BPIFA4P
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BPIFA4P
BPI fold containing family A, member 4 (BPIFA4) is a non-human protein encoded by the ''Bpifa4'' gene in monkey and cow. It is also known as Latherin in horse, encoded by the ''Lath/Bpifa4'' gene but somewhat divergent from the other species. Latherin/BPIFA4 is a secreted protein found in saliva and sweat. In humans, no protein is normally expressed and BPIFB5P is present only as a pseudogene ''BPIFB5P''. However, it has appeared as a secreted product in breast cancer cell lines, previously named BASE (''b''reast cancer ''a''nd ''s''alivary gland ''e''xpression) protein. Superfamily BPIFA3 is a member of a BPI fold protein superfamily defined by the presence of the bactericidal/permeability-increasing protein fold (BPI fold) which is formed by two similar domains in a "boomerang" shape. This superfamily is also known as the BPI/LBP/PLUNC family or the BPI/ LPB/ CETP family. The BPI fold creates apolar binding pockets that can interact with hydrophobic and amphipathic mole ...
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Lipid-binding Serum Glycoprotein
In molecular biology, the lipid-binding serum glycoproteins family, also known as the BPI/LBP/Plunc family or LBP/BPI/CETP family represents a family which includes mammalian lipid-binding serum glycoproteins and/or proteins containing a structural motif known as the ''BPI fold''. Members of this family include: *Bactericidal permeability-increasing protein (BPI) * Lipopolysaccharide-binding protein (LBP) *Cholesteryl ester transfer protein (CETP) * Phospholipid transfer protein (PLTP) * Palate, lung and nasal epithelium carcinoma-associated protein (PLUNC) Structure These proteins consist of N- and C-terminal domains, which share a similar two-layer alpha/beta structure, but show little sequence identity to each other. These domains were first described as being arranged in a "boomerang" shape that creates the BPI fold. The fold contains apolar binding pockets that can interact with hydrophobic and amphipathic molecules, such as the acyl carbon chains of lipopolysacch ...
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BPIFA2
BPI fold containing family A, member 2 (BPIFA2), also known as Parotid Secretory Protein (PSP), is a protein that in humans is encoded by the ''BPIFA2'' gene. The ''BPIFA2'' gene sequence predicts multiple transcripts ( splice variants); 2 mRNA variants have been well characterized. The resulting BPIFA2 is a secreted protein, expressed at very high levels in the parotid (salivary) gland; at high levels in oropharyneal mucosa, including tongue; and at moderate levels many other tissue types and glands including mammary gland, testis, lung, bladder, blood, prostate, adrenal gland, kidney, and pancreas. Superfamily BPIFA2 is a member of a BPI fold protein superfamily defined by the presence of the bactericidal/permeability-increasing protein fold (BPI fold) which is formed by two similar domains in a "boomerang" shape. This superfamily is also known as the BPI/LBP/PLUNC family or the BPI/ LPB/CETP family. The BPI fold creates apolar binding pockets that can interact with hydr ...
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BPIFB1
BPI fold containing family B, member 1 (BPIFB1) is a protein that in humans is encoded by the ''BPIFB1'' gene. BPIFB1 is a secreted protein, expressed at very high levels in mucosa of the airways (respiratory and olfactory epithelium) and salivary glands, and at moderate levels in the digestive tract (tongue, stomach, intestinal epithelium) and pancreas. Superfamily BPIFB1 is a member of a BPI fold protein superfamily defined by the presence of the bactericidal/permeability-increasing protein fold (BPI fold) which is formed by two similar domains in a "boomerang" shape. This superfamily is also known as the BPI/LBP/PLUNC family or the BPI/ LPB/CETP family. The BPI fold creates apolar binding pockets that can interact with hydrophobic and amphipathic molecules, such as the acyl carbon chains of lipopolysaccharide found on Gram-negative bacteria, but members of this family may have many other functions. Genes for the BPI/LBP/PLUNC superfamily are found in all vertebrate sp ...
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BPIFB9P
Vomeromodulin is a non-human protein also known as BPI fold containing family B, member 9 (BPIFB9) in the rat encoded by the ''Bpifb9/RYF3'' gene, and as BPI fold containing family B, member 9A (BPIFB9A) encoded by the ''Bpifb9a'' gene in the mouse. This protein has been characterized in mammals such as rodents, carnivores, even-toed ungulates, insectivores, bats, lagomorphs, and shrews but is apparently absent in primates and other vertebrates such as birds, reptiles, and amphibians. Its function is associated with detection of chemical odorant pheromone molecules. In humans no protein is expressed and it is present only as a pseudogene ''BPIFB9P''. The pseudogene was named based on its functional ortholog found in the other species. Superfamily Vomeromodulin/BPIFB9/BPIFB9A is a member of the BPI fold protein superfamily defined by the presence of the bactericidal/permeability-increasing protein fold (BPI fold) which is formed by two similar domains in a "boomerang" ...
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BPIFB5P
BPI fold containing family B, member 5 is a non-human protein encoded by the ''Bpifb5'' gene, also known as ''Lplunc5.'' The BPIFB5 protein and ''Bpifb5'' gene have been characterized in mammals such as rodents (mouse, rat) and even-toed ungulates (pig, cow) but are apparently lacking in primates and other vertebrates such as birds, reptiles, and amphibians. The protein in rodents is expressed at moderately high levels in Mucous membrane, mucosa of the airways (respiratory and olfactory epithelium) and at moderate levels in salivary glands, esophagus, and gonads (ovary, testis); in even-toed ungulates expression is high in testis, moderate in brain and striated muscle, and low in kidney. In humans no protein is expressed and it is present only as a pseudogene ''BPIFB5P''. The pseudogene was named based on its functional ortholog found in the other species. Superfamily BPIFB5 is a member of the BPI fold protein superfamily defined by the presence of the bactericidal/permeabil ...
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BPIFB6
BPI fold containing family B, member 6 (BPIFB6), also known as bactericidal/permeability-increasing protein-like 3 (BPIL3), is a protein that in humans is encoded by the ''BPIFB6'' gene, also known as ''BPIL3'' and ''LPLUNC6''. It is expressed at high levels in hypertrophic tonsils, at relatively moderate levels in oronasal epithelium including nasal mucosa, tongue, and salivary gland, as well as esophageal mucosa at lesser levels. Orthologs are present in many vertebrate species including mammals, birds, reptiles, and amphibians. Superfamily BPIFB6 is a member of a BPI fold protein superfamily defined by the presence of the bactericidal/permeability-increasing protein fold (BPI fold) which is formed by two similar domains in a "boomerang" shape. This superfamily is also known as the BPI/LBP/PLUNC family or the BPI/ LPB/ CETP family. The BPI fold creates apolar binding pockets that can interact with hydrophobic and amphipathic molecules, such as the acyl carbon chains ...
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BPIFB3
BPI fold containing family B, member 3 (BPIFB3) is a protein that in humans is encoded by the ''BPIFB3'' gene. Two variants have been detected in humans. Superfamily BPIFB3 is a member of a BPI fold protein superfamily defined by the presence of the bactericidal/permeability-increasing protein fold (BPI fold) which is formed by two similar domains in a "boomerang" shape. This superfamily is also known as the BPI/LBP/PLUNC family or the BPI/ LPB/ CETP family. The BPI fold creates apolar binding pockets that can interact with hydrophobic and amphipathic molecules, such as the acyl carbon chains of lipopolysaccharide found on Gram-negative bacteria, but members of this family may have many other functions. Genes for the BPI/LBP/PLUNC superfamily are found in all vertebrate species, including distant homologs in non-vertebrate species such as insects, mollusks, and roundworms. Within that broad grouping is the BPIF gene family whose members encode the BPI fold structur ...
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BPIFB2
BPI fold-containing family B, member 2, (BPIFB2) also known as bactericidal/permeability-increasing protein-like 1, (BPI-like 1) is a protein that in humans is encoded by the ''BPIFB2'' gene. Superfamily BPIFB2 is a member of a BPI fold protein superfamily defined by the presence of the bactericidal/permeability-increasing protein fold (BPI fold) which is formed by two similar domains in a "boomerang" shape. This superfamily is also known as the BPI/LBP/PLUNC family or the BPI/ LPB/ CETP family. The BPI fold creates apolar binding pockets that can interact with hydrophobic and amphipathic molecules, such as the acyl carbon chains of lipopolysaccharide found on Gram-negative bacteria, but members of this family may have many other functions. Genes for the BPI/LBP/PLUNC superfamily are found in all vertebrate species, including distant homologs in non-vertebrate species such as insects, mollusks, and roundworms. Within that broad grouping is the BPIF gene family whose m ...
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BPIFA1
BPI fold containing family A, member 1 (BPIFA1), also known as Palate, lung, and nasal epithelium clone (PLUNC), is a protein that in humans is encoded by the ''BPIFA1'' gene. It was also formerly known as "Secretory protein in upper respiratory tracts" (SPURT). The ''BPIFA1'' gene sequence predicts 4 transcripts ( splice variants); 3 mRNA variants have been well characterized. The resulting BPIFA1 is a secreted protein, expressed at very high levels in mucosa of the airways (olfactory and respiratory and epithelium) and salivary glands; at high levels in oropharyneal epithelium, including tongue and tonsils; and at moderate levels many other tissue types and glands including pituitary, testis, lung, bladder, blood, prostate, pancreas, levels in the digestive tract (tongue, stomach, intestinal epithelium) and pancreas. The protein can be detected on the apical side of epithelial cells and in airway surface liquid, nasal mucus, and sputum. Superfamily BPIFA1 is a member of a B ...
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Chewing
Chewing or mastication is the process by which food is crushed and ground by teeth. It is the first step of digestion, and it increases the surface area of foods to allow a more efficient break down by enzymes. During the mastication process, the food is positioned by the cheek and tongue between the teeth for grinding. The muscles of mastication move the jaws to bring the teeth into intermittent contact, repeatedly occluding and opening. As chewing continues, the food is made softer and warmer, and the enzymes in saliva begin to break down carbohydrates in the food. After chewing, the food (now called a bolus) is swallowed. It enters the esophagus and via peristalsis continues on to the stomach, where the next step of digestion occurs. Increasing the number of chews per bite increases relevant gut hormones. Studies suggest that chewing may decrease self-reported hunger and food intake. Chewing gum has been around for many centuries; there is evidence that northern Europeans ch ...
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Ruminant
Ruminants (suborder Ruminantia) are ungulate, hoofed herbivorous grazing or browsing mammals that are able to acquire nutrients from plant-based food by Enteric fermentation, fermenting it in a specialized stomach prior to digestion, principally through microbial actions. The process, which takes place in the front part of the digestive system and therefore is called foregut fermentation, typically requires the fermented ingesta (known as cud) to be regurgitated and chewed again. The process of rechewing the cud to further break down plant matter and stimulate digestion is called rumination. The word "ruminant" comes from the Latin ''ruminare'', which means "to chew over again". The roughly 200 species of ruminants include both domestic and wild species. Ruminating mammals include cattle, all domesticated and wild bovines, goats, sheep, giraffes, deer, gazelles, and antelopes.Fowler, M.E. (2010).Medicine and Surgery of Camelids, Ames, Iowa: Wiley-Blackwell. Chapter 1 General Biolo ...
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Lipopolysaccharides
Lipopolysaccharides (LPS) are large molecules consisting of a lipid and a polysaccharide that are bacterial toxins. They are composed of an O-antigen, an outer core, and an inner core all joined by a covalent bond, and are found in the outer membrane of Gram-negative bacteria. Today, the term ''endotoxin'' is often used synonymously with LPS, although there are a few endotoxins (in the original sense of toxins that are inside the bacterial cell that are released when the cell disintegrates) that are not related to LPS, such as the so-called delta endotoxin proteins produced by '' Bacillus thuringiensis''. Lipopolysaccharides can have substantial impacts on human health, primarily through interactions with the immune system. LPS is a potent activator of the immune system and pyrogen (agent that causes fever). In severe cases, LPS can play a role in causing septic shock. In lower levels and over a longer time period, there is evidence LPS may play an important and harmful role in ...
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