Mucins
Gastric Mucins
Mucin-5B
Mucin-1
Mucin-4
Mucin-3
Goblet Cells
Mucus
Glycosylation
Antigens, Tumor-Associated, Carbohydrate
Oligosaccharides
Trachea
Periodic Acid-Schiff Reaction
Carbohydrates
Intestinal Mucosa
Carbohydrate Sequence
Mucin expression and function in the female reproductive tract. (1/1160)
Reproductive tract epithelia are characterized by the presence of a thick, apical glycocalyx. This glycoprotein coat is drastically reduced in the uterus of many species during the time of embryo implantation. Recent studies indicate that mucin glycoproteins constitute a large proportion of the apical glycocalyx. One of these mucins, Muc-1, has particularly important functions at the luminal surface of the uterus and other female reproductive tract tissues. Muc-1 appears to play a dominant role in maintaining a functionally non-receptive uterine surface with regard to blastocyst attachment. Conversion to a receptive uterine state is brought about by the concerted actions of ovarian steroid hormones that in several species also strongly modulate Muc-1 protein and mRNA expression. Muc-1 also appears to serve a general function in protecting reproductive tract mucosa since Muc-1 null mice are particularly prone to bacterial infection. Collectively, these studies indicate that mucins, including Muc-1, play important barrier roles in reproductive processes and protection from bacterial pathogenesis in the female reproductive tract. (+info)Intestinal metaplasia of human stomach displays distinct patterns of mucin (MUC1, MUC2, MUC5AC, and MUC6) expression. (2/1160)
Intestinal metaplasia is a well-established premalignant condition of the stomach that is characterized by mucin carbohydrate modifications defined by histochemical methods. The purpose of the present study was to see whether the expression of mucin core proteins was modified in the different types of intestinal metaplasia and to evaluate the putative usefulness of mucins as "molecular markers" in this setting. We used a panel of monoclonal antibodies with well-defined specificities to MUC1, MUC2, MUC5AC, and MUC6 to characterize the expression pattern of mucins. In contrast to normal gastric mucosa, the complete form or type I intestinal metaplasia (n = 20) displayed little or no expression of MUC1, MUC5AC, or MUC6 in the metaplastic cells and strong expression of the intestinal mucin MUC2 in the goblet cells of all cases. The incomplete forms of intestinal metaplasia, type II (n = 25) and type III (n = 16), expressed MUC1 and MUC5AC in every case, both in goblet and in columnar cells. MUC6 was also expressed in 16 cases of type II intestinal metaplasia and in 11 cases of type III intestinal metaplasia. The intestinal mucin MUC2 was expressed in every case of incomplete intestinal metaplasia, mostly in goblet cells. The mucin expression profile in the different types of intestinal metaplasia allows the identification of two patterns: one defined by decreased levels of expression of "gastric" mucins (MUC1, MUC5AC, and MUC6) and expression of MUC2 intestinal mucin, which corresponds to type I intestinal metaplasia, and the other defined by coexpression of "gastric mucins" (MUC1, MUC5AC, and MUC6) together with the MUC2 mucin, encompassing types II and III intestinal metaplasia. Our results challenge the classical sequential pathway of intestinal metaplasia (from type I to type III via a type II intermediate step). (+info)Human colon adenocarcinomas express a MUC1-associated novel carbohydrate epitope on core mucin glycans defined by a monoclonal antibody (A10) raised against murine Ehrlich tumor cells. (3/1160)
A monoclonal antibody (mAb; A10) raised against murine Ehrlich tumor cell surface carbohydrates was tested for reactivity with human normal and malignant tissues. A10 reacted strongly, with a high proportion of adenocarcinomas arising from colon and other tissues but not with breast carcinomas or other malignant tumors. Normal tissues were virtually A10 unreactive, except for the duct cells from breast and pancreas and some bronchial mucosae. Ultrastructural studies showed mAb A10 immunolabeling of both microvilli and mucin droplets in colon cancer cells but not in normal absorptive or globet cells. A10 reacted strongly with mucin-enriched fractions from colon cancer tissues and HT-29 xenografts but not from normal colon tissues. A10 epitope was carried on MUC1 derived from colon adenocarcinomas and probably on other mucin species, although not on MUC2 molecules. A10 epitope was resistant to exoglycosidases and periodate oxidation but sensitive to the Smith's degradation and beta-elimination, suggesting the involvement of O-linked carbohydrates in nonterminal reducing positions. A mucin-type glycosidic linkage was supported because of the lack of A10 reactivity with HT-29 cells grown with phenyl-N-acetyl-alpha-D-galactosaminide. Deglycosylation studies with trifluoromethanesulfonic acid pointed to the involvement of core mucin glycans in the A10 epitope. This epitope was resistant to protease, O- and N-glycanase treatments carried out on trifluoromethanesulfonic acid-deglycosylated mucins. Inhibition studies with core 1, core 2, core 3, and core 6 suggested the latter [GlcNAcbeta(1-6)GalNAc] as being involved in A10 epitope. Taken together, the present results point to A10 defining a core 6-related epitope on core mucin glycans expressed by colon cancer MUC1 not previously associated with human cancer. (+info)CFTR expression does not influence glycosylation of an epitope-tagged MUC1 mucin in colon carcinoma cell lines. (4/1160)
The cause of the mucus clearance problems associated with cystic fibrosis remains poorly understood though it has been suggested that mucin hypersecretion, dehydration of mucins, and biochemical abnormalities in the glycosylation of mucins may be responsible. Since the biochemical and biophysical properties of a mucin are dependent on O-glycosylation, our aim was to evaluate the O-glycosylation of a single mucin gene product in matched pairs of cells that differed with respect to CFTR expression. An epitope-tagged MUC1 mucin cDNA (MUC1F) was used to detect variation in mucin glycosylation in stably transfected colon carcinoma cell lines HT29 and Caco2. The glycosylation of MUC1F mucin was evaluated in matched pairs of Caco2 cell lines that either express wild-type CFTR or have spontaneously lost CFTR expression. The general glycosylation pattern of MUC1F was evaluated by determining its reactivity with a series of monoclonal antibodies against known blood group and tumor-associated carbohydrate antigens. Metabolic labeling experiments were used to estimate the gross levels of glycosylation and sulfation of MUC1F mucin in these matched pairs of cell lines. Expression of CFTR in this experimental system did not affect the gross levels of glycosylation or sulfation of the MUC1F mucin nor the types of carbohydrates structures attached to the MUC1F protein. (+info)Fluctuations in CA 125 and CA 15-3 serum concentrations during spontaneous ovulatory cycles. (5/1160)
The aim of this study was to investigate cycle dependent changes of serum CA 125 and CA 15-3 concentrations during spontaneous ovulatory cycles. Twenty apparently healthy women with spontaneous menstrual cycles attending our infertility clinic were included. Of these women, 18 had occluded tubes as a result of sterilization. Ovulation was confirmed by luteinizing hormone test and ultrasonography and, to exclude endometriosis, a laparoscopy was performed. Serum samples for CA 125, CA 15-3, 17 beta-oestradiol and progesterone determinations were taken every second day starting on the 2nd day of the cycle until the 7th day of the next cycle. After correction for inter-individual variation in serum concentrations, highest CA 125 concentrations were found during the menstruation. During the follicular and peri-ovulatory phase CA 125 serum concentrations were lowest. For CA 15-3, serum concentrations were not statistically different throughout the cycle. CA 125 and oestradiol concentrations were negatively correlated, CA 15-3 and oestradiol concentrations were positively correlated. Absolute serum concentrations of both CA 125 and CA 15-3 vary among females. Within the female, fluctuations of CA 125 are phase related. In the population studied most of the patients had tubal obstruction and high CA 125 serum concentrations during menstruation, which revokes the theory that the menstrual rise of CA 125 is due only to retrograde menstruation. (+info)Dynamic epigenetic regulation of initial O-glycosylation by UDP-N-Acetylgalactosamine:Peptide N-acetylgalactosaminyltransferases. site-specific glycosylation of MUC1 repeat peptide influences the substrate qualities at adjacent or distant Ser/Thr positions. (6/1160)
In search of possible epigenetic regulatory mechanisms ruling the initiation of O-glycosylation by polypeptide:N-acetylgalactosaminyltransferases, we studied the influences of mono- and disaccharide substituents of glycopeptide substrates on the site-specific in vitro addition of N-acetylgalactosamine (GalNAc) residues by recombinant GalNAc-Ts (rGalNAc-T1, -T2, and -T3). The substrates were 20-mers (HGV20) or 21-mers (AHG21) of the MUC1 tandem repeat peptide carrying GalNAcalpha or Galbeta1-3GalNAcalpha at different positions. The enzymatic products were analyzed by MALDI mass spectrometry and Edman degradation for the number and sites of incorporated GalNAc. Disaccharide placed on the first position of the diad Ser-16-Thr-17 prevents glycosylation of the second, whereas disaccharide on the second position of Ser-16-Thr-17 and Thr-5-Ser-6 does not prevent GalNAc addition to the first. Multiple disaccharide substituents suppress any further glycosylation at the remaining sites. Glycosylation of Ser-16 is negatively affected by glycosylation at position -6 (Thr-10) or -10 (Ser-6) and is inhibited by disaccharide at position -11 (Thr-5), suggesting the occurrence of glycosylation-induced effects on distant acceptor sites. Kinetic studies revealed the accelerated addition of GalNAc to Ser-16 adjacent to GalNAc-substituted Thr-17, demonstrating positive regulatory effects induced by glycosylation on the monosaccharide level. These antagonistic effects of mono- and disaccharides could underlie a postulated regulatory mechanism. (+info)The role of tumour markers in predicting skeletal metastases in breast cancer patients with equivocal bone scintigraphy. (7/1160)
Bone scintigraphy (BS) is commonly performed in the staging and postoperative monitoring of breast cancer. Nevertheless, due to low specificity it often demonstrates hot spots with equivocal interpretation, which may be misleading in the management of these patients. The aim of this study was to assess the value of a serum tumour marker panel in selecting among the patients with equivocal BS those with bone metastases. Between January 1986 and December 1995, 297 breast cancer patients were followed-up after mastectomy with serial determinations of a CEA-TPA-CA15.3 tumour marker panel, BS and liver echography. The tumour marker panel was used to select patients with equivocal BS for examination of suspicious bone areas by further imaging techniques. Up to December 1995, 158 (53%) patients showed an equivocal BS and 47 patients developed bone metastases. In the 158 patients with equivocal BS, prolonged clinical and imaging follow-up over 45 months (mean; range 12-120) was used to ascertain the presence or absence of bone metastases. In these 158 patients the negative predictive value and positive predictive value of the tumour marker panel to predict bone metastases was 97% and 75% respectively. This study shows that in breast cancer patients the CEA-TPA-CA15.3 tumour marker panel has a high value in selecting those patients with bone metastases, or at high risk of developing clinically-evident bone metastases, among the large number of subjects with equivocal BS. (+info)The breast cancer-associated MUC1 gene generates both a receptor and its cognate binding protein. (8/1160)
MUC1 proteins, some of which contain a mucin-like domain and others lacking this region, can be generated from the human breast cancer-associated MUC1 gene by alternative splicing. The MUC1/Y isoform is devoid of the mucin domain and is a cell membrane protein that undergoes transphosphorylation on both serine and tyrosine residues. We have identified cognate binding proteins that specifically interact with the extracellular domain of MUC1/Y. Coimmunoprecipitation analyses clearly revealed the presence of complexes composed of MUC1/Y and its cognate binding proteins in primary breast tumor tissue. MUC1/Y-expressing mammary tumor cells can be specifically targeted, in vivo, with the labeled cognate binding protein. The k(D) of MUC1/Y for its binding proteins was estimated as 1.2 nM. The MUC1/Y binding proteins are also derived from the MUC1 gene and represent the secreted mucin-like polymorphic MUC1 proteins MUC1/SEC and MUC1/REP, which contain a tandem repeat array. Whereas nonposttranslationally modified MUC1/Y bound efficiently to MUC1/SEC, the latter mucin-like protein had to be posttranslationally modified in a cell-type specific manner to bind MUC1/Y. The interaction of MUC1/Y with MUC1/SEC has important biological functional correlates: (a) it induces MUC1/Y phosphorylation; and (b) it has a pronounced effect on cell morphology. These findings suggest that MUC1/Y and MUC1/SEC form an active receptor/ cognate binding protein complex that can elicit cellular responses. The proteins comprising this complex are, thus, generated by alternative splicing from one and the same gene, namely the MUC1 gene. (+info)Mucins are high molecular weight, heavily glycosylated proteins that are the major components of mucus. They are produced and secreted by specialized epithelial cells in various organs, including the respiratory, gastrointestinal, and urogenital tracts, as well as the eyes and ears.
Mucins have a characteristic structure consisting of a protein backbone with numerous attached oligosaccharide side chains, which give them their gel-forming properties and provide a protective barrier against pathogens, environmental insults, and digestive enzymes. They also play important roles in lubrication, hydration, and cell signaling.
Mucins can be classified into two main groups based on their structure and function: secreted mucins and membrane-bound mucins. Secreted mucins are released from cells and form a physical barrier on the surface of mucosal tissues, while membrane-bound mucins are integrated into the cell membrane and participate in cell adhesion and signaling processes.
Abnormalities in mucin production or function have been implicated in various diseases, including chronic inflammation, cancer, and cystic fibrosis.
Gastric mucins refer to the mucin proteins that are produced and secreted by the mucus-secreting cells in the stomach lining, also known as gastric mucosa. These mucins are part of the gastric mucus layer that coats and protects the stomach from damage caused by digestive acids and enzymes, as well as from physical and chemical injuries.
Gastric mucins have a complex structure and are composed of large glycoprotein molecules that contain both protein and carbohydrate components. They form a gel-like substance that provides a physical barrier between the stomach lining and the gastric juices, preventing acid and enzymes from damaging the underlying tissues.
There are several types of gastric mucins, including MUC5AC and MUC6, which have different structures and functions. MUC5AC is the predominant mucin in the stomach and is produced by surface mucous cells, while MUC6 is produced by deeper glandular cells.
Abnormalities in gastric mucin production or composition can contribute to various gastrointestinal disorders, including gastritis, gastric ulcers, and gastric cancer.
Mucin-5B, also known as MUC5B, is a type of mucin protein that is heavily glycosylated and found in the respiratory tract. It is one of the major components of airway mucus, which helps to trap and remove inhaled particles and microorganisms from the lungs.
Mucin-5B is a large molecular weight gel-forming mucin that is produced by goblet cells and submucosal glands in the respiratory epithelium. It has a complex structure, consisting of a protein backbone with numerous oligosaccharide side chains that give it its gel-like properties.
Mutations in the MUC5B gene have been associated with several lung diseases, including chronic obstructive pulmonary disease (COPD), bronchiectasis, and idiopathic pulmonary fibrosis (IPF). In particular, a common genetic variant in the MUC5B promoter region has been identified as a significant risk factor for developing IPF.
Mucin-1, also known as MUC1, is a type of protein called a transmembrane mucin. It is heavily glycosylated and found on the surface of many types of epithelial cells, including those that line the respiratory, gastrointestinal, and urogenital tracts.
Mucin-1 has several functions, including:
* Protecting the underlying epithelial cells from damage caused by friction, chemicals, and microorganisms
* Helping to maintain the integrity of the mucosal barrier
* Acting as a receptor for various signaling molecules
* Participating in immune responses
In cancer, MUC1 can be overexpressed or aberrantly glycosylated, which can contribute to tumor growth and metastasis. As a result, MUC1 has been studied as a potential target for cancer immunotherapy.
Mucin-4, also known as "Podocalyxin-like" or "PODXL," is a type of transmembrane mucin protein that is heavily glycosylated. It is primarily expressed on the surface of certain types of cells, including epithelial and endothelial cells.
Mucin-4 is a large molecule with a molecular weight ranging from 150 to 250 kDa, depending on its degree of glycosylation. It has a extracellular domain that contains several N-linked glycans and O-linked oligosaccharides, which give it a highly extended structure and contribute to its ability to form protective barriers on the cell surface.
Mucin-4 is involved in various biological processes, such as providing a barrier function, regulating cell adhesion, and modulating immune responses. It has been implicated in several diseases, including cancer, where it can promote tumor growth and metastasis by facilitating cell migration and invasion. In the kidney, Mucin-4 is expressed on the surface of podocytes, which are specialized epithelial cells that play a critical role in maintaining the filtration barrier in the glomerulus. Mutations in the MUC16 gene, which encodes Mucin-4, have been associated with nephrotic syndrome, a kidney disorder characterized by proteinuria and edema.
Mucin-3, also known as MUC3A or CA15-3, is a type of mucin protein that is heavily glycosylated and found on the apical surface of epithelial cells in the gastrointestinal tract. It is a transmembrane protein that plays a role in protecting the epithelial surface from damage, infection, and inflammation. Mucin-3 has been identified as a tumor antigen and its expression is often upregulated in various types of cancer, including colon, pancreatic, and ovarian cancers. The soluble form of Mucin-3 can be measured in the blood and used as a tumor marker to monitor the progression of certain cancers.
I'm sorry for any confusion, but "Mucin-6" is not a widely recognized or established medical term. Mucins are high molecular weight glycoproteins that are the major component of mucus, which is produced by specialized epithelial cells in various organs. Each mucin is identified by a number, such as Mucin-1, Mucin-2, and so on, based on their order of discovery.
However, I couldn't find any reputable medical sources that mention "Mucin-6." It's possible that it may be a topic of ongoing research or that it might be referred to by another name. I would recommend consulting a specific scientific study or researcher for more accurate and detailed information.
Goblet cells are specialized epithelial cells that are located in various mucosal surfaces, including the respiratory and gastrointestinal tracts. They are named for their goblet-like shape, which is characterized by a narrow base and a wide, rounded top that contains secretory granules. These cells play an essential role in producing and secreting mucins, which are high molecular weight glycoproteins that form the gel-like component of mucus.
Mucus serves as a protective barrier for the underlying epithelial cells by trapping foreign particles, microorganisms, and toxins, preventing them from coming into contact with the epithelium. Goblet cells also help maintain the hydration of the mucosal surface, which is important for normal ciliary function in the respiratory tract and for the movement of food through the gastrointestinal tract.
In summary, goblet cells are secretory cells that produce and release mucins to form the mucus layer, providing a protective barrier and maintaining the homeostasis of mucosal surfaces.
Mucus is a viscous, slippery secretion produced by the mucous membranes that line various body cavities such as the respiratory and gastrointestinal tracts. It serves to lubricate and protect these surfaces from damage, infection, and foreign particles. Mucus contains water, proteins, salts, and other substances, including antibodies, enzymes, and glycoproteins called mucins that give it its characteristic gel-like consistency.
In the respiratory system, mucus traps inhaled particles such as dust, allergens, and pathogens, preventing them from reaching the lungs. The cilia, tiny hair-like structures lining the airways, move the mucus upward toward the throat, where it can be swallowed or expelled through coughing or sneezing. In the gastrointestinal tract, mucus helps protect the lining of the stomach and intestines from digestive enzymes and other harmful substances.
Excessive production of mucus can occur in various medical conditions such as allergies, respiratory infections, chronic lung diseases, and gastrointestinal disorders, leading to symptoms such as coughing, wheezing, nasal congestion, and diarrhea.
Sialomucins are a type of glycoprotein mucins that contain high amounts of sialic acid, which is a family of negatively charged sugars found on the surface of many cell types. These mucins are produced by the major salivary glands and are a major component of saliva. They play an important role in lubricating and protecting the oral cavity, as well as contributing to the mouth's ability to resist infection and damage.
Sialomucins have also been shown to have various biological functions, such as regulating cell adhesion, modulating immune responses, and serving as receptors for certain viruses and bacteria. Abnormalities in sialomucin expression or structure have been implicated in several diseases, including cancer, autoimmune disorders, and infectious diseases.
Glycosylation is the enzymatic process of adding a sugar group, or glycan, to a protein, lipid, or other organic molecule. This post-translational modification plays a crucial role in modulating various biological functions, such as protein stability, trafficking, and ligand binding. The structure and composition of the attached glycans can significantly influence the functional properties of the modified molecule, contributing to cell-cell recognition, signal transduction, and immune response regulation. Abnormal glycosylation patterns have been implicated in several disease states, including cancer, diabetes, and neurodegenerative disorders.
Tumor-associated carbohydrate antigens (TACAs) are a type of tumor antigen that are expressed on the surface of cancer cells. These antigens are abnormal forms of carbohydrates, also known as glycans, which are attached to proteins and lipids on the cell surface.
TACAs are often overexpressed or expressed in a different form on cancer cells compared to normal cells. This makes them attractive targets for cancer immunotherapy because they can be recognized by the immune system as foreign and elicit an immune response. Some examples of TACAs include gangliosides, fucosylated glycans, and sialylated glycans.
Tumor-associated carbohydrate antigens have been studied as potential targets for cancer vaccines, antibody therapies, and other immunotherapeutic approaches. However, their use as targets for cancer therapy is still in the early stages of research and development.
Oligosaccharides are complex carbohydrates composed of relatively small numbers (3-10) of monosaccharide units joined together by glycosidic linkages. They occur naturally in foods such as milk, fruits, vegetables, and legumes. In the body, oligosaccharides play important roles in various biological processes, including cell recognition, signaling, and protection against pathogens.
There are several types of oligosaccharides, classified based on their structures and functions. Some common examples include:
1. Disaccharides: These consist of two monosaccharide units, such as sucrose (glucose + fructose), lactose (glucose + galactose), and maltose (glucose + glucose).
2. Trisaccharides: These contain three monosaccharide units, like maltotriose (glucose + glucose + glucose) and raffinose (galactose + glucose + fructose).
3. Oligosaccharides found in human milk: Human milk contains unique oligosaccharides that serve as prebiotics, promoting the growth of beneficial bacteria in the gut. These oligosaccharides also help protect infants from pathogens by acting as decoy receptors and inhibiting bacterial adhesion to intestinal cells.
4. N-linked and O-linked glycans: These are oligosaccharides attached to proteins in the body, playing crucial roles in protein folding, stability, and function.
5. Plant-derived oligosaccharides: Fructooligosaccharides (FOS) and galactooligosaccharides (GOS) are examples of plant-derived oligosaccharides that serve as prebiotics, promoting the growth of beneficial gut bacteria.
Overall, oligosaccharides have significant impacts on human health and disease, particularly in relation to gastrointestinal function, immunity, and inflammation.
The trachea, also known as the windpipe, is a tube-like structure in the respiratory system that connects the larynx (voice box) to the bronchi (the two branches leading to each lung). It is composed of several incomplete rings of cartilage and smooth muscle, which provide support and flexibility. The trachea plays a crucial role in directing incoming air to the lungs during inspiration and outgoing air to the larynx during expiration.
The Periodic Acid-Schiff (PAS) reaction is a histological staining method used to detect the presence of certain carbohydrates, such as glycogen and glycoproteins, in tissues or cells. This technique involves treating the tissue with periodic acid, which oxidizes the vicinal hydroxyl groups in the carbohydrates, creating aldehydes. The aldehydes then react with Schiff's reagent, forming a magenta-colored complex that is visible under a microscope.
The PAS reaction is commonly used to identify and analyze various tissue components, such as basement membranes, fungal cell walls, and mucins in the respiratory and gastrointestinal tracts. It can also be used to diagnose certain medical conditions, like kidney diseases, where abnormal accumulations of carbohydrates occur in the renal tubules or glomeruli.
In summary, the Periodic Acid-Schiff reaction is a staining method that detects specific carbohydrates in tissues or cells, which can aid in diagnostic and research applications.
Carbohydrates are a major nutrient class consisting of organic compounds that primarily contain carbon, hydrogen, and oxygen atoms. They are classified as saccharides, which include monosaccharides (simple sugars), disaccharides (double sugars), oligosaccharides (short-chain sugars), and polysaccharides (complex carbohydrates).
Monosaccharides, such as glucose, fructose, and galactose, are the simplest form of carbohydrates. They consist of a single sugar molecule that cannot be broken down further by hydrolysis. Disaccharides, like sucrose (table sugar), lactose (milk sugar), and maltose (malt sugar), are formed from two monosaccharide units joined together.
Oligosaccharides contain a small number of monosaccharide units, typically less than 20, while polysaccharides consist of long chains of hundreds to thousands of monosaccharide units. Polysaccharides can be further classified into starch (found in plants), glycogen (found in animals), and non-starchy polysaccharides like cellulose, chitin, and pectin.
Carbohydrates play a crucial role in providing energy to the body, with glucose being the primary source of energy for most cells. They also serve as structural components in plants (cellulose) and animals (chitin), participate in various metabolic processes, and contribute to the taste, texture, and preservation of foods.
The intestinal mucosa is the innermost layer of the intestines, which comes into direct contact with digested food and microbes. It is a specialized epithelial tissue that plays crucial roles in nutrient absorption, barrier function, and immune defense. The intestinal mucosa is composed of several cell types, including absorptive enterocytes, mucus-secreting goblet cells, hormone-producing enteroendocrine cells, and immune cells such as lymphocytes and macrophages.
The surface of the intestinal mucosa is covered by a single layer of epithelial cells, which are joined together by tight junctions to form a protective barrier against harmful substances and microorganisms. This barrier also allows for the selective absorption of nutrients into the bloodstream. The intestinal mucosa also contains numerous lymphoid follicles, known as Peyer's patches, which are involved in immune surveillance and defense against pathogens.
In addition to its role in absorption and immunity, the intestinal mucosa is also capable of producing hormones that regulate digestion and metabolism. Dysfunction of the intestinal mucosa can lead to various gastrointestinal disorders, such as inflammatory bowel disease, celiac disease, and food allergies.
A "carbohydrate sequence" refers to the specific arrangement or order of monosaccharides (simple sugars) that make up a carbohydrate molecule, such as a polysaccharide or an oligosaccharide. Carbohydrates are often composed of repeating units of monosaccharides, and the sequence in which these units are arranged can have important implications for the function and properties of the carbohydrate.
For example, in glycoproteins (proteins that contain carbohydrate chains), the specific carbohydrate sequence can affect how the protein is processed and targeted within the cell, as well as its stability and activity. Similarly, in complex carbohydrates like starch or cellulose, the sequence of glucose units can determine whether the molecule is branched or unbranched, which can have implications for its digestibility and other properties.
Therefore, understanding the carbohydrate sequence is an important aspect of studying carbohydrate structure and function in biology and medicine.
The conjunctiva is the mucous membrane that lines the inner surface of the eyelids and covers the front part of the eye, also known as the sclera. It helps to keep the eye moist and protected from irritants. The conjunctiva can become inflamed or infected, leading to conditions such as conjunctivitis (pink eye).