes for the exact precise sequence of building blocks in a new chain, to be faith-fully duplicated over and over again as an equivalent copy. Instead, GAGs are synthesized through the concerted action of a great repertoire of enzymes whose life and relative activities fluctuate very much. Inshort, HSGAG biosynthesis is a multi-step process that has various enzyme players.

Mainly the enzymes imply in HSGAG biosynthesis are now recognized, but exactly how the process of synthesis plays out is still in many areas an open question. We know just a few in regards to the ratio of enzymes or, even more basically essentially, whether they act independently or co-operatively in a multienzyme complex. It is known that HSGAGs are produced inside the cell in the membranes of the organelles called the Golgi apparatus. Most of all the enzymes implied making HSGAGs or span the organelle's membranes or are at least peripherally associated with them. This alignment essentially confines the equivalence of these enzymes to two dimensions within a lipid lattice.

Although the integral biochemical picture is not yet known, it is likely that the enzymes for HSGAG biosynthesis come together within the Golgi membrane, possibly as the chain is being constructed. For the most part, glycans don’t show at the cell outer part or in the extracellular matrix (ECM) as free-standing polymers. Rather, they are assembled onto determined proteins to form protein-glycan conjugates, or proteoglycans. With the exception of heparin, which is made as a free-standing sugar polymer, HSGAGs are mainly seeing in three major classes of proteoglycans.

A major distinction between these proteoglycans may be found in their particular alignment associated to the cell surface. In syndecans, the nucleous proteins cross the cell membrane. Glypicans are also put into membranes, but by a lipid anchor linked to the core protein. Perlecans reside in the ECM. There is much evidence that the unique composition of glycans attached to each core protein is not made at random.

Structure Determines Function. Proteoglycans are unique and morphologically intrincated macromolecules. A hint to the action of HSGAG proteoglycans shows from the long list of very relevant proteins with which they bind in discrete space and temporal communications.

These proteins include many vital growth factors and growth-factor receptors, proteins involved in in tissue and organ development and growing, others participating in immune and inflammatory replies, some that mediate cell adhesion, and so on. As in proteoglycans, the proteins that associate with them generally reside outside cells, both close to cell membranes or dispersed in all the ECM. Many of such proteins tour within the blood, where they are participants in systems such like blood coagulation, wound repair and tissue repair.

The communications in between glycans and the proteins they bind to show interactions in between structure and activity. These interactions among cells have normally been ascribed just to the noncovalent electrostatic attaction in between negatively charged sugars and positively charged proteins. A more exhaustive look, however, shows that several protein-glycan communications are as a matter of fact structurally selective. We here offer three examples of such specific communications—the binding of HSGAGs to antithrombin, to fibroblast growth factor (FBG) and to herpes simplex virus gD glycoprotein.

Sometimes, amazing structural determine commands the interaction in between HSGAGs and proteins under certain perspectivessujestive of the so-called lock-and-key complementarity in between enzymes and their substrates. The binding of heparin to antithrombin III (or ATIII) is a common sample of this interaction. ATIII is a protein that plays a very important role in the cascade of actions that takes us to blood coagulation.

Clinicians have noticed the influence of heparin on this process since the first years of 1930s, at the moment when heparin was first applied as an anticoagulant during a surgery. We now understand that when heparin unites to ATIII, this binding induces an important change in the creation of the protein. In turn, this change amazingly augments the inhibitory action that ATIII exerts on some other different proteins that commonly promote blood coagulation. A chain of tests have proven that just a small segment within heparin (that lives as a confused population of molecules) in fact binds to ATIII and induces its conformational change.

The minimal active binding sequence is a distinct pentasaccharide (that is, two-and-a-half disaccharide units). However, to jumstart as much anticoagulation as it would a full-length heparin molecule, a longer polysaccharide is required, one that can simultaneously bind to the protein thrombin as well as to antithrombin III. Although the HSGAG region that binds to thrombin doesn`t appear to need a specific line, its spacing relative to the ATIII-binding zone is really important.

This example illustrates two prominent views in regards to the interaction of proteins with HSGAGs, and maybe some other glycans. To begin with, the protein-binding region within the polysaccharide is not distributed at random throughout the chain; but, it is normally restricted to a limited number of contiguous disaccharides out of the more than 100 that might build its linear sequence. Second, a single glycan chain regularly posseses two or even more areas for protein binding. A person can think of the glycan, in this way, as a molecular connection that promotes the good interaction of two or several protein partners.

Fibroblast growth factor (FGF) signalling charmingly pictures the concept of HSGAGs bringing proteins together. In specific, the glycans facilitate the interaction of fibro-blast growth factor with its receptor at the cell exterior. The binding of growth factor to its receptor triggers a signaling cascade that ends up in the cell's nucleus, turning on genes that control cellular proliferation. To set in motion this cascade, a receptor embedded in the cell membrane needs to undergo a structural variation, a change that happens when one receptor interacts simultaneously with a second receptor.

It seems that the fibroblast growth factor (FGF) molecules in the exterior of the cell (at least in the case of the growth factor known as FGF-2) must on their own create a dimer, or pair, to put together two receptors on the cell exterior. Some investigations have demonstrated that FGF signaling may not completely need the presence of the glycan; yet in this congregation of molecules glycans do participate as a type of glue, maintaining the entire complex attached in the proper configuration needed for maximal signal transduction.

Choose a product according to your skin condition

Intense treatment serum to thorougly revitalize your skin. Apply 3 to 4 times a year for periods of 8 weeks once a day before bedtime.	For routine maintenance of normal and oily skin. Keeps skin deeply moisturized & looking younger & radiant.	For sensitive dry skin prone to allergies, eczema, dermatitis and rosacea.	To moisturize skin & get rid of dark pigmentation, age spots and rough sun damaged skin.
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