Glycoproteins in the context of "Lecithin–sphingomyelin ratio"

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👉 Glycoproteins in the context of Lecithin–sphingomyelin ratio

The lecithin–sphingomyelin ratio (L/S ratio or L-S ratio) is a test of fetal amniotic fluid to assess for fetal lung immaturity. Lungs require surfactant, a soap-like substance, to lower the surface tension of the fluid coating the alveolar epithelium in the lungs. This is especially important for premature babies trying to expand their lungs after birth. Surfactant is a mixture of lipids, proteins, and glycoproteins, lecithin and sphingomyelin being two of them. Lecithin makes the surfactant mixture more effective.

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Glycoproteins in the context of Glycocalyx

The glycocalyx is a microscopic, hair-like coating which covers the outer surface of virtually all cells, and plays a critical role in most signalling between cells and their surrounding environments. It is composed of branching biomolecules like proteins and lipids sometimes longer than the cell's own diameter, with various sugars covalently bound to them at particular locations.

The glycocalyx (pl.: glycocalyces or glycocalyxes), also known as the pericellular matrix and cell coat, is an external organelle consisting of a layer of glycosylated biomolecules called glycoconjugates, such as glycoproteins and glycolipids. These are embedded in and extend outwards from the cell membranes of virtually all cells. Generally, the carbohydrate portion of the glycolipids found on the surface of plasma membranes helps these molecules contribute to cell–cell recognition, communication, and intercellular adhesion.

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Glycoproteins in the context of S-layer

An S-layer (surface layer) is a part of the cell envelope found in almost all archaea, as well as in many types of bacteria.The S-layers of both archaea and bacteria consists of a monomolecular layer composed of only one (or, in a few cases, two) identical proteins or glycoproteins. This structure is built via self-assembly and encloses the whole cell surface. Thus, the S-layer protein can represent up to 15% of the whole protein content of a cell. S-layer proteins are poorly conserved or not conserved at all, and can differ markedly even between related species. Depending on species, the S-layers have a thickness between 5 and 25 nm and possess identical pores 2–8 nm in diameter.

The terminology "S-layer" was used the first time in 1976. The general use was accepted at the "First International Workshop on Crystalline Bacterial Cell Surface Layers, Vienna (Austria)" in 1984, and in the year 1987 S-layers were defined at the European Molecular Biology Organization Workshop on "Crystalline Bacterial Cell Surface Layers", Vienna as "Two-dimensional arrays of proteinaceous subunits forming surface layers on prokaryotic cells" (see "Preface", page VI in Sleytr "et al. 1988"). For a brief summary on the history of S-layer research see "References".A comprehensive historical account of the development of fundamental and applied S-layer research is given in the following current review.

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Glycoproteins in the context of Ground substance

Ground substance is an amorphous gel-like substance in the extracellular space of animals that contains all components of the extracellular matrix (ECM) except for fibrous materials such as collagen and elastin. Ground substance is active in the development, movement, and proliferation of tissues, as well as their metabolism. Additionally, cells use it for support, water storage, binding, and a medium for intercellular exchange (especially between blood cells and other types of cells). Ground substance provides lubrication for collagen fibers.

The components of the ground substance vary depending on the tissue. Ground substance is primarily composed of water and large organic molecules, such as glycosaminoglycans (GAGs), proteoglycans, and glycoproteins. GAGs are polysaccharides that trap water, giving the ground substance a gel-like texture. Important GAGs found in ground substance include hyaluronic acid, heparan sulfate, dermatan sulfate, and chondroitin sulfate. With the exception of hyaluronic acid, GAGs are bound to proteins called proteoglycans. Glycoproteins are proteins that attach components of the ground substance to one another and to the surfaces of cells. Components of the ground substance are secreted by fibroblasts. Usually it is not visible on slides, because it is lost during staining in the preparation process.

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