A hydroxylated form of the imino acid proline. A deficiency in ASCORBIC ACID can result in impaired hydroxyproline formation.
A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH).
A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.
A hydroxylated derivative of the amino acid LYSINE that is present in certain collagens.
A mixed-function oxygenase that catalyzes the hydroxylation of a prolyl-glycyl containing peptide, usually in PROTOCOLLAGEN, to a hydroxyprolylglycyl-containing-peptide. The enzyme utilizes molecular OXYGEN with a concomitant oxidative decarboxylation of 2-oxoglutarate to SUCCINATE. The enzyme occurs as a tetramer of two alpha and two beta subunits. The beta subunit of procollagen-proline dioxygenase is identical to the enzyme PROTEIN DISULFIDE-ISOMERASES.
A process in which normal lung tissues are progressively replaced by FIBROBLASTS and COLLAGEN causing an irreversible loss of the ability to transfer oxygen into the bloodstream via PULMONARY ALVEOLI. Patients show progressive DYSPNEA finally resulting in death.
A complex of related glycopeptide antibiotics from Streptomyces verticillus consisting of bleomycin A2 and B2. It inhibits DNA metabolism and is used as an antineoplastic, especially for solid tumors.
A disease marked by repeated episodes of increased bone resorption followed by excessive attempts at repair, resulting in weakened, deformed bones of increased mass. The resultant architecture of the bone assumes a mosaic pattern in which the fibers take on a haphazard pattern instead of the normal parallel symmetry.
Acids derived from monosaccharides by the oxidation of the terminal (-CH2OH) group farthest removed from the carbonyl group to a (-COOH) group. (From Stedmans, 26th ed)
Experimentally induced chronic injuries to the parenchymal cells in the liver to achieve a model for LIVER CIRRHOSIS.
The process of embryo initiation in culture from vegetative, non-gametic, sporophytic, or somatic plant cells.
A metalloproteinase which degrades helical regions of native collagen to small fragments. Preferred cleavage is -Gly in the sequence -Pro-Xaa-Gly-Pro-. Six forms (or 2 classes) have been isolated from Clostridium histolyticum that are immunologically cross-reactive but possess different sequences and different specificities. Other variants have been isolated from Bacillus cereus, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa, and species of Vibrio and Streptomyces. EC 3.4.24.3.
A condition due to a dietary deficiency of ascorbic acid (vitamin C), characterized by malaise, lethargy, and weakness. As the disease progresses, joints, muscles, and subcutaneous tissues may become the sites of hemorrhage. Ascorbic acid deficiency frequently develops into SCURVY in young children fed unsupplemented cow's milk exclusively during their first year. It develops also commonly in chronic alcoholism. (Cecil Textbook of Medicine, 19th ed, p1177)
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A rare amino acid found in elastin, formed by condensation of four molecules of lysine into a pyridinium ring.
A biosynthetic precursor of collagen containing additional amino acid sequences at the amino-terminal and carboxyl-terminal ends of the polypeptide chains.
Derivatives of OXALIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that are derived from the ethanedioic acid structure.
An antineoplastic agent derived from BLEOMYCIN.
A fibrillar collagen consisting of three identical alpha1(III) chains that is widely distributed in many tissues containing COLLAGEN TYPE I. It is particularly abundant in BLOOD VESSELS and may play a role in tissues with elastic characteristics.
Placing of a hydroxyl group on a compound in a position where one did not exist before. (Stedman, 26th ed)
Derivatives of ACETIC ACID which contain an hydroxy group attached to the methyl carbon.
Restoration of integrity to traumatized tissue.
A solvent for oils, fats, lacquers, varnishes, rubber waxes, and resins, and a starting material in the manufacturing of organic compounds. Poisoning by inhalation, ingestion or skin absorption is possible and may be fatal. (Merck Index, 11th ed)
The most common form of fibrillar collagen. It is a major constituent of bone (BONE AND BONES) and SKIN and consists of a heterotrimer of two alpha1(I) and one alpha2(I) chains.
Polysaccharides composed of repeating galactose units. They can consist of branched or unbranched chains in any linkages.
A specialized CONNECTIVE TISSUE that is the main constituent of the SKELETON. The principle cellular component of bone is comprised of OSTEOBLASTS; OSTEOCYTES; and OSTEOCLASTS, while FIBRILLAR COLLAGENS and hydroxyapatite crystals form the BONE MATRIX.
Any pathological condition where fibrous connective tissue invades any organ, usually as a consequence of inflammation or other injury.
Bone loss due to osteoclastic activity.
Either of the pair of organs occupying the cavity of the thorax that effect the aeration of the blood.
An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.1.
Surgical union or shunt between ducts, tubes or vessels. It may be end-to-end, end-to-side, side-to-end, or side-to-side.
Disorders affecting amino acid metabolism. The majority of these disorders are inherited and present in the neonatal period with metabolic disturbances (e.g., ACIDOSIS) and neurologic manifestations. They are present at birth, although they may not become symptomatic until later in life.
Heteropolysaccharides which contain an N-acetylated hexosamine in a characteristic repeating disaccharide unit. The repeating structure of each disaccharide involves alternate 1,4- and 1,3-linkages consisting of either N-acetylglucosamine or N-acetylgalactosamine.
Liver disease in which the normal microcirculation, the gross vascular anatomy, and the hepatic architecture have been variably destroyed and altered with fibrous septa surrounding regenerated or regenerating parenchymal nodules.
A non-metal element that has the atomic symbol P, atomic number 15, and atomic weight 31. It is an essential element that takes part in a broad variety of biochemical reactions.
Arabinose is a simple, pentose sugar (a monosaccharide with five carbon atoms) that is a constituent of various polysaccharides and glycosides, particularly found in plant tissues and some microorganisms, and can be metabolized in humans as a source of energy through the pentose phosphate pathway.
Naturally occurring or experimentally induced animal diseases with pathological processes sufficiently similar to those of human diseases. They are used as study models for human diseases.
The first enzyme of the proline degradative pathway. It catalyzes the oxidation of proline to pyrroline-5-carboxylic acid in the presence of oxygen and water. The action is not reversible. The specific activity of proline oxidase increases with age. EC 1.5.3.-.
A plant genus of the family Musaceae, order Zingiberales, subclass Zingiberidae, class Liliopsida.
A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.
Excretion of an excessive amount of OXALATES in the urine.

Variations in 35SO4 incorporation into glycosaminoglycans along canine coronary arteries. A possible index of artery wall stress. (1/1144)

Focal areas of accentuated wall stress along the course of canine coronary arteries may be revealed by the level of 35SO4 incorporation into glycosaminoglycans (GAG). In the anterior descending artery, 35SO4 incorporation in higher in the proximal than in the distal region and may be extraordinarily high as the vessel enters a proximally located muscle bridge and at the takeoff region of multidirectional branches. In the circumflex artery, the incorporation also is higher in the proximal than in the distal region and is high at the genu where the posterior descending artery forms. There are differences in uptake of 35SO4 in vessels even when the arteries arise from the same vascular bed.this was shown by the higher incorporation in the left coronary artery than in the right coronary artery. A general anatomical agreement exists between these sites of high 35SO4 incorporation and previously described locations of interval elastic disruption ans proliferation of intimal connective tissue in the dog.  (+info)

Suppression of experimental abdominal aortic aneurysms by systemic treatment with a hydroxamate-based matrix metalloproteinase inhibitor (RS 132908). (2/1144)

BACKGROUND: Abdominal aortic aneurysms (AAAs) are associated with chronic inflammation, disruption of medial elastin, and increased local production of elastolytic matrix metalloproteinases (MMPs). The purpose of this study was to investigate how treatment with a hydroxamate-based MMP antagonist (RS 132908) might affect the development of experimental AAAs. METHODS: Male Wistar rats underwent intraluminal perfusion of the abdominal aorta with 50 units of porcine pancreatic elastase followed by treatment for 14 days with RS 132908 (100 mg/kg/day subcutaneously; n = 8) or with vehicle alone (n = 6). The external aortic diameter (AD) was measured in millimeters before elastase perfusion and at death, with AAA defined as an increase in AD (DeltaAD) of at least 100%. Aortic wall elastin and collagen concentrations were measured with assays for desmosine and hydroxyproline, and fixed aortic tissues were examined by light microscopy. RESULTS: AAAs developed in all vehicle-treated rats, with a mean AD (+/- SE) that increased from 1.60 +/- 0.03 mm before perfusion to 5.98 +/- 1.02 mm on day 14 (DeltaAD = 276.4 +/- 67.7%). AAAs developed in only five of eight animals (62.5%) after MMP inhibition, with a mean AD that increased from 1.56 +/- 0.05 mm to 3.59 +/- 0.34 mm (DeltaAD = 128.1 +/- 18.7%; P <.05, vs vehicle). The overall inhibition of aortic dilatation attributable to RS 132908 was 53.6 +/- 6.8%. Aortic wall desmosine fell by 85.4% in the vehicle-treated rats (1210.6 +/- 87.8 pmol/sample to 176.7 +/- 33.4 pmol/sample; P <.05) but only by 65.6% in the animals treated with RS 312908 (416.2 +/- 120.5 pmol/sample). In contrast, hydroxyproline was not significantly affected by either elastase perfusion or drug treatment. Microscopic examination revealed the preservation of pericellular elastin and a greater degree of fibrocollagenous wall thickening after MMP inhibition, with no detectable difference in the extent of inflammation. CONCLUSIONS: Systemic MMP inhibition suppresses aneurysmal dilatation in the elastase-induced rodent model of AAA. Consistent with its direct inhibitory effect on various MMPs, RS 132908 promotes the preservation of aortic elastin and appears to enhance a profibrotic response within the aortic wall. Hydroxamate-based MMP antagonists may therefore be useful in the development of pharmacologic approaches to the suppression of AAAs.  (+info)

Altered connective tissue in children with congenital dislocation of the hip. (3/1144)

The umbilical cord was employed as a source of collagen in 10 children with congenital dislocation of hip. The amount of collagen and its solubility were measured in slices of the cords and in the umbilical veins and compared with the values in normal subjects. Both the amount of collagen and its solubility were decreased in children with congenital dislocation of the hip.  (+info)

Effects of pirfenidone on procollagen gene expression at the transcriptional level in bleomycin hamster model of lung fibrosis. (4/1144)

A time course study was carried out to elucidate the mechanisms for antifibrotic effect of pirfenidone (PD). Hamsters were intratracheally (i.t.) instilled with saline (SA) or bleomycin (BL) (7.5 units/kg/5 ml). The animals were fed a diet containing 0.5% PD or the same control diet (CD) without the drug 2 days before and throughout the study. The animals were sacrificed at various times after instillation. The lung hydroxyproline level in BL + CD groups was gradually increased and peaked at 21 days to 181% of the SA + CD control. The BL + PD-treated groups showed a gradual decrease in their lung collagen content, showing a maximum reduction of 40% at day 21. The lung malondialdehyde levels of the BL + CD groups were increased by several-fold of the corresponding SA + CD groups at various times. The lung prolyl hydroxylase (PH) activities in the BL + CD groups were also increased by several-fold of the corresponding SA + CD groups at these time points. The hamsters in the BL + PD showed a gradual decrease in the lung malondialdehyde levels from 10 to 21days compared with their corresponding BL + CD groups. Treatment with PD also reduced the lung PH activities in the BL + PD groups compared with the corresponding BL + CD groups. However, PD failed to manifest any direct inhibitory effect on PH activity in vitro. BL treatment increased the lung procollagen I and III gene expressions in the BL + CD groups by several-fold at varying times compared with the corresponding SA + CD, and treatment with PD in the BL + PD groups significantly down-regulated the BL-induced overexpression of these genes. Studies evaluating the regulation of these genes at the transcriptional level revealed PD significantly reduced the transcription of PC I at 14 days. Our results indicate that the antifibrotic effect of PD was partly due to suppression of the BL-induced inflammatory events and partly due to down-regulation of BL-induced overexpression of lung procollagen I and III genes.  (+info)

A new approach to assessing collagen turnover by using a micro-assay. A highly efficient and rapid turnover of collagen in rat periodontal tissues. (5/1144)

Measurement of [3H]proline incorporation into newly synthesized and mature collagen in connective tissues was used to compare rates and efficiency of collagen turnover. The approach minimizes label-recycling problems. By using a micro-assay to determine hydroxyproline specific radioactivities, a highly efficient and rapid collagen turnover in rat periodontal tissues was demonstrated.  (+info)

T cell independence of bleomycin-induced pulmonary fibrosis. (6/1144)

The role of T cells and cytokines in bleomycin (BLM)-induced fibrosis was evaluated in susceptible and resistant strains of normal and SCID mice. Histology and hydroxyproline analysis showed that BLM induced pulmonary fibrosis in C57BL/6 and (C57BL/6 x BALB/c)F1 mice, whereas BALB/c mice were resistant to the disease. To test whether lymphocytes were required for the induction of BLM-induced pulmonary fibrosis, SCID mice were injected intratracheally with BLM and evaluated for the development of pulmonary inflammation and fibrosis. Similar morphological changes and increases in hydroxyproline were observed in both C57BL/6 SCID and (C57BL/6 x CB.17)F1 SCID animals compared to those seen in wild-type C57BL/6 and (C57BL/6 x BALB/c)F1 mice. In contrast, CB.17 SCID mice, which are genetically similar to BALB/c mice, were resistant to disease induction. Analysis of the cellular infiltrate in BLM-treated C57Bl/6 SCID mice confirmed a lack of T cells in the lungs of SCID mice and demonstrated a pronounced accumulation of eosinophils in areas of developing pulmonary fibrosis. NK cells were significantly elevated in untreated SCID mice and did not increase further after BLM treatment. Analysis of selected cytokines 1 day after initiation of BLM-induced pulmonary fibrosis indicated that the levels of TNF-alpha and IFN-gamma appeared to segregate with fibrosis in both the SCID and wild-type mice. The data demonstrate that T cells are not required for the induction of fibrosis by BLM and suggest that responses by non-lymphoid cells may be sufficient for the induction of fibrosis.  (+info)

The action of the benzopyrones on an experimental model of lymphoedema: a contribution to their mode of action. (7/1144)

A number of preparations containing benzopyrones are used clinically as a therapy for lymphoedema; however, their exact mode of action is not well known. This work presents evidence which indicates that, as in the treatment of thermally induced oedemas, the benzopyrones work by enhancing the lysis of the accumulated proteins. This is evidenced by reduced levels of total protein in the extracellular compartment of the skin, while peptides and amino acids were increased in the serum at 6 and 12 h respectively after the drug's administration. Failure to observe very marked increases in peptides and amino acids at other times in the serum and skin was attributed to the rapid incorporation of these into the large number of maturing phagocytes which enter the lymphoedematous tissues. Likewise, protease activity levels were not elevated as expected. This possibly was the consequence of a number of factors including serum deactivation, inhibition of release and membrane stabilization.  (+info)

Histology and tissue chemistry of tidemark separation in hamsters. (8/1144)

Adult articular cartilage is divided by the tidemark into a deep calcified layer and a more superficial uncalcified layer. Histologic examination of articular cartilage from the knee joint of golden Syrian hamsters 123 days of age or older revealed defects at the tidemark in the tibia. Defects ranged from small separations of the calcified and uncalcified layers along the tidemark to progressively larger defects apparently formed by dissolution. These larger defects appeared as cavities in the noncalcified cartilage, had smooth rather than rough edges, frequently contained coalesced debris, and often resulted in a bulge in the articular surface. Occasionally, these large defects broke through the articular surface. Defects were not observed in tibial cartilage of younger (<90 days old) hamsters or in femoral cartilage from hamsters of any age. Exercise neither protected against nor increased the severity of the defects. Collagen cross-linking by pyridinoline was examined as a function of age and increased from 1,090 to 3,062 micromoles of pyridinoline/mole of hydroxyproline over the period of 1-9 months of age but was not correlated with defect formation. With increasing age, these focal tidemark defects could lead to osteoarthrosis-like cartilage lesions.  (+info)

Hydroxyproline is not a medical term per se, but it is a significant component in the medical field, particularly in the study of connective tissues and collagen. Here's a scientific definition:

Hydroxyproline is a modified amino acid that is formed by the post-translational modification of the amino acid proline in collagen and some other proteins. This process involves the addition of a hydroxyl group (-OH) to the proline residue, which alters its chemical properties and contributes to the stability and structure of collagen fibers. Collagen is the most abundant protein in the human body and is a crucial component of connective tissues such as tendons, ligaments, skin, and bones. The presence and quantity of hydroxyproline can serve as a marker for collagen turnover and degradation, making it relevant to various medical and research contexts, including the study of diseases affecting connective tissues like osteoarthritis, rheumatoid arthritis, and Ehlers-Danlos syndrome.

Collagen is the most abundant protein in the human body, and it is a major component of connective tissues such as tendons, ligaments, skin, and bones. Collagen provides structure and strength to these tissues and helps them to withstand stretching and tension. It is made up of long chains of amino acids, primarily glycine, proline, and hydroxyproline, which are arranged in a triple helix structure. There are at least 16 different types of collagen found in the body, each with slightly different structures and functions. Collagen is important for maintaining the integrity and health of tissues throughout the body, and it has been studied for its potential therapeutic uses in various medical conditions.

Proline is an organic compound that is classified as a non-essential amino acid, meaning it can be produced by the human body and does not need to be obtained through the diet. It is encoded in the genetic code as the codon CCU, CCC, CCA, or CCG. Proline is a cyclic amino acid, containing an unusual secondary amine group, which forms a ring structure with its carboxyl group.

In proteins, proline acts as a structural helix breaker, disrupting the alpha-helix structure and leading to the formation of turns and bends in the protein chain. This property is important for the proper folding and function of many proteins. Proline also plays a role in the stability of collagen, a major structural protein found in connective tissues such as tendons, ligaments, and skin.

In addition to its role in protein structure, proline has been implicated in various cellular processes, including signal transduction, apoptosis, and oxidative stress response. It is also a precursor for the synthesis of other biologically important compounds such as hydroxyproline, which is found in collagen and elastin, and glutamate, an excitatory neurotransmitter in the brain.

Hydroxylysine is a modified form of the amino acid lysine, which is formed by the addition of a hydroxyl group (-OH) to the lysine molecule. This process is known as hydroxylation and is catalyzed by the enzyme lysyl hydroxylase.

In the human body, hydroxylysine is an important component of collagen, which is a protein that provides structure and strength to tissues such as skin, tendons, ligaments, and bones. Hydroxylysine helps to stabilize the triple-helix structure of collagen by forming cross-links between individual collagen molecules.

Abnormalities in hydroxylysine metabolism can lead to various connective tissue disorders, such as Ehlers-Danlos syndrome and osteogenesis imperfecta, which are characterized by joint hypermobility, skin fragility, and bone fractures.

Procollagen-proline dioxygenase is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as an acceptor. This enzyme is involved in the post-translational modification of procollagens, which are the precursors of collagen, a crucial protein found in connective tissues such as tendons, ligaments, and skin.

Procollagen-proline dioxygenase catalyzes the reaction that adds two hydroxyl groups to specific proline residues in the procollagen molecule, converting them into hydroxyprolines. This modification is essential for the proper folding and stabilization of the collagen triple helix structure, which provides strength and resilience to connective tissues.

The enzyme requires iron as a cofactor and molecular oxygen as a substrate, with vitamin C (ascorbic acid) acting as an essential cofactor in the reaction cycle. The proper functioning of procollagen-proline dioxygenase is critical for maintaining the integrity and health of connective tissues, and deficiencies or mutations in this enzyme can lead to various connective tissue disorders, such as scurvy (caused by vitamin C deficiency) or certain forms of osteogenesis imperfecta (a genetic disorder characterized by fragile bones).

Pulmonary fibrosis is a specific type of lung disease that results from the thickening and scarring of the lung tissues, particularly those in the alveoli (air sacs) and interstitium (the space around the air sacs). This scarring makes it harder for the lungs to properly expand and transfer oxygen into the bloodstream, leading to symptoms such as shortness of breath, coughing, fatigue, and eventually respiratory failure. The exact cause of pulmonary fibrosis can vary, with some cases being idiopathic (without a known cause) or related to environmental factors, medications, medical conditions, or genetic predisposition.

Bleomycin is a type of chemotherapeutic agent used to treat various types of cancer, including squamous cell carcinoma, testicular cancer, and lymphomas. It works by causing DNA damage in rapidly dividing cells, which can inhibit the growth and proliferation of cancer cells.

Bleomycin is an antibiotic derived from Streptomyces verticillus and is often administered intravenously or intramuscularly. While it can be effective in treating certain types of cancer, it can also have serious side effects, including lung toxicity, which can lead to pulmonary fibrosis and respiratory failure. Therefore, bleomycin should only be used under the close supervision of a healthcare professional who is experienced in administering chemotherapy drugs.

Osteitis deformans, also known as Paget's disease of bone, is a chronic disorder of the bone characterized by abnormal turnover and remodeling of the bone. In this condition, the bone becomes enlarged, thickened, and deformed due to excessive and disorganized bone formation and resorption.

The process begins when the bone-remodeling cycle is disrupted, leading to an imbalance between the activity of osteoclasts (cells that break down bone) and osteoblasts (cells that form new bone). In Paget's disease, osteoclasts become overactive and increase bone resorption, followed by an overzealous response from osteoblasts, which attempt to repair the damage but do so in a disorganized manner.

The affected bones can become weakened, prone to fractures, and may cause pain, deformities, or other complications such as arthritis, hearing loss, or neurological symptoms if the skull or spine is involved. The exact cause of Paget's disease remains unknown, but it is believed that genetic and environmental factors play a role in its development.

Early diagnosis and treatment can help manage the symptoms and prevent complications associated with osteitis deformans. Treatment options include medications to slow down bone turnover, pain management, and orthopedic interventions when necessary.

Uronic acids are a type of organic compound that are carboxylic acids derived from sugars (carbohydrates). They are formed by the oxidation of the primary alcohol group (-CH2OH) on a pentose sugar, resulting in a carboxyl group (-COOH) at that position.

The most common uronic acid is glucuronic acid, which is derived from glucose. Other examples include galacturonic acid (derived from galactose), iduronic acid (derived from glucose or galactose), and mannuronic acid (derived from mannose).

Uronic acids play important roles in various biological processes, such as the formation of complex carbohydrates like glycosaminoglycans, which are major components of connective tissues. They also serve as important intermediates in the metabolism of sugars and other carbohydrates.

Experimental liver cirrhosis refers to a controlled research setting where various factors and substances are intentionally introduced to induce liver cirrhosis in animals or cell cultures. The purpose is to study the mechanisms, progression, potential treatments, and prevention strategies for liver cirrhosis. This could involve administering chemicals, drugs, alcohol, viruses, or manipulating genes associated with liver damage and fibrosis. It's important to note that results from experimental models may not directly translate to human conditions, but they can provide valuable insights into disease pathophysiology and therapeutic development.

Plant somatic embryogenesis techniques refer to the scientific methods used to induce and produce embryos from plant somatic cells, which are not involved in sexual reproduction. These techniques involve the culture of isolated plant cells or tissues on nutrient-rich media under controlled conditions that promote embryo development. The resulting embryos can be germinated into plants, which are genetically identical to the parent plant, a process known as clonal propagation.

Somatic embryogenesis techniques have various applications in plant biotechnology, including large-scale propagation of elite varieties, genetic transformation, and cryopreservation of plant genetic resources. The ability to produce embryos from somatic cells also has potential implications for understanding the fundamental mechanisms of plant development and evolution.

Microbial collagenase is not a medical term per se, but it does refer to an enzyme that is used in various medical and research contexts. Collagenases are a group of enzymes that break down collagen, a structural protein found in connective tissues such as skin, tendons, and ligaments. Microbial collagenase is a type of collagenase that is produced by certain bacteria, such as Clostridium histolyticum.

In medical terms, microbial collagenase is used in various therapeutic and research applications, including:

1. Wound healing: Microbial collagenase can be used to break down and remove necrotic tissue from wounds, which can help promote healing and prevent infection.
2. Dental applications: Collagenases have been used in periodontal therapy to remove calculus and improve the effectiveness of root planing and scaling procedures.
3. Research: Microbial collagenase is a valuable tool for researchers studying the structure and function of collagen and other extracellular matrix proteins. It can be used to digest tissue samples, allowing scientists to study the individual components of the extracellular matrix.

It's important to note that while microbial collagenase has many useful applications, it must be used with care, as excessive or improper use can damage healthy tissues and cause adverse effects.

Ascorbic acid deficiency is a condition that occurs when a person does not consume or absorb adequate amounts of ascorbic acid, also known as Vitamin C. This essential nutrient plays a crucial role in the production of collagen, a protein that helps to support blood vessel, tendon, ligament, and bone health. It is also involved in the absorption of iron and the synthesis of certain neurotransmitters.

Ascorbic acid deficiency can lead to a number of symptoms and complications. In its early stages, it may cause fatigue, weakness, and joint pain. As the deficiency progresses, it can lead to more serious conditions such as scurvy, a potentially life-threatening disease characterized by anemia, gum disease, skin hemorrhages, and poor wound healing.

Scurvy is now rare in developed countries where access to fresh fruits and vegetables, which are rich sources of vitamin C, is readily available. However, it can still occur in individuals who follow restrictive diets or have malabsorption disorders that prevent them from properly absorbing the nutrient. In these cases, supplementation with ascorbic acid may be necessary to prevent deficiency and its associated complications.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Desmosine is a unique amino acid that is not found in proteins, but instead is formed through the cross-linking of lysine residues in collagen and elastin fibers. These fibers are important components of the extracellular matrix, providing strength and elasticity to tissues such as skin, lungs, and blood vessels.

Desmosine is formed through a series of chemical reactions involving the oxidation of lysine residues and their subsequent condensation with other amino acids. This process creates cross-links between collagen and elastin fibers, which helps to stabilize their structure and enhance their mechanical properties.

Abnormalities in desmosine levels have been associated with various diseases, including emphysema, Marfan syndrome, and Ehlers-Danlos syndrome. Measuring desmosine levels in urine or tissue samples can provide valuable insights into the health of collagen and elastin fibers and help diagnose and monitor these conditions.

Procollagen is the precursor protein of collagen, which is a major structural protein in the extracellular matrix of various connective tissues, such as tendons, ligaments, skin, and bones. Procollagen is synthesized inside the cell (in the rough endoplasmic reticulum) and then processed by enzymes to remove specific segments, resulting in the formation of tropocollagen, which are the basic units of collagen fibrils.

Procollagen consists of three polypeptide chains (two alpha-1 and one alpha-2 chain), each containing a central triple-helical domain flanked by non-helical regions at both ends. These non-helical regions, called propeptides, are cleaved off during the processing of procollagen to tropocollagen, allowing the individual collagen molecules to align and form fibrils through covalent cross-linking.

Abnormalities in procollagen synthesis or processing can lead to various connective tissue disorders, such as osteogenesis imperfecta (brittle bone disease) and Ehlers-Danlos syndrome (a group of disorders characterized by joint hypermobility, skin hyperextensibility, and tissue fragility).

Oxalates, also known as oxalic acid or oxalate salts, are organic compounds that contain the functional group called oxalate. Oxalates are naturally occurring substances found in various foods such as spinach, rhubarb, nuts, and seeds. They can also be produced by the body as a result of metabolism.

In the body, oxalates can bind with calcium and other minerals to form crystals, which can accumulate in various tissues and organs, including the kidneys. This can lead to the formation of kidney stones, which are a common health problem associated with high oxalate intake or increased oxalate production in the body.

It is important for individuals with a history of kidney stones or other kidney problems to monitor their oxalate intake and limit consumption of high-oxalate foods. Additionally, certain medical conditions such as hyperoxaluria, a rare genetic disorder that causes increased oxalate production in the body, may require medical treatment to reduce oxalate levels and prevent complications.

I'm sorry for any confusion, but "Peplomycin" is not a widely recognized or established medical term. It appears that it might be a term related to a specific type of antibiotic drug called "Pleuromutilin." Pleuromutilins are a class of antibiotics derived from certain types of fungi. Peplomycin could potentially be a specific formulation, brand name, or experimental version of a pleuromutilin antibiotic, but without more context, it is difficult to provide a precise definition. I would recommend consulting the original source or seeking additional information for clarification.

Collagen Type III, also known as Collagen III Alpha 1 (COL3A1), is a type of collagen that is found in various connective tissues throughout the body. It is a fibrillar collagen that is produced by fibroblasts and is a major component of reticular fibers, which provide structural support to organs such as the liver, spleen, and lymph nodes. Collagen Type III is also found in the walls of blood vessels, the skin, and the intestinal tract.

Mutations in the COL3A1 gene can lead to a rare genetic disorder called Ehlers-Danlos syndrome type IV, which is characterized by fragile and elastic skin, easy bruising, and spontaneous rupture of blood vessels. Collagen Type III has been studied for its potential role in various other medical conditions, including fibrosis, cancer, and cardiovascular disease.

Hydroxylation is a biochemical process that involves the addition of a hydroxyl group (-OH) to a molecule, typically a steroid or xenobiotic compound. This process is primarily catalyzed by enzymes called hydroxylases, which are found in various tissues throughout the body.

In the context of medicine and biochemistry, hydroxylation can have several important functions:

1. Drug metabolism: Hydroxylation is a common way that the liver metabolizes drugs and other xenobiotic compounds. By adding a hydroxyl group to a drug molecule, it becomes more polar and water-soluble, which facilitates its excretion from the body.
2. Steroid hormone biosynthesis: Hydroxylation is an essential step in the biosynthesis of many steroid hormones, including cortisol, aldosterone, and the sex hormones estrogen and testosterone. These hormones are synthesized from cholesterol through a series of enzymatic reactions that involve hydroxylation at various steps.
3. Vitamin D activation: Hydroxylation is also necessary for the activation of vitamin D in the body. In order to become biologically active, vitamin D must undergo two successive hydroxylations, first in the liver and then in the kidneys.
4. Toxin degradation: Some toxic compounds can be rendered less harmful through hydroxylation. For example, phenol, a toxic compound found in cigarette smoke and some industrial chemicals, can be converted to a less toxic form through hydroxylation by enzymes in the liver.

Overall, hydroxylation is an important biochemical process that plays a critical role in various physiological functions, including drug metabolism, hormone biosynthesis, and toxin degradation.

Glycolates are a type of chemical compound that contain the group COOCH2, which is derived from glycolic acid. In a medical context, glycolates are often used in dental and medical materials as they can be biodegradable and biocompatible. For example, they may be used in controlled-release drug delivery systems or in bone cement. However, it's important to note that some glycolate compounds can also be toxic if ingested or otherwise introduced into the body in large amounts.

Wound healing is a complex and dynamic process that occurs after tissue injury, aiming to restore the integrity and functionality of the damaged tissue. It involves a series of overlapping phases: hemostasis, inflammation, proliferation, and remodeling.

1. Hemostasis: This initial phase begins immediately after injury and involves the activation of the coagulation cascade to form a clot, which stabilizes the wound and prevents excessive blood loss.
2. Inflammation: Activated inflammatory cells, such as neutrophils and monocytes/macrophages, infiltrate the wound site to eliminate pathogens, remove debris, and release growth factors that promote healing. This phase typically lasts for 2-5 days post-injury.
3. Proliferation: In this phase, various cell types, including fibroblasts, endothelial cells, and keratinocytes, proliferate and migrate to the wound site to synthesize extracellular matrix (ECM) components, form new blood vessels (angiogenesis), and re-epithelialize the wounded area. This phase can last up to several weeks depending on the size and severity of the wound.
4. Remodeling: The final phase of wound healing involves the maturation and realignment of collagen fibers, leading to the restoration of tensile strength in the healed tissue. This process can continue for months to years after injury, although the tissue may never fully regain its original structure and function.

It is important to note that wound healing can be compromised by several factors, including age, nutrition, comorbidities (e.g., diabetes, vascular disease), and infection, which can result in delayed healing or non-healing chronic wounds.

Carbon tetrachloride is a colorless, heavy, and nonflammable liquid with a mild ether-like odor. Its chemical formula is CCl4. It was previously used as a solvent and refrigerant, but its use has been largely phased out due to its toxicity and ozone-depleting properties.

Inhalation, ingestion, or skin contact with carbon tetrachloride can cause harmful health effects. Short-term exposure can lead to symptoms such as dizziness, headache, nausea, and vomiting. Long-term exposure has been linked to liver and kidney damage, as well as an increased risk of cancer.

Carbon tetrachloride is also a potent greenhouse gas and contributes to climate change. Its production and use are regulated by international agreements aimed at protecting human health and the environment.

Collagen Type I is the most abundant form of collagen in the human body, found in various connective tissues such as tendons, ligaments, skin, and bones. It is a structural protein that provides strength and integrity to these tissues. Collagen Type I is composed of three alpha chains, two alpha-1(I) chains, and one alpha-2(I) chain, arranged in a triple helix structure. This type of collagen is often used in medical research and clinical applications, such as tissue engineering and regenerative medicine, due to its excellent mechanical properties and biocompatibility.

Galactans are a type of complex carbohydrates known as oligosaccharides that are composed of galactose molecules. They can be found in certain plants, including beans, lentils, and some fruits and vegetables. In the human body, galactans are not digestible and can reach the colon intact, where they may serve as a substrate for fermentation by gut bacteria. This can lead to the production of short-chain fatty acids, which have been shown to have various health benefits. However, in some individuals with irritable bowel syndrome or other functional gastrointestinal disorders, consumption of galactans may cause digestive symptoms such as bloating, gas, and diarrhea.

"Bone" is the hard, dense connective tissue that makes up the skeleton of vertebrate animals. It provides support and protection for the body's internal organs, and serves as a attachment site for muscles, tendons, and ligaments. Bone is composed of cells called osteoblasts and osteoclasts, which are responsible for bone formation and resorption, respectively, and an extracellular matrix made up of collagen fibers and mineral crystals.

Bones can be classified into two main types: compact bone and spongy bone. Compact bone is dense and hard, and makes up the outer layer of all bones and the shafts of long bones. Spongy bone is less dense and contains large spaces, and makes up the ends of long bones and the interior of flat and irregular bones.

The human body has 206 bones in total. They can be further classified into five categories based on their shape: long bones, short bones, flat bones, irregular bones, and sesamoid bones.

Fibrosis is a pathological process characterized by the excessive accumulation and/or altered deposition of extracellular matrix components, particularly collagen, in various tissues and organs. This results in the formation of fibrous scar tissue that can impair organ function and structure. Fibrosis can occur as a result of chronic inflammation, tissue injury, or abnormal repair mechanisms, and it is a common feature of many diseases, including liver cirrhosis, lung fibrosis, heart failure, and kidney disease.

In medical terms, fibrosis is defined as:

"The process of producing scar tissue (consisting of collagen) in response to injury or chronic inflammation in normal connective tissue. This can lead to the thickening and stiffening of affected tissues and organs, impairing their function."

Bone resorption is the process by which bone tissue is broken down and absorbed into the body. It is a normal part of bone remodeling, in which old or damaged bone tissue is removed and new tissue is formed. However, excessive bone resorption can lead to conditions such as osteoporosis, in which bones become weak and fragile due to a loss of density. This process is carried out by cells called osteoclasts, which break down the bone tissue and release minerals such as calcium into the bloodstream.

A lung is a pair of spongy, elastic organs in the chest that work together to enable breathing. They are responsible for taking in oxygen and expelling carbon dioxide through the process of respiration. The left lung has two lobes, while the right lung has three lobes. The lungs are protected by the ribcage and are covered by a double-layered membrane called the pleura. The trachea divides into two bronchi, which further divide into smaller bronchioles, leading to millions of tiny air sacs called alveoli, where the exchange of gases occurs.

Alkaline phosphatase (ALP) is an enzyme found in various body tissues, including the liver, bile ducts, digestive system, bones, and kidneys. It plays a role in breaking down proteins and minerals, such as phosphate, in the body.

The medical definition of alkaline phosphatase refers to its function as a hydrolase enzyme that removes phosphate groups from molecules at an alkaline pH level. In clinical settings, ALP is often measured through blood tests as a biomarker for various health conditions.

Elevated levels of ALP in the blood may indicate liver or bone diseases, such as hepatitis, cirrhosis, bone fractures, or cancer. Therefore, physicians may order an alkaline phosphatase test to help diagnose and monitor these conditions. However, it is essential to interpret ALP results in conjunction with other diagnostic tests and clinical findings for accurate diagnosis and treatment.

Surgical anastomosis is a medical procedure that involves the connection of two tubular structures, such as blood vessels or intestines, to create a continuous passage. This technique is commonly used in various types of surgeries, including vascular, gastrointestinal, and orthopedic procedures.

During a surgical anastomosis, the ends of the two tubular structures are carefully prepared by removing any damaged or diseased tissue. The ends are then aligned and joined together using sutures, staples, or other devices. The connection must be secure and leak-free to ensure proper function and healing.

The success of a surgical anastomosis depends on several factors, including the patient's overall health, the location and condition of the structures being joined, and the skill and experience of the surgeon. Complications such as infection, bleeding, or leakage can occur, which may require additional medical intervention or surgery.

Proper postoperative care is also essential to ensure the success of a surgical anastomosis. This may include monitoring for signs of complications, administering medications to prevent infection and promote healing, and providing adequate nutrition and hydration.

Inborn errors of amino acid metabolism refer to genetic disorders that affect the body's ability to properly break down and process individual amino acids, which are the building blocks of proteins. These disorders can result in an accumulation of toxic levels of certain amino acids or their byproducts in the body, leading to a variety of symptoms and health complications.

There are many different types of inborn errors of amino acid metabolism, each affecting a specific amino acid or group of amino acids. Some examples include:

* Phenylketonuria (PKU): This disorder affects the breakdown of the amino acid phenylalanine, leading to its accumulation in the body and causing brain damage if left untreated.
* Maple syrup urine disease: This disorder affects the breakdown of the branched-chain amino acids leucine, isoleucine, and valine, leading to their accumulation in the body and causing neurological problems.
* Homocystinuria: This disorder affects the breakdown of the amino acid methionine, leading to its accumulation in the body and causing a range of symptoms including developmental delay, intellectual disability, and cardiovascular problems.

Treatment for inborn errors of amino acid metabolism typically involves dietary restrictions or supplementation to manage the levels of affected amino acids in the body. In some cases, medication or other therapies may also be necessary. Early diagnosis and treatment can help prevent or minimize the severity of symptoms and health complications associated with these disorders.

Glycosaminoglycans (GAGs) are long, unbranched polysaccharides composed of repeating disaccharide units. They are a major component of the extracellular matrix and connective tissues in the body. GAGs are negatively charged due to the presence of sulfate and carboxyl groups, which allows them to attract positively charged ions and water molecules, contributing to their ability to retain moisture and maintain tissue hydration and elasticity.

GAGs can be categorized into four main groups: heparin/heparan sulfate, chondroitin sulfate/dermatan sulfate, keratan sulfate, and hyaluronic acid. These different types of GAGs have varying structures and functions in the body, including roles in cell signaling, inflammation, and protection against enzymatic degradation.

Heparin is a highly sulfated form of heparan sulfate that is found in mast cells and has anticoagulant properties. Chondroitin sulfate and dermatan sulfate are commonly found in cartilage and contribute to its resiliency and ability to withstand compressive forces. Keratan sulfate is found in corneas, cartilage, and bone, where it plays a role in maintaining the structure and function of these tissues. Hyaluronic acid is a large, nonsulfated GAG that is widely distributed throughout the body, including in synovial fluid, where it provides lubrication and shock absorption for joints.

Liver cirrhosis is a chronic, progressive disease characterized by the replacement of normal liver tissue with scarred (fibrotic) tissue, leading to loss of function. The scarring is caused by long-term damage from various sources such as hepatitis, alcohol abuse, nonalcoholic fatty liver disease, and other causes. As the disease advances, it can lead to complications like portal hypertension, fluid accumulation in the abdomen (ascites), impaired brain function (hepatic encephalopathy), and increased risk of liver cancer. It is generally irreversible, but early detection and treatment of underlying causes may help slow down its progression.

Phosphorus is an essential mineral that is required by every cell in the body for normal functioning. It is a key component of several important biomolecules, including adenosine triphosphate (ATP), which is the primary source of energy for cells, and deoxyribonucleic acid (DNA) and ribonucleic acid (RNA), which are the genetic materials in cells.

Phosphorus is also a major constituent of bones and teeth, where it combines with calcium to provide strength and structure. In addition, phosphorus plays a critical role in various metabolic processes, including energy production, nerve impulse transmission, and pH regulation.

The medical definition of phosphorus refers to the chemical element with the atomic number 15 and the symbol P. It is a highly reactive non-metal that exists in several forms, including white phosphorus, red phosphorus, and black phosphorus. In the body, phosphorus is primarily found in the form of organic compounds, such as phospholipids, phosphoproteins, and nucleic acids.

Abnormal levels of phosphorus in the body can lead to various health problems. For example, high levels of phosphorus (hyperphosphatemia) can occur in patients with kidney disease or those who consume large amounts of phosphorus-rich foods, and can contribute to the development of calcification of soft tissues and cardiovascular disease. On the other hand, low levels of phosphorus (hypophosphatemia) can occur in patients with malnutrition, vitamin D deficiency, or alcoholism, and can lead to muscle weakness, bone pain, and an increased risk of infection.

Arabinose is a simple sugar or monosaccharide that is a stereoisomer of xylose. It is a pentose, meaning it contains five carbon atoms, and is classified as a hexahydroxyhexital because it has six hydroxyl (-OH) groups attached to the carbon atoms. Arabinose is found in various plant polysaccharides, such as hemicelluloses, gums, and pectic substances. It can also be found in some bacteria and yeasts, where it plays a role in their metabolism. In humans, arabinose is not an essential nutrient and must be metabolized by specific enzymes if consumed.

Animal disease models are specialized animals, typically rodents such as mice or rats, that have been genetically engineered or exposed to certain conditions to develop symptoms and physiological changes similar to those seen in human diseases. These models are used in medical research to study the pathophysiology of diseases, identify potential therapeutic targets, test drug efficacy and safety, and understand disease mechanisms.

The genetic modifications can include knockout or knock-in mutations, transgenic expression of specific genes, or RNA interference techniques. The animals may also be exposed to environmental factors such as chemicals, radiation, or infectious agents to induce the disease state.

Examples of animal disease models include:

1. Mouse models of cancer: Genetically engineered mice that develop various types of tumors, allowing researchers to study cancer initiation, progression, and metastasis.
2. Alzheimer's disease models: Transgenic mice expressing mutant human genes associated with Alzheimer's disease, which exhibit amyloid plaque formation and cognitive decline.
3. Diabetes models: Obese and diabetic mouse strains like the NOD (non-obese diabetic) or db/db mice, used to study the development of type 1 and type 2 diabetes, respectively.
4. Cardiovascular disease models: Atherosclerosis-prone mice, such as ApoE-deficient or LDLR-deficient mice, that develop plaque buildup in their arteries when fed a high-fat diet.
5. Inflammatory bowel disease models: Mice with genetic mutations affecting intestinal barrier function and immune response, such as IL-10 knockout or SAMP1/YitFc mice, which develop colitis.

Animal disease models are essential tools in preclinical research, but it is important to recognize their limitations. Differences between species can affect the translatability of results from animal studies to human patients. Therefore, researchers must carefully consider the choice of model and interpret findings cautiously when applying them to human diseases.

Proline oxidase is an enzyme that catalyzes the chemical reaction of oxidizing proline to Δ^1^-pyrroline-5-carboxylate (P5C) and hydrogen peroxide (H2O2). The reaction is a part of the catabolic pathway for proline utilization in some organisms.

The systematic name for this enzyme is L-proline:oxygen oxidoreductase (deaminating, decarboxylating). It belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as an acceptor. This enzyme participates in arginine and proline metabolism.

"Musa" is the genus name for bananas and plantains in the botanical classification system. It belongs to the family Musaceae and includes over 70 species of tropical herbaceous plants that are native to Southeast Asia. The fruit produced by these plants is also commonly referred to as "bananas" or "plantains," depending on the specific variety and its culinary use.

However, I believe you may have been looking for a medical term, and I apologize for any confusion. In that case, I should note that "Musa" is not a recognized medical term in English. If you have any further questions or need clarification on a different medical term, please let me know!

"Wistar rats" are a strain of albino rats that are widely used in laboratory research. They were developed at the Wistar Institute in Philadelphia, USA, and were first introduced in 1906. Wistar rats are outbred, which means that they are genetically diverse and do not have a fixed set of genetic characteristics like inbred strains.

Wistar rats are commonly used as animal models in biomedical research because of their size, ease of handling, and relatively low cost. They are used in a wide range of research areas, including toxicology, pharmacology, nutrition, cancer, cardiovascular disease, and behavioral studies. Wistar rats are also used in safety testing of drugs, medical devices, and other products.

Wistar rats are typically larger than many other rat strains, with males weighing between 500-700 grams and females weighing between 250-350 grams. They have a lifespan of approximately 2-3 years. Wistar rats are also known for their docile and friendly nature, making them easy to handle and work with in the laboratory setting.

Hyperoxaluria is a medical condition characterized by an excessive excretion of oxalate in the urine. Oxalate is a naturally occurring substance found in some foods and can also be produced by the body. When oxalate combines with calcium in the urine, it can form kidney stones or calcium oxalate deposits in the kidneys and other tissues, leading to kidney damage or systemic oxalosis. There are three types of hyperoxaluria: primary, secondary, and enteric. Primary hyperoxaluria is caused by genetic defects that affect the body's ability to regulate oxalate production, while secondary hyperoxaluria results from increased dietary intake or absorption of oxalate, or from other medical conditions. Enteric hyperoxaluria occurs in individuals with malabsorption syndromes, such as inflammatory bowel disease or after gastric bypass surgery, where excessive amounts of oxalate are absorbed from the gut into the bloodstream and excreted in the urine.

2S,4R)-4-Hydroxyproline, or L-hydroxyproline (C5H9O3N), is an amino acid, abbreviated as Hyp or O, e.g., in Protein Data Bank. ... Hydroxyproline is also found in the walls of oomycetes, fungus-like protists related to diatoms. (2S,4S)-cis-4-Hydroxyproline ... Hydroxyproline differs from proline by the presence of a hydroxyl (OH) group attached to the gamma carbon atom. Hydroxyproline ... Hydroxyproline is found in few proteins other than collagen. For this reason, hydroxyproline content has been used as an ...
Other names in common use include hydroxyproline epimerase, hydroxyproline 2-epimerase, and L-hydroxyproline epimerase. This ... In enzymology, a 4-hydroxyproline epimerase (EC 5.1.1.8) is an enzyme that catalyzes the chemical reaction trans-4-hydroxy-L- ... Adams E, Norton IL (May 1964). "Purification and properties of inducible hydroxyproline 2-epimerase from Pseudomonas". The ... The systematic name of this enzyme class is 4-hydroxyproline 2-epimerase. ...
... hydroxyproline Thus, the two substrates of this enzyme are UDP-N-acetylglucosamine and Skp1-protein-hydroxyproline, whereas its ... Skp1-hydroxyproline GlcNAc-transferase, and UDP-GlcNAc:hydroxyproline polypeptide GlcNAc-transferase. CM; Morris, HR; Panico, M ... Teng-Umnuay P, van der Wel H, West CM (1999). "Identification of a UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase in the ... The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:[Skp1-protein]-hydroxyproline N-acetyl-D-glucosaminyl- ...
The enzyme trans-L-3-hydroxyproline dehydratase (EC 4.2.1.77) catalyzes the chemical reaction trans-L-3-hydroxyproline ⇌ {\ ... This enzyme is also called trans-L-3-hydroxyproline hydro-lyase. Ramaswamy SG (1983). "Conversion of 3-hydroxyproline to ... The systematic name of this enzyme class is trans-L-3-hydroxyproline hydro-lyase (Δ1-pyrroline-2-carboxylate-forming). ...
Hydroxyproline. This imino acid differs from proline due to a hydroxyl group on carbon 4. Hypusine. This amino acid is obtained ... and in hydroxyproline the hydroxylation of proline is critical for maintaining connective tissues. Another example is the ...
Adams E, Goldstone A (December 1960). "Hydroxyproline metabolism. IV. Enzymatic synthesis of gamma-hydroxyglutamate from Delta ...
"Hydroxyproline metabolism. III. Enzymatic synthesis of hydroxyproline from Delta1-pyrroline-3-hydroxy-5-carboxylate". The ...
Specific sets of hydroxyproline O-β-galactosyltransferases, β-1,3-galactosyltransferases, β-1,6-galactosyltransferases, α- ... Proline residues in the protein backbone can be hydroxylated to Hydroxyproline (O) depending on the surrounding amino acids. ... Ogawa-Ohnishi, Mari; Matsubayashi, Yoshikatsu (2015-03-01). "Identification of three potent hydroxyproline O- ... and Analysis of Hydroxyproline-Rich Glycoproteins". Plant Physiology. 153 (2): 485-513. doi:10.1104/pp.110.156554. ISSN 0032- ...
For example, hydroxyproline , is synthesised from proline. Another example is selenomethionine). Non-proteinogenic amino acids ... Hydroxyproline, generated by hydroxylation of proline, is a major component of the connective tissue collagen. Hypusine in the ... while hydroxyproline is made by a post translational modification of proline. Microorganisms and plants synthesize many ...
This particular enzyme catalyzes the formation of (2S, 4R)-4-hydroxyproline, a compound that represents the most prevalent post ... Prolyl hydroxylase catalyzes the formation of hydroxyproline. The modification has a significant impact on the stability of ... Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen". Biochemical and Biophysical Research ... 4-hydroxyproline + succinate + CO2 The mechanism for the reaction is similar to that of other dioxygenases, and occurs in two ...
Shaffer, Karl J.; Taylor, Carol M. (2006-08-01). "β-Glycosides of Hydroxyproline via an Umpolung Approach". Organic Letters. 8 ...
1974). "Defective hydroxyproline metabolism in type II hyperprolinemia". Biochemical Medicine. 10 (4): 329-36. doi:10.1016/0006 ... "Genetic evidence for a common enzyme catalyzing the second step in the degradation of proline and hydroxyproline". J. Clin. ...
"An assay for hydroxyproline and proline on one sample and a simplified method for hydroxyproline". Analytical Biochemistry. 63 ... The only proteinogenic amino acid of this type is proline, although the related non-proteinogenic amino acids hydroxyproline ... Stout, E.R.; Fritz, G.J. (1966). "Role of Oxygen Fixation in Hydroxyproline Biosynthesis by Etiolated Seedlings". Plant ... Myhill, D.; Jackson, D.S. (1963). "Separation of proline and hydroxyproline using thin-layer chromatography". Analytical ...
"Entrez Gene: TULP1 tubby like protein 1". Powles TJ, Rosset G, Leese CL, Bondy PK (1977). "Early morning hydroxyproline ...
The protein is one of the enzymes (4-hydroxy-2-oxoglutarate aldolase) involved in metabolism of hydroxyproline to glyoxylate. ... The enzyme overactivity can form excessive glyoxylate from hydroxyproline. Glyoxylate is catabolised to oxalate, resulting in ...
The core-specific lectin contains hydroxyproline, hydroxylysine, and glucosylgalactosylhydroxylysine residues". J Biol Chem. ...
Collagen consists of both 3‐hydroxyproline and 4‐hydroxyproline residues. Hydroxylation occurs at the γ-C atom, forming ... This is due to the fact that collagen makes up about 25-35% of the protein in our bodies and contains a hydroxyproline at ... hydroxyproline (Hyp), which stabilizes the secondary structure of collagen due to the strong electronegative effects of oxygen ...
Two amino acids are alkanolamines, formally speaking: serine and hydroxyproline. Veratridine and veratrine Tropane alkaloids ...
Min JH, Yang H, Ivan M, Gertler F, Kaelin WG, Pavletich NP (2002). "Structure of an HIF-1alpha -pVHL complex: hydroxyproline ... hydroxyproline recognition in signaling". Science. 296 (5574): 1886-9. Bibcode:2002Sci...296.1886M. doi:10.1126/science.1073440 ... "Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL". Nature. 417 (6892): 975-8. Bibcode:2002Natur. ...
Pyridinoline Elevated levels of serum and urinary hydroxyproline are also found. Bone scans are useful in determining the ...
Min JH, Yang H, Ivan M, Gertler F, Kaelin WG, Pavletich NP (2002). "Structure of an HIF-1alpha -pVHL complex: hydroxyproline ...
... hydroxyproline recognition in signaling". Science. 296 (5574): 1886-9. Bibcode:2002Sci...296.1886M. doi:10.1126/science.1073440 ... "Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL". Nature. 417 (6892): 975-8. doi:10.1038/ ...
In nature, proline, hydroxyproline, pipecolic acid and sarcosine are well-known secondary amino acids. Proline is the only ... In protein, hydroxyproline is incorporated into protein by hydroxylation of proline. Pipecolic acid, a heavier analog of ... Ninhydrin tests of proline and hydroxyproline give yellow results. In enzymology, a N-methyl-L-amino-acid oxidase is an oxidase ...
... hydroxyproline recognition in signaling". Science. 296 (5574): 1886-9. doi:10.1126/science.1073440. PMID 12004076. S2CID ...
Kato H, Matsumura Y, Maeda H (May 1988). "Isolation and identification of hydroxyproline analogues of bradykinin in human urine ...
Wheat cells also release hydroxyproline glycoprotein (HRGP) in their cell walls. Secretion of HRGP is dependent on the signal ...
It was found that the elastic, collagen, and hydroxyproline components were higher in upper abdomen regions compared to lower ... The elastic, collagen, and hydroxyproline components were sampled and then studied. ...
This enzyme catalyses the following chemical reaction Hydrolysis of Xaa!Pro dipeptides; also acts on aminoacyl-hydroxyproline ...
... the latter tend to have similar proline and hydroxyproline contents to mammals. The lower proline and hydroxyproline contents ... Proline or hydroxyproline constitute about 1/6 of the total sequence. With glycine accounting for the 1/3 of the sequence, this ... The most common motifs in the amino acid sequence of collagen are glycine-proline-X and glycine-X-hydroxyproline, where X is ... Hydroxyproline derived from proline Hydroxylysine derived from lysine - depending on the type of collagen, varying numbers of ...
... hydroxyproline recognition in signaling". Science. 296 (5574): 1886-9. Bibcode:2002Sci...296.1886M. doi:10.1126/science.1073440 ...
2S,4R)-4-Hydroxyproline, or L-hydroxyproline (C5H9O3N), is an amino acid, abbreviated as Hyp or O, e.g., in Protein Data Bank. ... Hydroxyproline is also found in the walls of oomycetes, fungus-like protists related to diatoms. (2S,4S)-cis-4-Hydroxyproline ... Hydroxyproline differs from proline by the presence of a hydroxyl (OH) group attached to the gamma carbon atom. Hydroxyproline ... Hydroxyproline is found in few proteins other than collagen. For this reason, hydroxyproline content has been used as an ...
lt;b>Hydroxyproline parameters</b> for simulations ...
... Change Category: No Category. Dairy and Egg Products. Spices and Herbs. Baby Foods. ...
Extensins are members of the cell wall hydroxyproline-rich glycoprotein (HRGP) superfamily that form covalently cross-linked ... Identification of the Abundant Hydroxyproline-Rich Glycoproteins in the Root Walls of Wild-Type Arabidopsis, an ext3 Mutant ... Extensins are members of the cell wall hydroxyproline-rich glycoprotein (HRGP) superfamily that form covalently cross-linked ... "Identification of the Abundant Hydroxyproline-Rich Glycoproteins in the Root Walls of Wild-Type Arabidopsis, an ext3 Mutant ...
Click the button below to add the Boc-O-benzyl-L-trans-4-hydroxyproline dicyclohexylammonium salt 1 g to your wish list. ... Boc-O-benzyl-L-trans-4-hydroxyproline dicyclohexylammonium salt. (Boc-L-Hyp(Bzl)-OH DCHA) ...
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The concentration of Hydroxyproline(Hyp) in the samples is then determined by comparing the OD of the samples to the standard ... The microtiter plate provided in this kit has been pre-coated with Hydroxyproline(Hyp) protein. Standards or samples are added ... Hyp (Hydroxyproline) ELISA Kit - 96 wells plate. https://www.gentaur.be/shop/0855-elk7835-96t-hyp-hydroxyproline-elisa-kit-96- ... to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Hydroxyproline(Hyp). Next,Avidin ...
The concentration of Hydroxyproline(Hyp) in the samples is then determined by comparing the OD of the samples to the standard ... The microtiter plate provided in this kit has been pre-coated with Hydroxyproline(Hyp) protein. Standards or samples are added ... Hyp (Hydroxyproline) ELISA Kit - 96 wells plate. https://www.gentaur.be/shop/0855-elk7835-96t-hyp-hydroxyproline-elisa-kit-96- ... to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Hydroxyproline(Hyp). Next,Avidin ...
In-depth correlation analysis demonstrates that 4-hydroxyproline at the Yaa position of Gly-Xaa-Yaa repeats dominantly ... 4-hydroxyproline (4Hyp). However, positional difference in their stabilizing effect at the Xaa or Yaa position of collagenous ...
Hydroxyproline for Assay is available from Karlan upon request. ... The MSDS of QuantiChrom™Hydroxyproline for Assay is available ... QuantiChrom™Hydroxyproline Assay Kit-100T - 1 kit is backordered and will ship as soon as it is back in stock. ... The MSDS of QuantiChrom™Hydroxyproline for Assay is available from Karlan upon request. ...
24-hour urine. Refrigerate during collection. Patient should be on a collagen-free diet for 3 days prior to collection ...
... hydroxyproline has an essential role in collagen stability. Testing hydroxyproline in the serum and in the urine is common. ... Although serum hydroxyproline and urinary hydroxyproline measurements are strongly correlated, urinary hydroxyproline ... The reference range of hydroxyproline is as follows: [1] * Total hydroxyproline in the urine among those aged 18-21 years - 13- ... Hydroxyproline can be tested in the serum and in the urine. The serum level of hydroxyproline excretion correlates well with ...
... hydroxyproline has an essential role in collagen stability. Testing hydroxyproline in the serum and in the urine is common. ... Although serum hydroxyproline and urinary hydroxyproline measurements are strongly correlated, urinary hydroxyproline ... The reference range of hydroxyproline is as follows: [1] * Total hydroxyproline in the urine among those aged 18-21 years - 13- ... Hydroxyproline can be tested in the serum and in the urine. The serum level of hydroxyproline excretion correlates well with ...
Hydroxyproline is the main component of collagen in mammals (Gordon and Hahn 2010), and both proline and hydroxyproline are ... Hydroxyproline-rich glycoproteins are key protein constituents of the cell wall (Lee et al. 2007). Recent discoveries have ... However, the content of hydroxyproline was 4 to 5 times higher.. *Metschnikowia sp. lysates can be used in the form of mono- ... However, the content of hydroxyproline HPro was 4 to 5 times higher. The results of this study show that yeast lysates are an ...
Information, view and buy high quality L-Hydroxy proline, 99%+, 51-35-4, from Otto Chemie Pvt Ltd, Mumbai, India. Trans-4-Hydroxy-L-proline is a versatile reagent for the synthesis of neuroexcitatory kainoids and antifungal echinocandins. Also employed in the synthesis of chiral ligands for enantioselective ethylation of aldehydes. trans-4-Hydroxy-L-proline is a natural constituent of animal structural proteins such as collagen and elastin. A versatile reagent for the synthesis of neuroexcitatory kainoids and antifungal echinocandins.
The hydroxyproline concentration was measured by modified spectrophotometery. The collected data was analyzed using student t ... Objective-To determine the effect of ultrasound therapy on hydroxyproline (HP) content in superficial digital flexor tendon ( ... The hydroxyproline concentration was measured by modified spectrophotometery. The collected data was analyzed using student t ... Sharifi, D., Mohitmafi, S., Rassouli, A., Shams, G. Effect of Ultrasound Therapy on the Hydroxyproline Content in Experimental ...
Hydroxyproline:. *Children: 0 to 5. *Adults: not detected. Isoleucine:. *Children: 37 to 140 ...
Hydroxyproline. Dipalmitoyl hydroxyproline is a lipophilic collagen supporting active shown to hydrate, firm and reduce the ... Natural amino acid hydroxyproline smooths out fine lines and wrinkles. Glycablend. ™, our potent seed complex of chia, ... Dipalmitoyl hydroxyproline, Salvia hispanica (chia) seed oil, Tocopheryl acetate (vitamin E), Vaccinium myrtillus (blueberry) ...
Hydroxyproline. A collagen compound, included here to support healthy skin appearance.[3].. Advertisement ...
Hydroxyproline, L-Proline, Glyceryl Caprylate, Triethyl Citrate, Benzoic Acid, Phenoxyethanol ...
... Prejano M.; ... Amidohydrolases; Bacillus cereus; Bacterial Proteins; Binding Sites; Biocatalysis; Hydrogen Bonding; Hydroxyproline; Molecular ...
Immunolocalization and Changes of Hydroxyproline-Rich Glycoproteins During Symbiotic Germination of Dendrobium officinale.JPEG ... Hydroxyproline-rich glycoproteins (HRGPs) are abundant cell wall components involved in mycorrhizal symbiosis, but little is ... Image_2_Immunolocalization and Changes of Hydroxyproline-Rich Glycoproteins During Symbiotic Germination of Dendrobium ... Image_2_Immunolocalization and Changes of Hydroxyproline-Rich Glycoproteins During Symbiotic Germination of Dendrobium ...
Here we propose the concept of an electro-microbial route to uncouple food production from photosynthesis, thereby enabling production of nutritious food in space without the need to grow plant-based crops. In the proposed process, carbon dioxide is fixed into ethanol using either chemical catalysis or microbial carbon fixation, and the ethanol created is used as a carbon source for yeast to synthesize food for human or animal consumption. The process depends upon technologies that can utilize electrical energy to fix carbon into ethanol and uses an optimized strain of the yeast Saccharomyces cerevisiae to produce high-quality, food-grade, single-cell protein using ethanol as the sole carbon source in a minimal medium. Crops performing photosynthesis require months to mature and are challenging to grow under the conditions found in space, whereas the electro-microbial process could generate significant quantities of food on demand with potentially high yields and productivities. In this paper we explore
Hydroxyproline: 14%. *Glutamic acid: 11%. The exact amino acid composition varies depending on the type of animal tissue used ...
Hydroxyproline. Nutrient Val: 0 g. Additional Fortification: Tag Name: HYP. Rounded to dec points: 3. Alcohol, ethyl. Nutrient ...
Hydroxyproline is a component of the bone collagen. During degradation of bone, it is released into the serum and reaches the ... Today, serum hydroxyproline is considered a nonspecific marker of bone turnover, since it is derived from the degradation of ... Until the early 1990s, urinary hydroxyproline was one of the main bone resorption markers available, but this assay lacked ... From a practical standpoint, another major drawback of urinary hydroxyproline was the necessity for dietary restrictions on ...
Hydroxyproline assay. Frozen lung tissue samples were incubated in 250 μl PBS, after which 250 μl of 12 N HCl was added, and ... G) Relative change in collagen deposition (assessed by hydroxyproline level) upon MHV68 infection. (H) Relative change in Tgfb ... C) Increased collagen deposition (assessed by hydroxyproline level) in lungs of PINK1-deficient mice after infection. (D) ... E) Significant increase in collagen deposition (assessed by hydroxyproline level) and Col1a1 expression in PINK1-deficient ...
Know nutrition and calorie facts in 100gms of Soymilk (All flavors), enhanced. Includes - total fat, carbohydrates, proteins, vitamins and minerals.
Hydroxyproline. 0.03 Proline. 0.91 g. Serine. 0.86 g. Tyrosine. 0.77 g. Methionine. 0.52 g ...
  • As collagen is an essential protein found mostly in animal products, we've developed our Plant Collagen to mirror the amino acid profile of bovine collagen, using plant-based glycine, proline and hydroxyproline. (myprotein.com)
  • Hydroxyproline differs from proline by the presence of a hydroxyl (OH) group attached to the gamma carbon atom. (wikipedia.org)
  • Hydroxyproline is produced by hydroxylation of the amino acid proline by the enzyme prolyl hydroxylase following protein synthesis (as a post-translational modification). (wikipedia.org)
  • Hydroxyproline and proline play key roles for collagen stability. (wikipedia.org)
  • Two isomeric forms of hydroxyproline have been identified in collagenTrans-4-hydroxy-L-proline is found in type I and type III collagen, whereas higher amounts of trans-3-hydroxy-L-proline are found in type IV collagen. (medscape.com)
  • Hydroxyproline rich glycoproteins (HRGPs) are also found in plant cell walls. (wikipedia.org)
  • Identification of the Abundant Hydroxyproline-Rich Glycoproteins in th" by Yuning Chen, Dening Ye et al. (umass.edu)
  • Hydroxyproline-rich glycoproteins (HRGPs) are abundant cell wall components involved in mycorrhizal symbiosis, but little is known about their function in orchid mycorrhizal association. (figshare.com)
  • Extensins are members of the cell wall hydroxyproline-rich glycoprotein (HRGP) superfamily that form covalently cross-linked networks in primary cell walls. (umass.edu)
  • Increased serum and urine levels of hydroxyproline have also been demonstrated in Paget's disease. (wikipedia.org)
  • Dipalmitoyl hydroxyproline is a lipophilic collagen supporting active shown to hydrate, firm and reduce the appearance of wrinkles, promoting supple, younger looking skin. (trilogyproducts.com)
  • Way beyond your average lip product, this proven-effective solution is formulated with an exceptional emollient blend of Dipalmitoyl Hydroxyproline, Vitamin C, Vitamin E, Shea Butter, and Vegetable Olus Oil from Olives. (pevonia.co.uk)
  • Hyperhydroxyprolinemia is a benign condition caused by a defect in 4-hydroxyproline dehydrogenase. (medscape.com)
  • Analysis of hydroxyproline (collagen) and pyridinoline (collagen cross-links) in biopsies prepared for routine histological evaluation with OCT compound was performed. (cdc.gov)
  • Testing hydroxyproline in the serum and in the urine is common. (medscape.com)
  • Hydroxyproline can be tested in the serum and in the urine. (medscape.com)
  • The ratio of hydroxyproline/creatinine in a fresh specimen of early morning urine, considered the total urinary hydroxyproline, is the best index of collagen breakdown in metastatic bone disease. (medscape.com)
  • Although serum hydroxyproline and urinary hydroxyproline measurements are strongly correlated, urinary hydroxyproline measurement in 24-hour or spot urine is easier to collect. (medscape.com)
  • Spot urine testing is measurement of choice in screening for bony involvement by malignancy because collagen intake does not influence hydroxyproline/creatinine. (medscape.com)
  • There is a general consensus that collagen stability is largely maintained by Pro and its major hydroxylated form, 4-hydroxyproline (4Hyp). (qxmd.com)
  • As a major part of collagen, hydroxyproline has an essential role in collagen stability. (medscape.com)
  • Although it is not directly incorporated into proteins, hydroxyproline comprises roughly 4% of all amino acids found in animal tissue, an amount greater than seven other amino acids that are translationally incorporated. (wikipedia.org)
  • The serum level of hydroxyproline excretion correlates well with its urinary level. (medscape.com)
  • [ 1 ] However, urinary hydroxyproline better discriminates (x 100) between normal and metastatic disease of the bone. (medscape.com)
  • Klein L. Urinary Hydroxyproline during Late Pregnancy and Postpartum Involution. (medscape.com)
  • The concentration of Hydroxyproline(Hyp) in the samples is then determined by comparing the OD of the samples to the standard curve. (gentaur.fr)
  • The hydroxyproline concentration was measured by modified spectrophotometery. (ivsajournals.com)
  • Hydroxyproline is found in few proteins other than collagen. (wikipedia.org)
  • However, the mammalian proteins elastin and argonaute 2 have collagen-like domains in which hydroxyproline is formed. (wikipedia.org)
  • For this reason, hydroxyproline content has been used as an indicator to determine collagen and/or gelatin amount. (wikipedia.org)
  • However, the content of hydroxyproline HPro was 4 to 5 times higher. (ncsu.edu)
  • Effect of Ultrasound Therapy on the Hydroxyproline Content in Experimental Tendon Injuries in Horses. (ivsajournals.com)
  • The MCHC is assayed for hydroxyproline content. (acuatlanta.net)
  • Hydroxyproline is a major component of the protein collagen, comprising roughly 13.5% of mammalian collagen. (wikipedia.org)
  • Hydroxyproline is also found in the walls of oomycetes, fungus-like protists related to diatoms. (wikipedia.org)
  • 2S,4S)-cis-4-Hydroxyproline is found in the toxic cyclic peptides from Amanita mushrooms (e.g., phalloidin). (wikipedia.org)
  • In-depth correlation analysis demonstrates that 4-hydroxyproline at the Yaa position of Gly-Xaa-Yaa repeats dominantly stabilizes collagen triple helix. (qxmd.com)
  • A portion of the hydrolysate was analyzed for hydroxyproline using high performance liquid chromatography with collagen type I as the standard. (cdc.gov)
  • This measurement is preferable to free serum hydroxyproline measurement in this setting. (medscape.com)
  • Infused with retinol and hydroxyproline, this concentrated face treatment sheet mask combats the signs of aging and dryness and delivers essential moisture to boost suppleness and radiance, revealing a more youthful complexion. (dermstore.com)
  • Dipalmitoyl Hydroxyproline - An ingredient made with amino acids - the building blocks of life. (colormebeautiful.com)
  • The serum level of hydroxyproline excretion correlates well with its urinary level. (medscape.com)
  • The urinary excretion of hydroxyproline (Hyp), abundant in collagen protein, may serve as a biomarker of habitual collagen intake, assisting with investigations of current interest in the role of dietary collagen intake in supporting the synthesis of collagenous body tissues. (humankinetics.com)
  • 2. Although pretreatment values for urinary total hydroxyproline excretion and cardiac output were considerably increased in some patients, there was no correlation between these two variables in the group as a whole. (portlandpress.com)
  • 3. [Urinary hydroxyproline excretion in primary hyperparathyroidism. (nih.gov)
  • Proline hydroxylase activity was measured as the hydroxyproline: proline ratio after incubation of lung extract with C-14- proline. (cdc.gov)
  • Hydroxyproline rich glycoproteins (HRGPs) are also found in plant cell walls. (wikipedia.org)
  • Developmental localization and the role of hydroxyproline rich glycoproteins during somatic embryogenesis of banana (Musaspp. (biomedcentral.com)
  • The present study was planned to investigate the ultrastructural changes and hydroxyproline level in the lungs of the mice induced. (sdu.edu.tr)
  • Hydroxyproline is produced by hydroxylation of the amino acid proline by the enzyme prolyl hydroxylase following protein synthesis (as a post-translational modification). (wikipedia.org)
  • [8] Hydroxylation occurs at the γ-C atom, forming hydroxyproline (Hyp), which stabilizes the secondary structure of collagen due to the strong electronegative effects of oxygen. (wikipedia.org)
  • A cell free system capable of catalyzing both the incorporation of proline into a peptide chain and its subsequent hydroxylation to hydroxyproline has been obtained from rat lung tissue. (cdc.gov)
  • It was subsequently shown that the increase in stability is primarily through stereoelectronic effects and that hydration of the hydroxyproline residues provides little or no additional stability. (wikipedia.org)
  • Collagen consists of both 3‐hydroxyproline and 4‐hydroxyproline residues. (wikipedia.org)
  • Increased serum and urine levels of hydroxyproline have also been demonstrated in Paget's disease. (wikipedia.org)
  • Testing hydroxyproline in the serum and in the urine is common. (medscape.com)
  • Hydroxyproline can be tested in the serum and in the urine. (medscape.com)
  • This measurement is preferable to free serum hydroxyproline measurement in this setting. (medscape.com)
  • Hydroxyproline is a major component of the protein collagen, comprising roughly 13.5% of mammalian collagen. (wikipedia.org)
  • L-Hydroxyproline is a common non-standard protein amino acid, which has high application value as the main raw material of antiviral drug atazanavir. (industrialchemgroup.com)
  • HYDROXYPROLINE O-ARABINOSYLTRANSFERASEs (HPATs) initiate a post-translational protein modification (Hyp-Ara) found abundantly on cell wall structural proteins. (omicsdi.org)
  • This is due to the fact that collagen makes up about 25-35% of the protein in our bodies and contains a hydroxyproline at almost every 3rd residue in its amino acid sequence. (wikipedia.org)
  • Recent evidence has shown that the degradation of 4-hydroxyproline (Hyp), generated from endogenous and dietary sources, leads to an increase in glycolate and oxalate levels in plasma and urine. (wfu.edu)
  • exposed KKAy lungs was confirmed with immunohistochemistry, tissue hydroxyproline content, and tissue mRNA expression of fibrosis-associated genes ( Ccl11 , Il13 , and Mmp12 ). (nih.gov)
  • Lung fibrosis was confirmed by increased hydroxyproline levels in. (cdc.gov)
  • In the left ventricle of untreated SHR compared with age- and sex-matched normotensive WKY rats we found more extensive interstitial and perivascular fibrosis, an increased collagen volume fraction, an increased hydroxyproline concentration and an increased number of mast cells. (lww.com)
  • In the left ventricles of quinapril-treated SHR compared with those of untreated SHR we found a marked decrease in fibrosis, a lower collagen volume fraction, a lower hydroxyproline concentration and fewer mast cells. (lww.com)
  • However, the mammalian proteins elastin and argonaute 2 have collagen-like domains in which hydroxyproline is formed. (wikipedia.org)
  • IMPORTANCE Hydroxyproline is abundant in proteins in animal and plant tissues and serves as a carbon and a nitrogen source for bacteria in diverse environments, including the rhizosphere, compost, and the mammalian gut. (mcmaster.ca)
  • Following 4 weeks of bleomycin treatment, the lungs were examined histologically (using light and electron microscopes) and the hydroxyproline level was measured at 4th, 6th, 8th, and 10th weeks of the experiment. (sdu.edu.tr)
  • The metabolism of hydroxyproline was examined by a combination of HPLC and ion chromatography/mass spectrometry techniques. (nih.gov)
  • Store at room testosterone propionate acid, hydroxyproline, and zinc levels texas, New Jersey and Florida. (wirelessdesignmag.com)
  • Hydroxyproline O-arabinosyltransferase mutants oppositely alter tip growth in Arabidopsis thaliana and Physcomitrella patens. (omicsdi.org)
  • This analysis included bronchoalveolar lavage (BAL) for cell and fluid analysis, and tissue for pathology, immunohistology, mRNA, and hydroxyproline. (nih.gov)
  • Spot urine testing is measurement of choice in screening for bony involvement by malignancy because collagen intake does not influence hydroxyproline/creatinine. (medscape.com)
  • Elucidating the genetics of hydroxyproline catabolism will aid in the annotation of these genes in other genomes and metagenomic libraries. (mcmaster.ca)
  • Physcomitrella hpat mutants lack cell-wall associated hydroxyproline arabinosides and can be rescued with exogenous cellulose, while global expression profiling shows that cell wall-associated genes are severely misexpressed, implicating a defect in cell wall formation during tip growth. (omicsdi.org)
  • Angiotensin-converting enzyme activity and angiotensin (Ang)II and hydroxyproline contents of the LV were determined. (nih.gov)
  • The investigators concluded this after finding that 4-hydroxyproline in the Yaa position has better positive correlation with collagen's denaturation temperature than does the total amount of hydroxyproline (including 3- and 4-hydroxyproline) in the Xaa position. (medscape.com)
  • Applicable to meat and meat products containing less than 0,5 % (m/m) hydroxyproline. (iso.org)
  • These hydroxyprolines serve as the attachment points for glycan chains which are added as post-translational modifications. (wikipedia.org)
  • L-Hydroxyproline is usually used as a food additive (used as a relatively small amount of sweetener) and a relatively large amount of pharmaceutical penicillene side chain intermediates. (industrialchemgroup.com)
  • Glyoxylate production was substantially greater when mitochondria were incubated with hydroxyproline in comparison with proline. (nih.gov)