Cell Biology Terms Starting With B
Cell Biology Glossary: B
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Basal Lamina
/ BAY-sul LAM-ih-nuh / · Latin: basalis (base) + lamina (thin plate)
Basal lamina is a thin, specialized sheet of extracellular matrix that underlies epithelial cells, muscle fibers, and blood vessels, anchoring them to surrounding connective tissue and regulating molecular exchange between tissue compartments.
The basal lamina is typically 50 to 100 nanometers thick and contains four major components: type IV collagen, laminin, nidogen, and the heparan sulfate proteoglycan perlecan, which self-assemble into a mesh without requiring a cellular template. Laminin binds integrin receptors on the overlying cell surface, transmitting mechanical signals between the matrix and the cytoskeleton. In kidney glomeruli, the basal lamina between capillary endothelial cells and podocytes filters blood by size and charge, normally excluding proteins larger than about 70 kilodaltons.
During tissue repair and embryonic development, the basal lamina also provides directional cues that guide migrating cells along defined paths.
Certain cancers become invasive when tumor cells secrete matrix metalloproteinases that degrade the basal lamina. Breast cancer cells, for example, must breach the mammary epithelial basal lamina before they can enter blood vessels and metastasize to distant organs.
The basal lamina is a layer of cells. It is a non-cellular protein and carbohydrate matrix secreted by the epithelial and other cells that rest on it.
In the cornea, the epithelial basal lamina is roughly 60 nanometers thick and regenerates within 48 to 72 hours after superficial injury. Migrating epithelial cells use laminin and fibronectin deposited in this layer as a scaffold to resurface the wound before the full matrix is restored.
Urinary System Fun Facts →Beta Catenin
/ BAY-tah KAT-eh-nin / · Greek beta, second; Latin catena, chain
Beta-catenin is a protein that links the cell-adhesion molecule E-cadherin to the actin cytoskeleton at cell-cell contacts and, when released from that complex, travels to the nucleus to activate genes controlling cell growth and differentiation.
Normally, a destruction complex containing the proteins APC, Axin, and GSK-3 beta continuously phosphorylates beta-catenin, marking it for proteasomal degradation within minutes of synthesis. When a Wnt ligand binds its Frizzled receptor, this destruction complex is inactivated, beta-catenin accumulates in the cytoplasm, and the stabilized protein translocates to the nucleus. There it binds TCF/LEF transcription factors and drives expression of proliferation genes including MYC and CCND1.
During vertebrate embryogenesis, this pathway patterns the dorsal-ventral body axis and maintains intestinal stem cell identity throughout adult life.
In colorectal cancer, mutations in the APC gene disrupt the destruction complex, causing beta-catenin to accumulate and drive uncontrolled cell division. More than 80 percent of colorectal tumors carry loss-of-function APC mutations, making this one of the most frequently disrupted signaling nodes in human cancer.
Beta-catenin is only a structural junction protein. When regulated by Wnt pathways, it can enter the nucleus and affect gene expression.
In the zebrafish (Danio rerio) embryo, maternal beta-catenin protein accumulates on the dorsal side within the first 30 minutes after fertilization, before any zygotic transcription begins. This early asymmetry is sufficient to specify the entire dorsal body axis, demonstrating that a single protein's localization can determine the fundamental orientation of a vertebrate body plan.
Bile Canaliculus
/ BYL kan-ah-LIK-yoo-lus / · Old English bile; Latin canaliculus, small channel
Bile canaliculus is a narrow intercellular channel formed between adjacent hepatocytes that collects bile secreted by those cells and carries it toward larger bile ducts.
Each bile canaliculus forms at the apical membranes of two neighboring hepatocytes and measures approximately 1 micrometer in diameter. Microvilli projecting from those apical surfaces increase the membrane area available for bile salt secretion into the channel. Tight junctions composed of claudin and occludin proteins seal the canalicular space from the blood sinusoid, preventing bile from leaking into the circulation.
Bile flows through the canalicular network toward the canals of Hering and then into interlobular bile ducts at the portal triad of each liver lobule.
Bile canaliculi lack their own walls; the channel is bounded entirely by the plasma membranes of two hepatocytes. If tight junctions between those cells are disrupted, as occurs in cholestatic liver disease, bile acids leak into the bloodstream and cause jaundice and tissue damage.
Fun Facts About Digestive System →Bile canaliculi are not capillaries and do not carry blood. They are sealed intercellular spaces between hepatocytes dedicated exclusively to bile collection and transport.
Circulatory System Fun Facts →In the human liver, each hepatocyte borders multiple bile canaliculi simultaneously, so a single cell contributes to several parallel drainage channels at once. Bile secretion into these channels is driven by ATP-dependent transporters, including the bile salt export pump (BSEP), and the entire canalicular network can drain roughly 600 to 1000 milliliters of bile per day in a healthy adult.
Brush Border
/ brush BOR-der / · English: brush + border
Brush border is a dense array of microvilli on the apical surface of absorptive epithelial cells that dramatically expands the membrane area available for nutrient uptake and digestion.
Each microvillus in the brush border measures roughly 1 micrometer long and 0.1 micrometers wide, and a single human intestinal enterocyte carries approximately 1,000 to 3,000 of them, increasing functional surface area up to 25-fold compared to a flat membrane. Actin filaments bundled by villin and fimbrin proteins form the structural core of each microvillus and anchor it to the terminal web beneath the apical membrane. Digestive enzymes including lactase, sucrase, and aminopeptidase are embedded directly in the brush border membrane, coupling final hydrolysis of nutrients to their immediate transport into the cell.
Celiac disease and rotavirus infection both damage the brush border, flattening microvilli and reducing absorptive capacity, which leads to malabsorption and diarrhea.
The brush border of the small intestine is coated by a carbohydrate-rich layer called the glycocalyx, which traps digestive enzymes near the membrane surface and protects epithelial cells from self-digestion by pancreatic proteases. This glycocalyx can extend up to 0.5 micrometers above the microvillus tips.
Brush borders are made of cilia that beat to move material. Microvilli are non-motile, actin-supported projections that increase surface area; they do not beat or generate directional flow.
Plasma Membrane Functions →Proximal tubule cells in the kidney bear a brush border that recovers filtered glucose, amino acids, and small proteins from the glomerular filtrate. Each day, these cells reclaim nearly all of the approximately 180 liters of filtrate the kidneys process, preventing the loss of nutrients that would otherwise appear in urine.
Are Enzymes Proteins? →Budding
/ BUD-ing / · Old English: budda (rounded lump)
Budding is an asexual reproductive process in which a new cell or organism develops as a small outgrowth on the parent, then separates to live independently.
In the baker’s yeast Saccharomyces cerevisiae, a bud emerges at a genetically determined site on the mother cell surface, grows by localized insertion of new membrane and cell wall material, and reaches roughly 30 percent of the mother cell’s volume before cytokinesis severs the connection. The bud site is marked by a ring of septin proteins that recruit the machinery for polarized growth. Mitochondria, ribosomes, and other organelles are actively transported into the bud before separation, so the daughter cell is fully equipped to survive independently.
Multicellular animals including hydra (Hydra vulgaris) also reproduce by budding, producing tentacled outgrowths that detach as complete juvenile organisms.
Budding in yeast is not random. The mother cell remembers where it last budded: haploid cells bud from an axial site adjacent to the previous division scar, while diploid cells alternate between the two poles of the cell, a difference controlled by distinct sets of landmark proteins.
Budding is the same as splitting exactly in half. Budding produces two unequal cells, whereas binary fission typically generates two cells of similar size.
Candida albicans, the fungus responsible for thrush and systemic candidiasis, switches between budding and filamentous growth depending on environmental conditions. At 37 degrees Celsius in the presence of serum, budding cells transition to hyphal growth within about 90 minutes, and this morphological switch is directly linked to the organism's ability to invade host tissue.
Yeast →