Actin in the context of Adherens junction

Cellular differentiation is the process in which a stem cell changes from one type to a differentiated one. Usually, the cell changes to a more specialized type. Differentiation happens multiple times during the development of a multicellular organism as it changes from a simple zygote to a complex system of tissues and cell types. Differentiation continues in adulthood as adult stem cells divide and create fully differentiated daughter cells during tissue repair and during normal cell turnover. Some differentiation occurs in response to antigen exposure. Differentiation dramatically changes a cell's size, shape, membrane potential, metabolic activity, and responsiveness to signals. These changes are largely due to highly controlled modifications in gene expression and are the study of epigenetics. With a few exceptions, cellular differentiation almost never involves a change in the DNA sequence itself. Metabolic composition, however, gets dramatically altered where stem cells are characterized by abundant metabolites with highly unsaturated structures whose levels decrease upon differentiation. Thus, different cells can have very different physical characteristics despite having the same genome.

A specialized type of differentiation, known as terminal differentiation, is of importance in some tissues, including vertebrate nervous system, striated muscle, epidermis and gut. During terminal differentiation, a precursor cell formerly capable of cell division permanently leaves the cell cycle, dismantles the cell cycle machinery and often expresses a range of genes characteristic of the cell's final function (e.g. myosin and actin for a muscle cell). Differentiation may continue to occur after terminal differentiation if the capacity and functions of the cell undergo further changes.

Biopolymers are natural polymers produced by the cells of living organisms. Like other polymers, biopolymers consist of monomeric units that are covalently bonded in chains to form larger molecules. There are three main classes of biopolymers, classified according to the monomers used and the structure of the biopolymer formed: polynucleotides, polypeptides, and polysaccharides. The polynucleotides, RNA and DNA, are long polymers of nucleotides. Polypeptides include proteins and shorter polymers of amino acids; some major examples include collagen, actin, and fibrin. Polysaccharides are linear or branched chains of sugar carbohydrates; examples include starch, cellulose, and alginate. Other examples of biopolymers include natural rubbers (polymers of isoprene), suberin and lignin (complex polyphenolic polymers), cutin and cutan (complex polymers of long-chain fatty acids), melanin, and polyhydroxyalkanoates (PHAs).

In addition to their many essential roles in living organisms, biopolymers have applications in many fields including the food industry, manufacturing, packaging, and biomedical engineering.

Muscle is a soft tissue, one of the four basic types of animal tissue. There are three types of muscle tissue in vertebrates: skeletal muscle, cardiac muscle, and smooth muscle. Muscle tissue gives skeletal muscles the ability to contract. Muscle tissue contains special contractile proteins called actin and myosin which interact to cause movement. Among many other muscle proteins present are two regulatory proteins, troponin and tropomyosin. Muscle is formed during embryonic development, in a process known as myogenesis.

Skeletal muscle tissue is striated, consisting of elongated, multinucleate muscle cells called muscle fibers, and is responsible for movements of the body. Other tissues in skeletal muscle include tendons and perimysium. Smooth and cardiac muscle contract involuntarily, without conscious intervention. These muscle types may be activated both through the interaction of the central nervous system as well as by innervation from peripheral plexus or endocrine (hormonal) activation. Skeletal muscle only contracts voluntarily, under the influence of the central nervous system. Reflexes are a form of non-conscious activation of skeletal muscles, but nonetheless arise through activation of the central nervous system, albeit not engaging cortical structures until after the contraction has occurred.

The chlorarachniophytes are a small group of exclusively marine algae widely distributed in tropical and temperate waters. They are typically mixotrophic, ingesting bacteria and smaller protists as well as conducting photosynthesis. Normally they have the form of small amoebae, with branching cytoplasmic extensions that capture prey and connect the cells together, forming a net. These extensions are dependent on the presence of light and polymerization of the actin cytoskeleton. They may also form flagellate zoospores, which characteristically have a single subapical flagellum that spirals backwards around the cell body, and walled coccoid cells.

The chloroplasts were presumably acquired by ingesting some green alga. They are surrounded by four membranes, the outermost of which is continuous with the endoplasmic reticulum, and contain a small nucleomorph between the middle two, which is a remnant of the alga's nucleus. This contains a small amount of DNA and divides without forming a mitotic spindle. The origin of the chloroplasts from green algae is supported by their pigmentation, which includes chlorophylls a and b, and by genetic similarities. The only other groups of algae that contain nucleomorphs are a few species of dinoflagellates, which also have plastids originating from green algae, and the cryptomonads, which acquired their chloroplasts from a red alga.

Muscle is a specialised soft tissue, one of the four basic types of animal tissues. There are three types of muscle tissues in vertebrates:- skeletal muscle tissue, cardiac muscle tissue, and smooth muscle tissue. Muscle tissue gives skeletal muscles the ability to contract and relax. Muscle tissue contains special contractile proteins called actin and myosin which interact to cause movement. Among many other muscle proteins present are two regulatory proteins, troponin and tropomyosin. Muscle is formed during embryonic development, in a process known as myogenesis.

Skeletal muscle tissue is striated, consisting of elongated, multinucleate muscle cells called muscle fibers, and is responsible for movements of the body. Other tissues in skeletal muscle include tendons and perimysium. Smooth and cardiac muscle contract involuntarily, without conscious intervention. These muscle types may be activated both through the interaction of the central nervous system as well as by innervation from peripheral plexus or endocrine (hormonal) activation. Skeletal muscle only contracts voluntarily, under the influence of the central nervous system. Reflexes are a form of non-conscious activation of skeletal muscles, but nonetheless arise through activation of the central nervous system, albeit not engaging cortical structures until after the contraction has occurred.

Myosins (/ˈmaɪəsɪn, -oʊ-/) are a family of motor proteins (though most often protein complexes) best known for their roles in muscle contraction and in a wide range of other motility processes in eukaryotes. They are ATP-dependent and responsible for actin-based motility.

The first myosin (M2) to be discovered was in 1864 by Wilhelm Kühne. Kühne had extracted a viscous protein from skeletal muscle that he held responsible for keeping the tension state in muscle. He called this protein myosin. The term has been extended to include a group of similar ATPases found in the cells of both striated muscle tissue and smooth muscle tissue.

In hematology, erythrocyte deformability refers to the ability of erythrocytes (red blood cells, RBCs) to change shape under a given level of applied stress without hemolysing (rupturing). This is an important property because erythrocytes must change their shape extensively under the influence of mechanical forces in fluid flow or while passing through microcirculation (see hemodynamics). The extent and geometry of this shape change can be affected by the mechanical properties of the erythrocytes, the magnitude of the applied forces, and the orientation of erythrocytes with the applied forces. Deformability is an intrinsic cellular property of erythrocytes determined by geometric and material properties of the cell membrane, although as with many measurable properties the ambient conditions may also be relevant factors in any given measurement. No other cells of mammalian organisms have deformability comparable with erythrocytes; furthermore, non-mammalian erythrocytes are not deformable to an extent comparable with mammalian erythrocytes. In human RBCs there are structural supports that aid resilience, which include the cytoskeleton: actin and spectrin that are held together by ankyrin.

Intracellular transport is the movement of vesicles and substances within a cell. Intracellular transport is required for maintaining homeostasis within the cell by responding to physiological signals. Proteins synthesized in the cytosol are distributed to their respective organelles, according to their specific amino acid's sorting sequence. Eukaryotic cells transport packets of components to particular intracellular locations by attaching them to molecular motors that haul them along microtubules and actin filaments. Since intracellular transport heavily relies on microtubules for movement, the components of the cytoskeleton play a vital role in trafficking vesicles between organelles and the plasma membrane by providing mechanical support. Through this pathway, it is possible to facilitate the movement of essential molecules such as membrane‐bounded vesicles and organelles, mRNA, and chromosomes.

Intracellular transport is unique to eukaryotic cells because they possess organelles enclosed in membranes that need to be mediated for exchange of cargo to take place. Conversely, in prokaryotic cells, there is no need for this specialized transport mechanism because there are no membranous organelles and compartments to traffic between. Prokaryotes are able to subsist by allowing materials to enter the cell via simple diffusion. Intracellular transport is more specialized than diffusion; it is a multifaceted process which utilizes transport vesicles. Transport vesicles are small structures within the cell consisting of a fluid enclosed by a lipid bilayer that hold cargo. These vesicles will typically execute cargo loading and vesicle budding, vesicle transport, the binding of the vesicle to a target membrane and the fusion of the vesicle membranes to target membrane. To ensure that these vesicles embark in the right direction and to further organize the cell, special motor proteins attach to cargo-filled vesicles and carry them along the cytoskeleton. For example, they have to ensure that lysosomal enzymes are transferred specifically to the golgi apparatus and not to another part of the cell which could lead to deleterious effects.

Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond. By convention, a chain under 30 amino acids is often identified as a peptide, rather than a protein. To be able to perform their biological function, proteins fold into one or more specific spatial conformations driven by a number of non-covalent interactions, such as hydrogen bonding, ionic interactions, Van der Waals forces, and hydrophobic packing. To understand the functions of proteins at a molecular level, it is often necessary to determine their three-dimensional structure. This is the topic of the scientific field of structural biology, which employs techniques such as X-ray crystallography, NMR spectroscopy, cryo-electron microscopy (cryo-EM) and dual polarisation interferometry, to determine the structure of proteins.

Protein structures range in size from tens to several thousand amino acids. By physical size, proteins are classified as nanoparticles, between 1–100 nm. Very large protein complexes can be formed from protein subunits. For example, many thousands of actin molecules assemble into a microfilament.

HeLa (/ˈhiːlɑː/) is an immortalized cell line used in scientific research. It is the oldest human cell line and one of the most commonly used. HeLa cells are durable and prolific, allowing for extensive applications in scientific study. The line is derived from cervical cancer cells taken on February 8, 1951, from Henrietta Lacks, a 31-year-old African American woman, after whom the line is named. Lacks died of cancer on October 4, 1951.

The cells from Lacks's cancerous cervical tumor were taken without her knowledge, which was common practice in the United States at the time. Cell biologist George Otto Gey found that they could be kept alive, and developed a cell line. Previously, cells cultured from other human cells would survive for only a few days, but cells from Lacks's tumor behaved differently.

Myogenesis is the formation of skeletal muscular tissue, particularly during embryonic development.Muscle fibers generally form through the fusion of precursor myoblasts into multinucleated fibers called myotubes. In the early development of an embryo, myoblasts can either proliferate, or differentiate into a myotube. What controls this choice in vivo is generally unclear. If placed in cell culture, most myoblasts will proliferate if enough fibroblast growth factor (FGF) or another growth factor is present in the medium surrounding the cells. When the growth factor runs out, the myoblasts cease division and undergo terminal differentiation into myotubes.

Myoblast differentiation proceeds in stages. The first stage involves cell cycle exit and the commencement of expression of certain genes. The second stage of differentiation involves the alignment of the myoblasts with one another. Studies have shown that even rat and chick myoblasts can recognise and align with one another, suggesting evolutionary conservation of the mechanisms involved. The third stage is the actual cell fusion itself. In this stage, the presence of calcium ions is critical. Fusion in humans is aided by a set of metalloproteinases coded for by the ADAM12 gene, and a variety of other proteins. Fusion involves recruitment of actin to the plasma membrane, followed by close apposition and creation of a pore that subsequently rapidly widens.

Porosomes are cup-shaped supramolecular structures in the cell membranes of eukaryotic cells where secretory vesicles transiently dock in the process of vesicle fusion and secretion. The transient fusion of secretory vesicle membrane at a porosome, base via SNARE proteins, results in the formation of a fusion pore or continuity for the release of intravesicular contents from the cell. After secretion is complete, the fusion pore temporarily formed at the base of the porosome is sealed. Porosomes are few nanometers in size and contain many different types of protein, especially chloride and calcium channels, actin, and SNARE proteins that mediate the docking and fusion of the vesicles with the cell membrane. Once the vesicles have docked with the SNARE proteins, they swell, which increases their internal pressure. They then transiently fuse at the base of the porosome, and these pressurized contents are ejected from the cell. Examination of cells following secretion using electron microscopy, demonstrate increased presence of partially empty vesicles following secretion. This suggested that during the secretory process, only a portion of the vesicular contents are able to exit the cell. This could only be possible if the vesicle were to temporarily establish continuity with the cell plasma membrane, expel a portion of its contents, then detach, reseal, and withdraw into the cytosol (endocytose). In this way, the secretory vesicle could be reused for subsequent rounds of exo-endocytosis, until completely empty of its contents.

Porosomes vary in size depending on the cell type. Porosome in the exocrine pancreas and in endocrine and neuroendocrine cells range from 100 nm to 180 nm in diameter while in neurons they range from 10 nm to 15 nm (about 1/10 the size of pancreatic porosomes). When a secretory vesicle containing v-SNARE docks at the porosome base containing t-SNARE, membrane continuity (ring complex) is formed between the two. The size of the t/v-SNARE complex is directly proportional to the size of the vesicle. These vesicles contain dehydrated proteins (non-active) which are activated once they are hydrated. GTP is required for the transport of water through the water channels or Aquaporins, and ions through ion channels to hydrate the vesicle. Once the vesicle fuses at the porosome base, the contents of the vesicle at high pressure are ejected from the cell.

A myofibril (also known as a muscle fibril or sarcostyle) is a basic rod-like organelle of a muscle cell. Skeletal muscles are composed of long, tubular cells known as muscle fibers, and these cells contain many chains of myofibrils. Each myofibril has a diameter of 1–2 micrometres. They are created during embryonic development in a process known as myogenesis.

Myofibrils are composed of long proteins including actin, myosin, and titin, and other proteins that hold them together. These proteins are organized into thick, thin, and elastic myofilaments, which repeat along the length of the myofibril in sections or units of contraction called sarcomeres. Muscles contract by sliding the thick myosin, and thin actin myofilaments along each other.

A sarcomere (Greek σάρξ sarx "flesh", μέρος meros "part") 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 (called muscle fibers or myofibers) 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.

Two of the important proteins are myosin, which forms the thick filament, and actin, which forms the thin filament. Myosin has a long fibrous tail and a globular head that binds to actin. The myosin head also binds to ATP, which is the source of energy for muscle movement. Myosin can only bind to actin when the binding sites on actin are exposed by calcium ions.