| Microvillus | |
|---|---|
 Enterocytes with microvilli | |
| Details | |
| Identifiers | |
| Latin | microvillus |
| MeSH | D008871 |
| TH | H1.00.01.1.01011 |
| FMA | 67296 |
| Anatomical terms of microanatomy | |
Microvilli (SG: microvillus) are microscopic cellular membrane protrusions that increase the surface area for diffusion and minimize any increase in volume, [1] and are involved in a wide variety of functions, including absorption, secretion, cellular adhesion, and mechanotransduction.
Microvilli are covered in plasma membrane, which encloses cytoplasm and microfilaments. Though these are cellular extensions, there are little or no cellular organelles present in the microvilli.
Each microvillus has a dense bundle of cross-linked actin filaments, which serves as its structural core. 20 to 30 tightly bundled actin filaments are cross-linked by bundling proteins fimbrin (or plastin-1), villin and espin to form the core of the microvilli.
In the enterocyte microvillus, the structural core is attached to the plasma membrane along its length by lateral arms made of myosin 1a and Ca2+ binding protein calmodulin. Myosin 1a functions through a binding site for filamentous actin on one end and a lipid binding domain on the other. The plus ends of the actin filaments are located at the tip of the microvillus and are capped, possibly by capZ proteins, [2] while the minus ends are anchored in the terminal web composed of a complicated set of proteins including spectrin and myosin II.
The space between microvilli at a cell's surface is called the intermicrovillous space. Intermicrovillous space increases with contractile activity of myosin II and tropomyosin, and decreases when contraction ceases.
Thousands of microvilli form a structure called the brush border that is found on the apical surface of some epithelial cells, such as the small intestines. (Microvilli should not be confused with intestinal villi, which are made of many cells. Each of these cells has many microvilli.) Microvilli are observed on the plasma surface of eggs, aiding in the anchoring of sperm cells that have penetrated the extracellular coat of egg cells. Clustering of elongated microtubules around a sperm allows for it to be drawn closer and held firmly so fusion can occur. They are large objects that increase surface area for absorption.
Microvilli are also of importance on the cell surface of white blood cells, as they aid in the migration of white blood cells.
As mentioned, microvilli are formed as cell extensions from the plasma membrane surface.
Actin filaments, present in the cytosol, are most abundant near the cell surface. These filaments are thought to determine the shape and movement of the plasma membrane.
The nucleation of actin fibers occurs as a response to external stimuli, allowing a cell to alter its shape to suit a particular situation.
This could account for the uniformity of the microvilli, which are observed to be of equal length and diameter. This nucleation process occurs from the minus end, allowing rapid growth from the plus end.
Though the length and composition of microvilli is consistent within a certain group of homogenous cells, it can differ slightly in a different part of the same organism.
For example, the microvilli in the small and large intestines in mice are slightly different in length and amount of surface coat covering. [3]
Microvilli function as the primary surface of nutrient absorption in the gastrointestinal tract. Because of this vital function, the microvillar membrane is packed with enzymes that aid in the breakdown of complex nutrients into simpler compounds that are more easily absorbed. For example, enzymes that digest carbohydrates called glycosidases are present at high concentrations on the surface of enterocyte microvilli. Thus, microvilli not only increase the cellular surface area for absorption, they also increase the number of digestive enzymes that can be present on the cell surface. Microvilli are also present on immune cells, allowing the immune cells to sense features on the surface of pathogens and other antigen-presenting cells. [4]
The microvilli are covered with glycocalyx, consisting of peripheral glycoproteins that can attach themselves to a plasma membrane via transmembrane proteins.
This layer may be used to aid binding of substances needed for uptake, to adhere nutrients or as protection against harmful elements.
It can be another location for functional enzymes to be localized.
The destruction of microvilli can occur in certain diseases because of the rearrangement of cytoskeleton in host cell. This is seen in infections caused by EPEC subgroup Escherichia coli , in celiac disease, and microvillus inclusion disease [5] (an inherited disease characterized by defective microvilli and presence of cytoplasmic inclusions of the cell membrane other than the apical surface).
The destruction of microvilli can actually be beneficial sometimes, as in the case of elimination of microvilli on white blood cells which can be used to combat auto immune diseases. [6]
Congenital lack of microvilli in the intestinal tract causes microvillus atrophy, a rare, usually fatal condition found in new-born babies.
The small intestine or small bowel is an organ in the gastrointestinal tract where most of the absorption of nutrients from food takes place. It lies between the stomach and large intestine, and receives bile and pancreatic juice through the pancreatic duct to aid in digestion. The small intestine is about 5.5 metres long and folds many times to fit in the abdomen. Although it is longer than the large intestine, it is called the small intestine because it is narrower in diameter.
The cytoskeleton is a complex, dynamic network of interlinking protein filaments present in the cytoplasm of all cells, including those of bacteria and archaea. In eukaryotes, it extends from the cell nucleus to the cell membrane and is composed of similar proteins in the various organisms. It is composed of three main components: microfilaments, intermediate filaments, and microtubules, and these are all capable of rapid growth or disassembly depending on the cell's requirements.
Smooth muscle is an involuntary non-striated muscle, so-called because it has no sarcomeres and therefore no striations. It is divided into two subgroups, single-unit and multiunit smooth muscle. Within single-unit muscle, the whole bundle or sheet of smooth muscle cells contracts as a syncytium.
Calcium metabolism is the movement and regulation of calcium ions (Ca2+) in (via the gut) and out (via the gut and kidneys) of the body, and between body compartments: the blood plasma, the extracellular and intracellular fluids, and bone. Bone acts as a calcium storage center for deposits and withdrawals as needed by the blood via continual bone remodeling.
A sarcomere is the smallest functional unit of striated muscle tissue. It is the repeating unit between two Z-lines. Skeletal muscles are composed of tubular muscle cells which are formed during embryonic myogenesis. Muscle fibers contain numerous tubular myofibrils. Myofibrils are composed of repeating sections of sarcomeres, which appear under the microscope as alternating dark and light bands. Sarcomeres are composed of long, fibrous proteins as filaments that slide past each other when a muscle contracts or relaxes. The costamere is a different component that connects the sarcomere to the sarcolemma.
Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils. It is found in essentially all eukaryotic cells, where it may be present at a concentration of over 100 μM; its mass is roughly 42 kDa, with a diameter of 4 to 7 nm.
Intestinal villi are small, finger-like projections that extend into the lumen of the small intestine. Each villus is approximately 0.5–1.6 mm in length, and has many microvilli projecting from the enterocytes of its epithelium which collectively form the striated or brush border. Each of these microvilli are about 1 µm in length, around 1000 times shorter than a single villus. The intestinal villi are much smaller than any of the circular folds in the intestine.
Enterocytes, or intestinal absorptive cells, are simple columnar epithelial cells which line the inner surface of the small and large intestines. A glycocalyx surface coat contains digestive enzymes. Microvilli on the apical surface increase its surface area. This facilitates transport of numerous small molecules into the enterocyte from the intestinal lumen. These include broken down proteins, fats, and sugars, as well as water, electrolytes, vitamins, and bile salts. Enterocytes also have an endocrine role, secreting hormones such as leptin.
The cell cortex, also known as the actin cortex, cortical cytoskeleton or actomyosin cortex, is a specialized layer of cytoplasmic proteins on the inner face of the cell membrane. It functions as a modulator of membrane behavior and cell surface properties. In most eukaryotic cells lacking a cell wall, the cortex is an actin-rich network consisting of F-actin filaments, myosin motors, and actin-binding proteins. The actomyosin cortex is attached to the cell membrane via membrane-anchoring proteins called ERM proteins that plays a central role in cell shape control. The protein constituents of the cortex undergo rapid turnover, making the cortex both mechanically rigid and highly plastic, two properties essential to its function. In most cases, the cortex is in the range of 100 to 1000 nanometers thick.
In biology, a protein filament is a long chain of protein monomers, such as those found in hair, muscle, or in flagella. Protein filaments form together to make the cytoskeleton of the cell. They are often bundled together to provide support, strength, and rigidity to the cell. When the filaments are packed up together, they are able to form three different cellular parts. The three major classes of protein filaments that make up the cytoskeleton include: actin filaments, microtubules and intermediate filaments.
A brush border is the microvillus-covered surface of simple cuboidal and simple columnar epithelium found in different parts of the body. Microvilli are approximately 100 nanometers in diameter and their length varies from approximately 100 to 2,000 nanometers. Because individual microvilli are so small and are tightly packed in the brush border, individual microvilli can only be resolved using electron microscopes; with a light microscope they can usually only be seen collectively as a fuzzy fringe at the surface of the epithelium. This fuzzy appearance gave rise to the term brush border, as early anatomists noted that this structure appeared very much like the bristles of a paintbrush.
Microfold cells are found in the gut-associated lymphoid tissue (GALT) of the Peyer's patches in the small intestine, and in the mucosa-associated lymphoid tissue (MALT) of other parts of the gastrointestinal tract. These cells are known to initiate mucosal immunity responses on the apical membrane of the M cells and allow for transport of microbes and particles across the epithelial cell layer from the gut lumen to the lamina propria where interactions with immune cells can take place.
The terminal web is a filamentous structure found at the apical surface of epithelial cells that possess microvilli. It is composed primarily of actin filaments stabilized by spectrin, which also anchors the terminal web to the apical cell membrane. The presence of myosin II and tropomyosin helps to explain the contractile ability of the terminal web. When contracted, the terminal web causes a decrease in diameter of the apex of the cell, causing the microvilli, which are anchored into the terminal web through their stiff actin fibers, to spread apart. This spreading apart of the microvilli aids cells in absorption.
Unconventional myosin-Ia is a protein that in humans is encoded by the MYO1A gene.
The intestinal epithelium is the single cell layer that form the luminal surface (lining) of both the small and large intestine (colon) of the gastrointestinal tract. Composed of simple columnar epithelial cells, it serves two main functions: absorbing useful substances into the body and restricting the entry of harmful substances. As part of its protective role, the intestinal epithelium forms an important component of the intestinal mucosal barrier. Certain diseases and conditions are caused by functional defects in the intestinal epithelium. On the other hand, various diseases and conditions can lead to its dysfunction which, in turn, can lead to further complications.
Actin remodeling is the biochemical process that allows for the dynamic alterations of cellular organization. The remodeling of actin filaments occurs in a cyclic pattern on cell surfaces and exists as a fundamental aspect to cellular life. During the remodeling process, actin monomers polymerize in response to signaling cascades that stem from environmental cues. The cell's signaling pathways cause actin to affect intracellular organization of the cytoskeleton and often consequently, the cell membrane. Again triggered by environmental conditions, actin filaments break back down into monomers and the cycle is completed. Actin-binding proteins (ABPs) aid in the transformation of actin filaments throughout the actin remodeling process. These proteins account for the diverse structure and changes in shape of Eukaryotic cells. Despite its complexity, actin remodeling may result in complete cytoskeletal reorganization in under a minute.
Rho-associated protein kinase (ROCK) is a kinase belonging to the AGC family of serine-threonine specific protein kinases. It is involved mainly in regulating the shape and movement of cells by acting on the cytoskeleton.
Plastin is part of a family of actin-bundling proteins, specifically the α-actinin family of actin-binding protein, which are found in many lifeforms, from humans and other animals to plants and yeasts. These proteins are known to cross-link actin filaments into bundles for various cell purposes.
In molecular biology, the FERM domain is a widespread protein module involved in localising proteins to the plasma membrane. FERM domains are found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain is located at the N terminus in the majority of proteins in which it is found.
Tuft cells are chemosensory cells in the epithelial lining of the intestines. Similar tufted cells are found in the respiratory epithelium where they are known as brush cells. The name "tuft" refers to the brush-like microvilli projecting from the cells. Ordinarily there are very few tuft cells present but they have been shown to greatly increase at times of a parasitic infection. Several studies have proposed a role for tuft cells in defense against parasitic infection. In the intestine, tuft cells are the sole source of secreted interleukin 25 (IL-25).