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Lachesis (genus)
''Lachesis'', also known as bushmasters,Campbell JA, Lamar WW. 2004. The Venomous Reptiles of the Western Hemisphere. 2 volumes. Comstock Publishing Associates, Ithaca and London. 870 pp. 1500 plates. . is a genus of venomous pit vipers found in forested areas of Central and South America. The generic name refers to one of the Three Fates, Lachesis, in Greek mythology who determined the length of the thread of life. Four species are currently recognized. Description Adults vary in length from , although some may grow to as much as , making it the longest venomous snake in the Western Hemisphere. Bushmasters are the longest type of viper in the world. ''L. muta'' is possibly the largest of the three species currently recognized, although more scant information suggest ''L. stenophrys'' broadly overlaps in size and may average at a similar size, while ''L. melanocephala'' and ''L. acrochorda'' are seemingly slightly smaller than the prior two species. Although they are not the hea ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lachesis Muta
''Lachesis muta'', also known as the Southern American bushmaster or Atlantic bushmaster, is a venomous pit viper species found in South America, as well as the island of Trinidad in the Caribbean. Two subspecies are currently recognized, including the nominate subspecies described here. Taxonomy Two additional subspecies, ''L. m. melanocephala'' and ''L. m. stenophrys'', had earlier been recognized. However, both were elevated to species level by Zamudio and Green in 1997 (see '' L. melanocephala'' and '' L. stenophrys''). Subspecies Description Adults grow to an average of 2 to 2.5 m (6½-8 feet), although 3 m (10 feet) is not too unusual. The largest recorded specimen was 3.65 m (almost 12 feet) long, making this the largest of all vipers and the longest venomous snake in the western hemisphere.Mehrtens JM (1987). ''Living Snakes of the World in Color''. New York: Sterling Publishers. 480 pp. . ''Lachesis muta'' is the third longest venomous snake in the world, ex ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tail Vibration
Tail vibration is a common behavior in some snakes where the tail is vibrated rapidly as a defensive response to a potential predator. Tail vibration should not be confused with where the tail is twitched in order to attract prey. While rattlesnakes are perhaps the most famous group of snakes to exhibit tail vibration behavior, many other snake groups—particularly those in the Colubridae and Viperidae families—are known to vibrate tails when feeling threatened. Description Process Tail vibration involves the rapid shaking of the tail in response to a predatory threat. The behavior is particularly widespread among New World species of Viperidae and Colubridae.Allf, Bradley C., Paul AP Durst, and David W. Pfennig. "Behavioral Plasticity and the Origins of Novelty: The Evolution of the Rattlesnake Rattle." The American Naturalist 188.4 (2016): 475–483Young, Bruce A. "Snake bioacoustics: toward a richer understanding of the behavioral ecology of snakes." The Quarterly review o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lachesis Acrochorda
''Lachesis acrochorda'', also known commonly as the Chocoan bushmaster, Campbell JA, Lamar WW (2004). ''The Venomous Reptiles of the Western Hemisphere''. 2 volumes. Ithaca and London: Comstock Publishing Associates. 870 pp., 1,500 plates. . is a species of venomous pit viper in the family Viperidae. The species is native to Central America and South America. Taxonomy ''L. acrochorda'' was formerly considered a synonym of '' Lachesis stenophrys''. Description ''L. acrochorda'' has a light brown head and black postocular stripes that can range from 1-2 scales wide. The longest recorded length of a male individual in Ecuador was ; for females it was . Geographic range ''L. acrochorda'' is found in Panama, northern and western Colombia (in the Departments of Chocó, Cauca and Antioquia), and northwestern Ecuador. Habitat The preferred natural habitat of ''L. acrochorda'' is lowland forest, premontane wet forest, and montane wet forest, mostly in mature forests, at alti ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Kallikrein
Kallikreins are a subgroup of serine proteases, enzymes capable of cleaving peptide bonds in proteins. In humans, plasma kallikrein (encoded by '' KLKB1 gene'') has no known paralogue, while tissue kallikrein-related peptidases (''KLKs'') encode a family of fifteen closely related serine proteases. These genes are localised to chromosome 19q13, forming the largest contiguous cluster of proteases within the human genome. Kallikreins are responsible for the coordination of various physiological functions including blood pressure, semen liquefaction and skin desquamation. Occurrence In 1934, Eugen Werle reported finding a substance in the pancreas of humans and various animals in such large amounts that the pancreas could be taken for its site of origin. He named it kallikrein, by derivation from the Greek word for pancreas. Since then, similar enzymes have been found in the biological fluids of humans and other mammals, as well as in some snake venoms. Venom The caterpillar kno ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bradykinin
Bradykinin (BK) (Greek brady-, slow; -kinin, kīn(eîn) to move) is a peptide that promotes inflammation. It causes arterioles to dilate (enlarge) via the release of prostacyclin, nitric oxide, and endothelium-derived hyperpolarizing factor and makes veins constrict, via prostaglandin F2, thereby leading to leakage into capillary beds, due to the increased pressure in the capillaries. Bradykinin is a physiologically and pharmacologically active peptide of the kinin group of proteins, consisting of nine amino acids. A class of drugs called angiotensin converting enzyme inhibitors (ACE inhibitors) increase bradykinin levels by inhibiting its degradation, thereby increasing its blood pressure lowering effect. ACE inhibitors are FDA approved for the treatment of hypertension and heart failure. Structure Bradykinin, sometimes referred to as BK, is a 9-amino acid peptide chain. The amino acid sequence of bradykinin is: Arg- Pro- Pro- Gly- Phe- Ser- Pro- Phe- Arg (RPPGFSPFR). ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Kininogen
Kininogens are precursor proteins for kinins, biologically active polypeptides involved in blood coagulation, vasodilation, smooth muscle contraction, inflammatory regulation, and the regulation of the cardiovascular and renal systems. Types of kininogen There are two main types of kininogen (KNG), high-molecular-weight-kininogen and low-molecular-weight-kininogen, with a third type – T-kininogen – only found in rats but not humans. High molecular weight kininogen High-molecular-weight-kininogen (HK) is a non-enzymatic cofactor involved in the kinin-kallikrein system, which plays a role in blood coagulation, blood pressure regulation, and inflammation. It is synthesized in endothelial cells and is produced mostly by the liver. It is also a precursor protein for bradykinin. Low molecular weight kininogen Low-molecular-weight-kininogen (LK) is mainly a precursor protein for kallidin. LK, however, is not actively involved in blood coagulation, but its byproducts c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phospholipase
A phospholipase is an enzyme that hydrolyzes phospholipids into fatty acids and other lipophilic substances. Acids trigger the release of bound calcium from cellular stores and the consequent increase in free cytosolic Ca2+, an essential step in calcium signaling to regulate intracellular processes. There are four major classes, termed A, B, C, and D, which are distinguished by the type of reaction which they catalyze: *Phospholipase A ** Phospholipase A1 – cleaves the ''sn''-1 acyl chain (where ''sn'' refers to stereospecific numbering). **Phospholipase A2 – cleaves the ''sn''-2 acyl chain, releasing arachidonic acid. *Phospholipase B – cleaves both ''sn''-1 and ''sn''-2 acyl chains; this enzyme is also known as a lysophospholipase. *Phospholipase C – cleaves before the phosphate, releasing diacylglycerol and a phosphate-containing head group. PLCs play a central role in signal transduction, releasing the second messenger inositol triphosphate. *Phospholipase D – ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Metalloprotease
A metalloproteinase, or metalloprotease, is any protease enzyme whose catalytic mechanism involves a metal. An example is ADAM12 which plays a significant role in the fusion of muscle cells during embryo development, in a process known as myogenesis. Most metalloproteases require zinc, but some use cobalt. The metal ion is coordinated to the protein via three ligands. The ligands coordinating the metal ion can vary with histidine, glutamate, aspartate, lysine, and arginine. The fourth coordination position is taken up by a labile water molecule. Treatment with chelating agents such as EDTA leads to complete inactivation. EDTA is a metal chelator that removes zinc, which is essential for activity. They are also inhibited by the chelator orthophenanthroline. Classification There are two subgroups of metalloproteinases: * Exopeptidases, metalloexopeptidases ( EC number: 3.4.17). * Endopeptidases, metalloendopeptidases (3.4.24). Well known metalloendopeptidases include ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fibrinogen
Fibrinogen (factor I) is a glycoprotein complex, produced in the liver, that circulates in the blood of all vertebrates. During tissue and vascular injury, it is converted enzymatically by thrombin to fibrin and then to a fibrin-based blood clot. Fibrin clots function primarily to occlude blood vessels to stop bleeding. Fibrin also binds and reduces the activity of thrombin. This activity, sometimes referred to as antithrombin I, limits clotting. Fibrin also mediates blood platelet and endothelial cell spreading, tissue fibroblast proliferation, capillary tube formation, and angiogenesis and thereby promotes revascularization and wound healing. Reduced and/or dysfunctional fibrinogens occur in various congenital and acquired human fibrinogen-related disorders. These disorders represent a group of rare conditions in which individuals may present with severe episodes of pathological bleeding and thrombosis; these conditions are treated by supplementing blood fibrinogen level ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thrombin
Thrombin (, ''fibrinogenase'', ''thrombase'', ''thrombofort'', ''topical'', ''thrombin-C'', ''tropostasin'', ''activated blood-coagulation factor II'', ''blood-coagulation factor IIa'', ''factor IIa'', ''E thrombin'', ''beta-thrombin'', ''gamma-thrombin'') is a serine protease, an enzyme that, in humans, is encoded by the ''F2'' gene. Prothrombin (coagulation factor II) is proteolytically cleaved to form thrombin in the clotting process. Thrombin in turn acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzing many other coagulation-related reactions. History After the description of fibrinogen and fibrin, Alexander Schmidt hypothesised the existence of an enzyme that converts fibrinogen into fibrin in 1872. Prothrombin was discovered by Pekelharing in 1894. Physiology Synthesis Thrombin is produced by the enzymatic cleavage of two sites on prothrombin by activated Factor X (Xa). The activity of factor Xa is great ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Plasminogen
Plasmin is an important enzyme () present in blood that degrades many blood plasma proteins, including fibrin clots. The degradation of fibrin is termed fibrinolysis. In humans, the plasmin protein (in the zymogen form of plasminogen) is encoded by the ''PLG'' gene. Function Plasmin is a serine protease that acts to dissolve fibrin blood clots. Apart from fibrinolysis, plasmin proteolyses proteins in various other systems: It activates collagenases, some mediators of the complement system, and weakens the wall of the Graafian follicle, leading to ovulation. Plasmin is also integrally involved in inflammation. It cleaves fibrin, fibronectin, thrombospondin, laminin, and von Willebrand factor. Plasmin, like trypsin, belongs to the family of serine proteases. Plasmin is released as a zymogen called plasminogen (PLG) from the liver into the systemic circulation. Two major glycoforms of plasminogen are present in humans - type I plasminogen contains two glycosylation mo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Colombia
Colombia (, ; ), officially the Republic of Colombia, is a country in South America with insular regions in North America—near Nicaragua's Caribbean coast—as well as in the Pacific Ocean. The Colombian mainland is bordered by the Caribbean Sea to the north, Venezuela to the east and northeast, Brazil to the southeast, Ecuador and Peru to the south and southwest, the Pacific Ocean to the west, and Panama to the northwest. Colombia is divided into 32 departments and the Capital District of Bogotá, the country's largest city. It covers an area of 1,141,748 square kilometers (440,831 sq mi), and has a population of 52 million. Colombia's cultural heritage—including language, religion, cuisine, and art—reflects its history as a Spanish colony, fusing cultural elements brought by immigration from Europe and the Middle East, with those brought by enslaved Africans, as well as with those of the various Amerindian civilizations that predate colonization. S ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
