A cell membrane is a membrane that is found surrounding the cell. It serves various purposes. It keeps the cell turgid and holds the contents of the cell. It is made up of lipid bilayer and can intake lipid-soluble substances. It serves as a barrier that prevents unwanted and unnecessary substances from entering the cell. Also, it allows the essential nutrients to make their way into the cell and helps the cell dispose of its waste material.
fluid mosaic model of cell membrane pdf download
Although the thickness and size of the cells vary from type of cell to cell, the cell organelles and the contents remain more or less the same. The contents of the cell depend on the function those cells have to play inside the body. For example, we can say that the mitochondrial inner membrane has 24% lipids and 76% proteins. Similarly, myelin constitutes 76% lipids and 18% proteins.
The matrix is a lipid that enables the contents to flow unhindered. This is due to the hydrophobic reactions of proteins and lipids. The non-polar regions of the phospholipids bind with the non-polar regions of the surrounding molecules. The polar area is present outside. This feature gives the structure of a lipid bilayer to the cell membrane. It helps in the being of the cell membrane, a semi-permeable barrier.
In this article, we have tried to explain the fluid, functional model of the cell membrane. This theory explains the very characteristics of the cell membrane as well as its functions. It throws light on the composition and the functionality of the cell membrane. Its selective permeability helps in the proper functioning of the body by allowing the required substances to enter the cells and the waste products to leave the cell. This model is a consistent one that has its restrictions urged by thermodynamics.
Like all other cellular membranes, the plasma membrane consists of both lipids and proteins. The fundamental structure of the membrane is the phospholipid bilayer, which forms a stable barrier between two aqueous compartments. In the case of the plasma membrane, these compartments are the inside and the outside of the cell. Proteins embedded within the phospholipid bilayer carry out the specific functions of the plasma membrane, including selective transport of molecules and cell-cell recognition.
The plasma membrane is the most thoroughly studied of all cell membranes, and it is largely through investigations of the plasma membrane that our current concepts of membrane structure have evolved. The plasma membranes of mammalian red blood cells (erythrocytes) have been particularly useful as a model for studies of membrane structure. Mammalian red blood cells do not contain nuclei or internal membranes, so they represent a source from which pure plasma membranes can be easily isolated for biochemical analysis. Indeed, studies of the red blood cell plasma membrane provided the first evidence that biological membranes consist of lipid bilayers. In 1925, two Dutch scientists (E. Gorter and R. Grendel) extracted the membrane lipids from a known number of red blood cells, corresponding to a known surface area of plasma membrane. They then determined the surface area occupied by a monolayer of the extracted lipid spread out at an air-water interface. The surface area of the lipid monolayer turned out to be twice that occupied by the erythrocyte plasma membranes, leading to the conclusion that the membranes consisted of lipid bilayers rather than monolayers.
As discussed in Chapter 2, the plasma membranes of animal cells contain four major phospholipids (phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, and sphingomyelin), which together account for more than half of the lipid in most membranes. These phospholipids are asymmetrically distributed between the two halves of the membrane bilayer (Figure 12.2). The outer leaflet of the plasma membrane consists mainly of phosphatidylcholine and sphingomyelin, whereas phosphatidylethanolamine and phosphatidylserine are the predominant phospholipids of the inner leaflet. A fifth phospholipid, phosphatidylinositol, is also localized to the inner half of the plasma membrane. Although phosphatidylinositol is a quantitatively minor membrane component, it plays an important role in cell signaling, as discussed in the next chapter. The head groups of both phosphatidylserine and phosphatidylinositol are negatively charged, so their predominance in the inner leaflet results in a net negative charge on the cytosolic face of the plasma membrane.
In addition to the phospholipids, the plasma membranes of animal cells contain glycolipids and cholesterol. The glycolipids are found exclusively in the outer leaflet of the plasma membrane, with their carbohydrate portions exposed on the cell surface. They are relatively minor membrane components, constituting only about 2% of the lipids of most plasma membranes. Cholesterol, on the other hand, is a major membrane constituent of animal cells, being present in about the same molar amounts as the phospholipids.
Because of its rigid ring structure, cholesterol plays a distinct role in membrane structure. Cholesterol will not form a membrane by itself, but inserts into a bilayer of phospholipids with its polar hydroxyl group close to the phospholipid head groups (see Figure 12.2). Depending on the temperature, cholesterol has distinct effects on membrane fluidity. At high temperatures, cholesterol interferes with the movement of the phospholipid fatty acid chains, making the outer part of the membrane less fluid and reducing its permeability to small molecules. At low temperatures, however, cholesterol has the opposite effect: By interfering with interactions between fatty acid chains, cholesterol prevents membranes from freezing and maintains membrane fluidity. Although cholesterol is not present in bacteria, it is an essential component of animal cell plasma membranes. Plant cells also lack cholesterol, but they contain related compounds (sterols) that fulfill a similar function.
While lipids are the fundamental structural elements of membranes, proteins are responsible for carrying out specific membrane functions. Most plasma membranes consist of approximately 50% lipid and 50% protein by weight, with the carbohydrate portions of glycolipids and glycoproteins constituting 5 to 10% of the membrane mass. Since proteins are much larger than lipids, this percentage corresponds to about one protein molecule per every 50 to 100 molecules of lipid. In 1972, Jonathan Singer and Garth Nicolson proposed the fluid mosaic model of membrane structure, which is now generally accepted as the basic paradigm for the organization of all biological membranes. In this model, membranes are viewed as two-dimensional fluids in which proteins are inserted into lipid bilayers (Figure 12.3).
The membrane-spanning portions of transmembrane proteins are usually α helices of 20 to 25 hydrophobic amino acids that are inserted into the membrane of the endoplasmic reticulum during synthesis of the polypeptide chain (see Figures 9.11, 9.12, and 9.13). These proteins are then transported in membrane vesicles from the endoplasmic reticulum to the Golgi apparatus, and from there to the plasma membrane. Carbohydrate groups are added to the polypeptide chains in both the endoplasmic reticulum and Golgi apparatus, so most transmembrane proteins of the plasma membrane are glycoproteins with their oligosaccharides exposed on the surface of the cell.
Studies of red blood cells have provided good examples of both peripheral and integral proteins associated with the plasma membrane. The membranes of human erythrocytes contain about a dozen major proteins, which were originally identified by gel electrophoresis of membrane preparations. Most of these are peripheral membrane proteins that have been identified as components of the cortical cytoskeleton, which underlies the plasma membrane and determines cell shape (see Chapter 11). For example, the most abundant peripheral membrane protein of red blood cells is spectrin, which is the major cytoskeletal protein of erythrocytes. Other peripheral membrane proteins of red blood cells include actin, ankyrin, and band 4.1. Ankyrin serves as the principal link between the plasma membrane and the cytoskeleton by binding to both spectrin and the integral membrane protein band 3 (see Figure 11.11). An additional link between the membrane and the cytoskeleton is provided by band 4.1, which binds to the junctions of spectrin and actin, as well as to glycophorin (the other major integral membrane protein of erythrocytes).
The two major integral membrane proteins of red blood cells, glycophorin and band 3, provide well-studied examples of transmembrane protein structure (Figure 12.6). Glycophorin is a small glycoprotein of 131 amino acids, with a molecular weight of about 30,000, half of which is protein and half carbohydrate. Glycophorin crosses the membrane with a single membrane-spanning α helix of 23 amino acids, with its glycosylated amino-terminal portion exposed on the cell surface. Although glycophorin was one of the first transmembrane proteins to be characterized, its precise function remains unknown. In contrast, the function of the other major transmembrane protein of red blood cells is well understood. This protein, originally known as band 3, is the anion transporter responsible for the passage of bicarbonate (HCO3-) and chloride (Cl-) ions across the red blood cell membrane. The band 3 polypeptide chain is 929 amino acids and is thought to have 14 membrane-spanning α-helical regions. Within the membrane, dimers of band 3 form globular structures containing internal channels through which ions are able to travel across the lipid bilayer.
In contrast to transmembrane proteins, a variety of proteins (many of which behave as integral membrane proteins) are anchored in the plasma membrane by covalently attached lipids or glycolipids (Figure 12.10). Members of one class of these proteins are inserted into the outer leaflet of the plasma membrane by glycosylphosphatidylinositol (GPI) anchors. GPI anchors are added to certain proteins that have been transferred into the endoplasmic reticulum and are anchored in the membrane by a C-terminal transmembrane region (see Figure 9.16). The transmembrane region is cleaved as the GPI anchor is added, so these proteins remain attached to the membrane only by the glycolipid. Since the polypeptide chains of GPI-anchored proteins are transferred into the endoplasmic reticulum, they are glycosylated and exposed on the surface of the cell following transport to the plasma membrane. 2ff7e9595c
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