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Proinsulin
Proinsulin is the prohormone precursor to insulin made in the beta cells of the Pancreatic Islets, specialized regions of the pancreas. In humans, proinsulin is encoded by the ''INS'' gene. The pancreatic islets only secrete between 1% and 3% of proinsulin intact. However, because proinsulin has a longer half life than insulin, it can account for anywhere from 5–30% of the insulin-like structures circulating in the blood. There are higher concentrations of proinsulin after meals and lower levels when a person is fasting. Additionally, while proinsulin and insulin have structural differences, proinsulin does demonstrate some affinity for the insulin receptor. Due to the relative similarities in structure, proinsulin can produce between 5% and 10% of the metabolic activity similarly induced by insulin. Proinsulin is the final single chain protein structure secreted by cells before cleavage into mature insulin. Proinsulin was discovered by Professor Donald F. Steiner of the Un ...
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Proinsulin Annotated
Proinsulin is the prohormone precursor to insulin made in the beta cells of the Pancreatic islets, Pancreatic Islets, specialized regions of the pancreas. In humans, proinsulin is encoded by the ''INS'' gene. The pancreatic islets only secrete between 1% and 3% of proinsulin intact. However, because proinsulin has a longer half life than insulin, it can account for anywhere from 5–30% of the insulin-like structures circulating in the blood. There are higher concentrations of proinsulin after meals and lower levels when a person is fasting. Additionally, while proinsulin and insulin have structural differences, proinsulin does demonstrate some affinity for the insulin receptor. Due to the relative similarities in structure, proinsulin can produce between 5% and 10% of the metabolic activity similarly induced by insulin. Proinsulin is the final single chain protein structure secreted by cells before cleavage into mature insulin. Proinsulin was discovered by Professor Donald F. Stei ...
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Proinsulin 3
Proinsulin is the prohormone precursor to insulin made in the beta cells of the Pancreatic Islets, specialized regions of the pancreas. In humans, proinsulin is encoded by the ''INS'' gene. The pancreatic islets only secrete between 1% and 3% of proinsulin intact. However, because proinsulin has a longer half life than insulin, it can account for anywhere from 5–30% of the insulin-like structures circulating in the blood. There are higher concentrations of proinsulin after meals and lower levels when a person is fasting. Additionally, while proinsulin and insulin have structural differences, proinsulin does demonstrate some affinity for the insulin receptor. Due to the relative similarities in structure, proinsulin can produce between 5% and 10% of the metabolic activity similarly induced by insulin. Proinsulin is the final single chain protein structure secreted by cells before cleavage into mature insulin. Proinsulin was discovered by Professor Donald F. Steiner of the Univers ...
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Prohormone
A prohormone is a committed precursor of a hormone consisting of peptide hormones synthesized together that has a minimal hormonal effect by itself because of its expression-suppressing structure, often created by protein folding and binding additional peptide chains to certain ends, that makes hormone receptor binding sites located on its peptide hormone chain segments inaccessible. Prohormones can travel the blood stream as a hormone in an inactivated form, ready to be activated later in the cell by post-translational modification. The body naturally produces prohormones as a way to regulate hormone expression, making them an optimal storage and transportation unit for inactive hormones. Once prohormones are needed to be expressed, prohormone convertase, a protein, cleaves the prohormones and separates them into one or more active hormones. Often in nature, this cleaving process happens immediately, and a prohormone is quickly converted to a set of one or more peptide hormone ...
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C-peptide
The connecting peptide, or C-peptide, is a short 31-amino-acid polypeptide that connects insulin's A-chain to its B-chain in the proinsulin molecule. In the context of diabetes or hypoglycemia, a measurement of C-peptide blood serum levels can be used to distinguish between different conditions with similar clinical features. In the insulin synthesis pathway, first preproinsulin is translocated into the endoplasmic reticulum of beta cells of the pancreas with an A-chain, a C-peptide, a B-chain, and a signal sequence. The signal sequence is cleaved from the N-terminus of the peptide by a signal peptidase, leaving proinsulin. After proinsulin is packaged into vesicles in the Golgi apparatus (beta-granules), the C-peptide is removed, leaving the A-chain and B-chain bound together by disulfide bonds, that constitute the insulin molecule. History Proinsulin C-peptide was first described in 1967 in connection with the discovery of the insulin biosynthesis pathway. Isolation o ...
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Insulin Receptor
The insulin receptor (IR) is a transmembrane receptor that is activated by insulin, IGF-I, IGF-II and belongs to the large class of receptor tyrosine kinase. Metabolically, the insulin receptor plays a key role in the regulation of glucose homeostasis; a functional process that under degenerate conditions may result in a range of clinical manifestations including diabetes and cancer. Insulin signalling controls access to blood glucose in body cells. When insulin falls, especially in those with high insulin sensitivity, body cells begin only to have access to lipids that do not require transport across the membrane. So, in this way, insulin is the key regulator of fat metabolism as well. Biochemically, the insulin receptor is encoded by a single gene , from which alternate splicing during transcription results in either IR-A or IR-B isoforms. Downstream post-translational events of either isoform result in the formation of a proteolytically cleaved α and β subunit, which up ...
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Secretory Vesicles
Secretion is the movement of material from one point to another, such as a secreted chemical substance from a cell or gland. In contrast, excretion is the removal of certain substances or waste products from a cell or organism. The classical mechanism of cell secretion is via secretory portals at the plasma membrane called porosomes. Porosomes are permanent cup-shaped lipoprotein structures embedded in the cell membrane, where secretory vesicles transiently dock and fuse to release intra-vesicular contents from the cell. Secretion in bacterial species means the transport or translocation of effector molecules. For example: proteins, enzymes or toxins (such as cholera toxin in pathogenic bacteria e.g. ''Vibrio cholerae'') from across the interior (cytoplasm or cytosol) of a bacterial cell to its exterior. Secretion is a very important mechanism in bacterial functioning and operation in their natural surrounding environment for adaptation and survival. In eukaryotic cells Mecha ...
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Bovine
Bovines (subfamily Bovinae) comprise a diverse group of 10 genera of medium to large-sized ungulates, including Bos, cattle, bison, African buffalo, Bubalus, water buffalos, and the four-horned and spiral-horned antelopes. The members of this group are classified into loose Tribe (biology), tribes rather than formal subgroups, as the evolutionary relationships within the groups are still uncertain. General characteristics include cloven hoof, cloven hooves and usually at least one of the sexes of a species having Horn (anatomy), true horns. The largest Extant species, extant bovine is the gaur. In many countries, bovid milk and meat is used as food by humans. Cattle are kept as livestock almost everywhere except in parts of India and Nepal, where they are Cattle in religion and mythology, considered sacred by most Hindus. Bovids are used as draft animals and as riding animals. Small breeds of domestic bovid, such as the Miniature Zebu, are kept as pets. Bovid leather is durable an ...
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Porcine
The pig (''Sus domesticus''), also called swine (: swine) or hog, is an omnivorous, domesticated, even-toed, hoofed mammal. It is named the domestic pig when distinguishing it from other members of the genus '' Sus''. Some authorities consider it a subspecies of ''Sus scrofa'' (the wild boar or Eurasian boar); other authorities consider it a distinct species. Pigs were domesticated in the Neolithic, both in China and in the Near East (around the Tigris Basin). When domesticated pigs arrived in Europe, they extensively interbred with wild boar but retained their domesticated features. Pigs are farmed primarily for meat, called pork. The animal's skin or hide is used for leather. China is the world's largest pork producer, followed by the European Union and then the United States. Around 1.5 billion pigs are raised each year, producing some 120 million tonnes of meat, often cured as bacon. Some are kept as pets. Pigs have featured in human culture since Neolithic times, ap ...
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Iatrogenic
Iatrogenesis is the causation of a disease, a harmful complication, or other ill effect by any medical activity, including diagnosis, intervention, error, or negligence." Iatrogenic", ''Merriam-Webster.com'', Merriam-Webster, Inc., accessed 27 Jun 2020. First used in this sense in 1924, the term was introduced to sociology in 1976 by Ivan Illich, alleging that industrialized societies impair quality of life by overmedicalizing life."iatrogenesis"
''A Dictionary of Sociology'', . updated 31 May 2020.
Iatrogenesis may thus include mental suffering via medical beliefs or a practitioner's statements. Some iatrogen ...
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Endoprotease
Endopeptidase or endoproteinase are proteolytic peptidases that break peptide bonds of nonterminal amino acids (i.e. within the molecule), in contrast to exopeptidases, which break peptide bonds from end-pieces of terminal amino acids. For this reason, endopeptidases cannot break down peptides into monomers, while exopeptidases can break down proteins into monomers. A particular case of endopeptidase is the oligopeptidase, whose substrates are oligopeptides instead of proteins. They are usually very specific for certain amino acids. Examples of endopeptidases include: * Trypsin - cuts after Arg or Lys, unless followed by Pro. Very strict. Works best at pH 8. * Chymotrypsin - cuts after Phe, Trp, or Tyr, unless followed by Pro. Cuts more slowly after His, Met or Leu. Works best at pH 8. * Elastase - cuts after Ala, Gly, Ser, or Val, unless followed by Pro. * Thermolysin - cuts ''before'' Ile, Met, Phe, Trp, Tyr, or Val, unless ''preceded'' by Pro. Sometimes cuts after Ala, Asp, ...
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Type 1 Diabetes
Type 1 diabetes (T1D), formerly known as juvenile diabetes, is an autoimmune disease that occurs when the body's immune system destroys pancreatic cells (beta cells). In healthy persons, beta cells produce insulin. Insulin is a hormone required by the body to store and convert blood sugar into energy. T1D results in high blood sugar levels in the body prior to treatment. Common symptoms include frequent urination, increased thirst, increased hunger, weight loss, and other complications. Additional symptoms may include blurry vision, tiredness, and slow wound healing (owing to impaired blood flow). While some cases take longer, symptoms usually appear within weeks or a few months. The cause of type 1 diabetes is not completely understood, but it is believed to involve a combination of genetic and environmental factors. The underlying mechanism involves an autoimmune destruction of the insulin-producing beta cells in the pancreas. Diabetes is diagnosed by testing the leve ...
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