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Duodenum with brush border of microvilli.
Illustration of the brush border membrane of small intestinal villi

A brush border (striated border or brush border membrane) 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;[1] 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.

Brush border cells are found mainly in the following organs:

  • The small intestine tract: This is where absorption takes place.[2][3][4] The brush borders of the intestinal lining are the site of terminal carbohydrate digestions. The microvilli that constitute the brush border have enzymes for this final part of digestion anchored into their apical plasma membrane as integral membrane proteins. These enzymes are found near to the transporters that will then allow absorption of the digested nutrients.
  • The kidney: Here the brush border is useful in distinguishing the proximal tubule (which possesses the brush border) from the distal convoluted tubule (which does not).[5][6]
  • The large intestine also has microvilli on the surface of its enterocytes.

The brush border morphology increases a cell's surface area, a trait which is especially useful in absorptive cells. Cells that absorb substances need a large surface area in contact with the substance to be efficient.[7]

In intestinal cells, the microvilli are referred to as brush border and are protoplasmic extensions contrary to villi which are submucosal folds, while in the kidneys, microvilli are referred to as striated border.[8]

See also

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References

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Brush border

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from Grokipedia
The brush border is a specialized consisting of a dense covering of microvilli on the apical surface of epithelial cells in absorptive tissues, including the , , and , where the microvilli dramatically increase the cell's surface area to facilitate absorption and . These microvilli are uniform, finger-like projections approximately 100 nm in diameter and 1–3 µm in length, supported by parallel bundles of 30–40 filaments cross-linked by bundling proteins such as villin, espin, and fimbrin. The brush border's plasma membrane is enriched with , transporters, and channels, enabling efficient nutrient uptake while forming a physical barrier against pathogens and luminal contents. In the , the brush border is particularly prominent on enterocytes, where it amplifies the absorptive surface area by 9- to 16-fold, playing a central role in the terminal and absorption of carbohydrates, proteins, and through membrane-bound hydrolases like sucrase-isomaltase and aminopeptidases. Beyond absorption, it contributes to host defense by restricting microbial access and supporting interactions with the , with its structural integrity maintained by anchoring to the underlying terminal web via myosin-1a, ezrin, and protocadherin-based intercellular adhesions. In the , the brush border on cells similarly enhances of ions, water, and solutes, and may serve mechanosensory functions in response to fluid flow. Assembly of the brush border involves polymerization at microvillar tips, regulated by proteins like EPS8 and motors, ensuring the hexagonal packing essential for its function.

Structure

Microvilli Organization

Microvilli are finger-like projections extending from the apical surface of epithelial cells, forming the brush border, and typically measure 1-2 μm in length and 0.1 μm in diameter. These microvilli are arranged in a densely packed on the cell surface, optimizing space utilization with thousands per cell. This organization dramatically expands the apical surface area, providing a 9- to 16-fold increase relative to a flat epithelial surface. At their core, microvilli contain parallel bundles of 20-40 filaments, arranged in a hexagonal array with barbed ends oriented toward the distal tip. These filaments are cross-linked and bundled primarily by fimbrin and villin, which saturate the bundle to maintain rigidity and a uniform diameter of about 50-100 nm, while anchoring mechanisms the bundle to the plasma membrane. Beneath the microvilli lies the terminal web, a dense actin-myosin network that embeds the pointed ends of the actin filaments and provides mechanical support to the entire brush border structure. This region ensures stability by linking the microvillar cores to the underlying .

Cytoskeletal and Membrane Components

The plasma membrane of the brush border features specialized lipid rafts, which are cholesterol- and sphingolipid-enriched microdomains that facilitate compartmentalization and organization of membrane proteins. These rafts contribute to the structural integrity and functional segregation within the microvillar membrane, supporting processes like nutrient transport. Actin bundles within microvilli are stabilized by cross-linking proteins such as espin and plastin, which rigidify the core to maintain the protrusions' shape and length. Espin, a high-affinity actin-bundling protein, cross-links parallel actin filaments, while plastin (also known as fimbrin or I-plastin) similarly bundles F-actin to provide mechanical support in the brush border. These proteins work alongside others like villin to ensure the dense packing and stability of the cytoskeletal framework. Spacing between microvilli is maintained through inter-microvillar adhesions mediated by protocadherin-24 (PCDH24) and mucin-like glycoproteins, which form calcium-dependent links at microvillar tips to prevent fusion and promote uniform packing. PCDH24 interacts with mucin-like protocadherin to create these adhesion complexes, essential for brush border assembly and organization. The brush border is coated by a , a carbohydrate-rich layer approximately 1 μm thick, composed primarily of glycoproteins and glycolipids that form a protective barrier against luminal contents. This layer, anchored to the microvillar membrane, includes highly glycosylated transmembrane mucins and glycolipids that contribute to its mesh-like structure and barrier properties.

Locations

Intestinal Epithelium

The brush border is primarily located on the apical surface of enterocytes, the predominant epithelial cells lining the , where it faces the intestinal lumen to facilitate direct interaction with luminal contents. This structure is especially prevalent in the proximal regions, including the and , which are optimized for the initial phases of nutrient processing and uptake following gastric and pancreatic . Each features approximately 3,000 densely packed microvilli that form the brush border, arranged in a to maximize coverage. These microvilli collectively contribute the majority of the small intestine's absorptive surface area, with amplification factors from the brush border alone estimated at 20- to 30-fold, resulting in a total intestinal surface area of around 200-300 m² in humans when accounting for all structural enhancements. Adaptations in the intestinal brush border support high-volume uptake, including microvilli lengths of up to 2.5-3 μm, which are longer than in other epithelial sites to enhance exposure to digestive contents. This configuration allows for efficient post-digestion absorption in the -rich environment of the . The structure is evolutionarily conserved across mammals, reflecting its essential role in optimizing dietary energy extraction. In addition to absorption, the brush border provides a protective barrier against intestinal pathogens.

Renal Epithelium

The brush border is prominently featured on the apical surface of in the proximal convoluted tubule of the , where it plays a crucial role in the of filtered substances from the glomerular filtrate. This structure facilitates the recovery of approximately 70% of the filtered , along with a substantial portion of ions such as sodium and , and organic solutes like glucose and , through enhanced surface area and integrated transport mechanisms. The proximal tubule's brush border thus serves as the primary site for bulk , maintaining fluid and by preventing excessive loss in . In contrast to the intestinal brush border, the renal version consists of shorter microvilli, typically measuring about 1 μm in length, which form a less densely packed array optimized for efficient solute recovery from the protein-poor glomerular filtrate rather than high-volume nutrient absorption from digesta. This adaptation allows for rapid and across a surface area expanded by roughly 20- to 40-fold compared to a flat , supporting the kidney's high-capacity demands without the need for the tighter hexagonal packing seen in enterocytes. The renal brush border is closely integrated with an endocytic apparatus, featuring clathrin-coated pits concentrated at the base of the microvilli to enable receptor-mediated uptake of low-molecular-weight proteins such as that escape glomerular . These pits invaginate to form vesicles that traffic filtered proteins to lysosomes for degradation, preventing tubular overload and contributing to the clearance of up to 99.9% of filtered under normal conditions. This endocytic process is particularly active in the S1 and S2 segments of the , where the brush border's structural features support both reabsorptive and degradative functions. Adaptations for pH-dependent transport are evident in the distribution of the vacuolar () along the renal border, where this is inserted into the apical membrane to drive H+ and facilitate the reabsorption of and other buffers. The 's activity is regulated by factors such as and luminal flow, enabling dynamic adjustments to acid-base balance; for instance, it energizes secondary of organics and ions via gradients across the microvillar membrane. This localization ensures that proton extrusion supports the proximal tubule's role in reclaiming over two-thirds of filtered , underscoring the border's specialization for renal acid-base .

Choroid Plexus

The brush border is also present on the apical surface of epithelial cells in the , a vascularized structure within the 's ventricles. Here, the microvilli project into the (CSF)-filled ventricular lumen, significantly increasing the surface area to facilitate the secretion of CSF and the exchange of ions, nutrients, and waste products between blood and CSF. This adaptation supports the choroid plexus's primary function in producing approximately 500 mL of CSF per day in adults, maintaining and forming part of the blood-CSF barrier. The brush border in this location features numerous transporters and enzymes, enabling processes essential for CSF composition and .

Functions

Nutrient Absorption

The brush border in the dramatically amplifies the absorptive surface area through its dense array of microvilli, enabling efficient uptake of nutrients from the lumen via both and mechanisms. This structural adaptation increases the effective surface area of the villi by approximately 20-fold, facilitating the contact of luminal contents with membrane-bound transporters and channels. Active transport across the brush border membrane is mediated by specialized apical transporters, such as the sodium-glucose linked transporter 1 (SGLT1), which co-transports and with sodium ions using the established by the Na+/K+-ATPase on the basolateral membrane. Similarly, the proton-coupled transporter 1 (PEPT1) facilitates the uptake of di- and tripeptides from protein products, driven by a proton , primarily in the and proximal . These transporters ensure high-affinity absorption even at low luminal concentrations, preventing nutrient loss in feces. Nutrient absorption occurs via two primary pathways: transcellular, which predominates for most solutes and involves or carrier-mediated through the , and paracellular, a passive route through tight junctions that primarily handles small ions and but is tightly regulated to maintain barrier integrity. Tight junctions, located at the apex of the lateral membranes between enterocytes, selectively permit paracellular flux of ions like sodium and , complementing apical uptake while preventing unregulated leakage of larger molecules. This dual-pathway system optimizes overall absorption efficiency in the . The brush border also plays a critical role in the absorption of vitamins and minerals, exemplified by (cobalamin), which binds to in the and is subsequently recognized by specific receptors on the microvilli of ileal enterocytes for . Minerals such as calcium and iron are similarly absorbed via brush border transporters like TRPV6 and DMT1, respectively, often coupled with or ascorbic acid for enhanced uptake. These processes ensure essential . In humans, the brush border-mediated mechanisms are responsible for absorbing the majority of dietary carbohydrates, approximately equivalent to 200-300 grams of glucose per day on a typical diet, underscoring their quantitative impact on and metabolic regulation. In the renal , the brush border enhances reabsorption of ions, water, glucose, , and other solutes from the glomerular filtrate, utilizing similar apical transporters like SGLT2 for glucose, contributing to maintaining bodily and potentially serving mechanosensory functions in response to tubular fluid flow.

Digestive Enzyme Activity

The brush border of the small hosts a suite of integral membrane hydrolases that perform the terminal stages of nutrient , converting complex carbohydrates, peptides, and certain lipid-associated substrates into absorbable monomers through luminal at the apical surface. These enzymes are embedded within the plasma membrane of enterocytes, positioned to generate high local concentrations of products immediately adjacent to absorption sites, thereby facilitating efficient uptake. This process ensures that the majority of dietary starches and disaccharides undergo final breakdown here, following partial by pancreatic and salivary enzymes. For carbohydrate digestion, sucrase-isomaltase serves as a key bifunctional enzyme, with its sucrase domain hydrolyzing into glucose and , while the isomaltase domain cleaves α-1,6-glycosidic bonds in and limit dextrins derived from . Similarly, maltase-glucoamylase hydrolyzes and other α-1,4-linked oligosaccharides into glucose units, completing the conversion of breakdown products from pancreatic α-amylase. These actions yield monosaccharides in the intestinal lumen for direct absorption. In protein digestion, aminopeptidases, such as aminopeptidase N and aminopeptidase A, act on the N-terminal ends of peptides, sequentially releasing free or smaller di- and tripeptides from oligopeptides generated by pancreatic proteases. This exopeptidase activity ensures the final liberation of absorbable and peptides, with diverse isoforms targeting specific residues like acidic or proline-linked sequences. For lipid-related substrates, , an ectoenzyme anchored in the brush border membrane, hydrolyzes phosphate esters, including those from and phospholipids like , contributing to the processing of dietary phospholipids and phosphoproteins. While bulk digestion occurs via pancreatic , this enzyme supports the steps necessary for lipid derivative absorption. The activity of these enzymes is regulated by substrate availability, with expression and function upregulated by dietary carbohydrates for sucrase-isomaltase and by proteins for aminopeptidases, ensuring adaptive responses to nutrient intake. Optimal in the alkaline range (around 7-8) enhances catalytic efficiency, particularly for , while embedding within the provides a structured microenvironment that promotes substrate-enzyme proximity and protects against luminal dilution, optimizing kinetics for .

Molecular Composition

Key Proteins

The brush border's structural integrity relies on a core bundle of actin filaments within each microvillus, which provides the foundational scaffold for protrusion formation and maintenance. Villin, an actin-bundling and severing protein, plays a pivotal role in organizing these parallel actin filaments into rigid bundles while also enabling dynamic remodeling through its severing activity. Myosin-1a, a class I myosin motor protein, contributes to actin bundle tension and facilitates attachment of the plasma membrane to the cytoskeleton, ensuring proper microvillar shape and membrane sliding along the actin core. Transport proteins embedded in the brush border are essential for nutrient uptake and . Sodium-glucose 1 (SGLT1) mediates the coupled transport of sodium and glucose across the apical , driving glucose absorption into enterocytes. Facilitative glucose 2 (GLUT2) supports the efflux of glucose from the cell, often recruited to the brush border under high luminal glucose conditions to enhance absorption efficiency. The sodium-hydrogen exchanger 3 (NHE3) regulates pH by exchanging sodium for protons on the brush border, contributing to sodium absorption and . Adhesion and scaffolding proteins link the to the and stabilize microvillar arrays. Ezrin, a member of the ezrin-radixin-moesin family, cross-links filaments to the plasma , promoting microvillar elongation and organization through its conformational activation. Protein interactions are critical for brush border stability, with disruptions leading to architectural defects. Mutations in Myosin-1a impair bundle integrity and association, resulting in disorganized microvilli, loss of core components, and overall structural instability in enterocytes.

Lipid and Glycocalyx Elements

The brush border exhibits specialized compositions that contribute to its structural and functional integrity. It is particularly enriched in glycosphingolipids, such as globotriaosylceramide and lactosylceramide, alongside high levels of , which together promote the formation of lipid rafts or microdomains. These microdomains facilitate the lateral segregation and clustering of enzymes and transporters, enhancing their in localized processes. Additionally, glycosylphosphatidylinositol (GPI)-anchored proteins, which are tethered to the via these s, are abundantly present in the brush border, further stabilizing these detergent-resistant domains in both intestinal and renal epithelia. Overlying the is the , a carbohydrate-rich coating that imparts unique biophysical properties to the brush border. This layer primarily consists of core glycoproteins, including mucin-like proteins such as MUC17 and that bind carbohydrates, forming a filamentous network. Prominent among its components are residues, which terminate many chains and confer a net negative charge to the , while also contributing to its viscous, gel-like consistency. This sialylation pattern not only increases the hydrodynamic volume but also modulates interactions with the luminal environment. The plays a critical protective by trapping near the membrane surface, thereby localizing their activity and preventing diffusion into the lumen. Furthermore, its negatively charged sialic acids generate electrostatic repulsion that inhibits microbial , acting as a selective barrier against bacterial pathogens while allowing passage. This mechanism complements the physical hindrance provided by the dense carbohydrate matrix, reducing the risk of in the intestinal and renal environments. Biogenesis of the brush border involves post-translational modifications primarily in the Golgi apparatus, where glycosyltransferases add complex chains to core proteins and after their insertion into microvilli membranes. These enzymes, including sialyltransferases, sequentially elongate glycan structures in the trans-Golgi network before vesicular transport delivers the assembled components to the apical surface. This process ensures the matures concurrently with microvillar elongation, maintaining its protective attributes.

Development and Regulation

Formation in Epithelial Cells

The formation of the brush border in epithelial cells initiates during the differentiation of enterocyte precursors, which originate from stem cells in the intestinal crypts and migrate upward along the crypt-villus axis toward the villus tip. This migration, spanning approximately 3-5 days in mice, coincides with the progressive maturation of these cells into functional enterocytes, where the apical surface remodels to generate microvilli. Nascent microvilli first emerge as a sparse of short protrusions at the crypt-villus transition zone, typically within 24-48 hours post-differentiation in cellular models of epithelial maturation. Microvillar assembly involves actin nucleators identified in proteomic studies of brush borders, including the and formins such as cordon-bleu (COBL) and diaphanous-related formin 1, for generating initial protrusions and linear filament elongation. COBL, an actin nucleator with WH2 domains, drives the of parallel actin filaments from their barbed ends at the microvillar tips, enabling elongation while regulates G-actin allocation to sustain growth. Bundling proteins like villin then these filaments into rigid cores, stabilizing the protrusions as they lengthen to 1-3 µm. Actin , with assembly at distal tips and disassembly proximally, powers the motility of individual microvilli, facilitating their clustering through Ca²⁺-dependent adhesion via protocadherins like CDHR2. Apical-basal polarity is established concurrently, directing brush border components to the apical domain through Rab11-positive endosomes that traffic proteins and via vesicles along tracks. This targeted delivery ensures the selective accumulation of apical , such as enzymes and transporters, preventing mislocalization and supporting ordered microvillar packing. In embryonic development, brush border maturation occurs late in , with transcriptional regulation by factors like CDX2 activating genes for apical structures (e.g., ALPI) after embryonic day 14.5 in mice, leading to full assembly by approximately postnatal day 5 as crypt-villus architecture solidifies. CDX2 binds dynamically to enhancers, promoting chromatin accessibility for enterocyte-specific programs that culminate in a dense, functional brush border array.

Maintenance Mechanisms

The maintenance of the brush border in intestinal and renal epithelial cells relies on dynamic cytoskeletal remodeling driven by treadmilling and motor activity, ensuring constant renewal of microvilli structures. Actin polymerization at the tips of microvilli, facilitated by formins, drives elongation, while depolymerization at the base via ADF/cofilin maintains turnover; motors, including non-muscle myosin IIA, generate contractile forces that regulate microvillar height and spacing, preventing collapse under physiological stresses. This process results in a short for microvilli components, approximately 1-2 days, allowing rapid to environmental changes such as flux or mechanical shear. Endocytic recycling pathways play a crucial role in removing damaged or aged elements from the brush border while inserting newly synthesized components to sustain integrity. Predominantly clathrin-independent mechanisms, such as caveolin-mediated and macropinocytosis, facilitate the internalization of apical membrane proteins like and sucrase-isomaltase, followed by sorting in early endosomes for recycling back to the plasma membrane or degradation in lysosomes if irreparably damaged. This selective turnover prevents accumulation of dysfunctional elements, maintaining enzymatic and , with studies showing that inhibition of these pathways leads to brush border disassembly within hours. Calcium signaling modulates brush border stiffness through interactions between calmodulin and myosin motors, enabling adaptive responses to shear stress from luminal flow. Elevated intracellular Ca²⁺ levels activate , which binds to (MLCK), phosphorylating regulatory light chains and enhancing actomyosin contractility; this stiffens the brush border to withstand hydrodynamic forces, as demonstrated in renal cells where Ca²⁺ transients correlate with increased microvillar rigidity. Such mechanosensitive adjustments are vital for preventing erosion in high-flow environments like the . Feedback loops involving nutrient sensing through the pathway upregulate brush border biogenesis during periods of high demand, linking metabolic status to structural maintenance. Activation of by like stimulates protein synthesis of core microvillar components, such as villin and ezrin, via of downstream targets like S6K1; this enhances assembly and membrane insertion, with experimental models showing mTOR inhibition impairs brush border density under nutrient-replete conditions. This regulatory mechanism ensures the brush border scales with absorptive workload, promoting in fed states.

Pathophysiology

Associated Disorders

Microvillus inclusion disease (MVID) is a rare congenital enteropathy characterized by severe dysfunction of the intestinal brush border, primarily due to mutations in the MYO5B gene, which encodes myosin Vb, a essential for apical trafficking and microvilli organization in enterocytes. These mutations lead to the internalization of microvilli into intracellular inclusions, resulting in loss of brush border structure, impaired nutrient absorption, and life-threatening secretory that manifests in infancy, often requiring total parenteral nutrition. The disease has an estimated prevalence of fewer than 1 in 1,000,000 births, with fewer than 200 cases reported worldwide, reported worldwide across diverse populations, with clusters noted in groups such as Native Americans and Mediterranean regions. Congenital sucrase-isomaltase deficiency (CSID) is an autosomal recessive disorder caused by mutations in the SI gene, leading to absent or reduced activity of the brush border enzyme , impairing the digestion of and starches. This results in osmotic , , and upon ingestion of sucrose-containing foods, typically presenting in infancy or . In celiac disease, an autoimmune disorder triggered by ingestion in genetically susceptible individuals, the brush border undergoes significant atrophy and villus blunting in the , leading to reduced activity of such as and sucrase-isomaltase, which impairs and absorption. This -induced damage involves T-cell mediated inflammation that flattens the villi and disrupts the epithelial barrier, contributing to symptoms like , , and nutritional deficiencies. Globally, celiac disease affects approximately 1.4% of the population, with brush border integrity and activities recovering upon adherence to a strict . Enteropathogenic (EPEC) infections cause acute brush border disruption through attaching-and-effacing (A/E) lesions, where the bacterial injects the translocated intimin receptor (Tir) protein into host enterocytes, recruiting host to form pedestals while effacing microvilli and altering the brush border architecture. This Tir-mediated polymerization and cytoskeletal rearrangement inhibit normal and absorption, leading to watery , particularly in children in developing regions. The effacement process directly contributes to the pathogen's intimate adherence and , exacerbating fluid secretion and mucosal . In the , anti-brush border (ABBA) disease, also known as anti- nephropathy, is a rare autoimmune disorder where autoantibodies target the low-density lipoprotein receptor-related protein 2 (/megalin) on the brush border, causing tubulointerstitial , tubular dysfunction, and progressive . Fanconi syndrome, often secondary to genetic or acquired causes, involves generalized dysfunction including brush border defects, leading to impaired of glucose, , , and , resulting in and .

Therapeutic and Diagnostic Approaches

Diagnostic approaches to brush border dysfunction primarily involve histopathological examination of intestinal biopsies to assess microvilli integrity and activity. Electron microscopy serves as the gold standard for confirming microvillus inclusion disease (MVID), revealing characteristic intracytoplasmic inclusions lined by intact microvilli within surface enterocytes, which are absent or rudimentary on the apical surface. Biopsy-based disaccharidase assays, performed on duodenal tissue obtained via , quantitatively measure levels such as sucrase and isomaltase to diagnose deficiencies, providing the definitive evaluation for conditions like congenital sucrase-isomaltase deficiency. Advanced imaging techniques enhance visualization of brush border components in both diagnostic and research contexts. , often employing staining to label F-actin filaments, allows detailed assessment of microvillar architecture and cytoskeletal organization in epithelial cells, aiding in the identification of structural abnormalities. Non-invasive breath tests, such as breath tests following or ingestion, detect due to brush border deficiencies by measuring elevated exhaled from undigested carbohydrates fermented by . Therapeutic strategies for brush border impairments focus on symptom management and nutritional support, tailored to the underlying condition. For sucrase-isomaltase deficiency, enzyme replacement therapy with sacrosidase (Sucraid), an oral solution derived from , effectively hydrolyzes and , alleviating gastrointestinal symptoms when administered with meals. In MVID, total provides essential nutrients intravenously to circumvent severe , serving as a lifelong supportive measure while awaiting potential transplantation. Anti-tumor factor (TNF) agents, such as , are employed in inflammatory bowel diseases where mucosal disrupts brush border function, promoting epithelial repair and reducing cytokine-driven damage to the intestinal barrier. Emerging therapies aim to address root causes of brush border defects through targeted interventions. As of 2025, ongoing Phase 2 clinical trials are evaluating crofelemer, an antisecretory agent, for reducing dependence in pediatric MVID patients, with proof-of-concept studies showing up to 27% reduction in support needs. Similarly, Shylicine™, a novel agent targeting in MVID, is in Phase 2 trials. Preclinical models of MVID have explored approaches to restore MYO5B function, with studies using intestinal organoids demonstrating potential for correcting apical trafficking defects and improving microvillar formation. supplementation, particularly with strains like , shows promise in modulating microbiota-brush border interactions by enhancing activity and barrier integrity, potentially mitigating in dysbiotic states.

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