Aspartic Acid Endopeptidases
Aspartic Acid
Endopeptidases
Neprilysin
Aspartic Acid Proteases
Serine Endopeptidases
Amino Acid Sequence
Thiorphan
Molecular Sequence Data
Protease Inhibitors
PHEX Phosphate Regulating Neutral Endopeptidase
Cysteine Endopeptidases
Amino Acids
Substrate Specificity
Mutagenesis, Site-Directed
Asparagine
Binding Sites
Base Sequence
Glycopeptides
Pepstatins
Mutation
Peptides
Sequence Homology, Amino Acid
Hydrogen-Ion Concentration
Structure-Activity Relationship
Glutamates
Peptide Fragments
Cloning, Molecular
Models, Molecular
Amino Acid Substitution
Isoaspartic Acid
Cathepsin E
Protein Conformation
Chromatography, High Pressure Liquid
Escherichia coli
Neurotensin
Alanine
Lysostaphin
Pepsin A
Catalysis
Electrophoresis, Polyacrylamide Gel
Cathepsin D
Glycine
Sequence Alignment
Serine
Peptide Hydrolases
Protein Structure, Tertiary
Catalytic Domain
Carboxypeptidases
Protein Processing, Post-Translational
Trypsin
Atrial Natriuretic Factor
Point Mutation
Glutamic Acid
Chromatography, Gel
Protein Binding
Aspartate-tRNA Ligase
Thermolysin
Proline
Enzyme Stability
Cathepsin B
Protein Structure, Secondary
Chromatography, Ion Exchange
Cattle
DNA, Complementary
DNA Primers
Carbohydrates
Conserved Sequence
Cathepsins
Aminopeptidases
Transfection
Plasmids
Substance P
Chromatography
Threonine
Crystallography, X-Ray
Enkephalin, Leucine
Kidney
Bradykinin
Botulinum Toxins, Type A
Aspartate-Semialdehyde Dehydrogenase
Cell Membrane
Phosphorylation
Membrane Proteins
Flavobacterium
Bacillus
Stereoisomerism
Molecular Structure
Chemistry
Chemical Phenomena
Forensic Sciences
Swine
Sequence Homology, Nucleic Acid
ATP-Dependent Endopeptidases
Castor Bean
Keratin-2
Plant Proteins
Polymerase Chain Reaction
Chromatography, Paper
Zinc
Proteins
Circular Dichroism
Mass Spectrometry
Recombinant Fusion Proteins
Carboxypeptidases A
Papain
Rabbits
Mutation, Missense
Propionates
Enzyme Activation
Chymotrypsin
2S Albumins, Plant
COS Cells
Peptide Mapping
Radiometric Dating
Cyanogen Bromide
Amino Acid Motifs
DNA
Macromolecular Substances
Restriction Mapping
Homoserine Dehydrogenase
Familial Hypophosphatemic Rickets
Hydrogen Bonding
Angiotensin-Converting Enzyme Inhibitors
Chymosin
Cell Wall
Mutagenesis
Peptidyl-Dipeptidase A
Chromatography, DEAE-Cellulose
Ketosteroids
Temperature
Blotting, Western
Phenylalanine
Isoflurophate
Sequence Analysis, DNA
Isoelectric Focusing
Pepsinogens
Leucyl Aminopeptidase
Cells, Cultured
Oligodeoxyribonucleotides
Kinins
RNA, Messenger
Electrophoresis
Codon
Aminocaproates
Seed Storage Proteins
Isoelectric Point
Cathepsin C
Saccharomyces cerevisiae
Muramidase
Stabilization from autoproteolysis and kinetic characterization of the human T-cell leukemia virus type 1 proteinase. (1/2015)
We have developed a system for expression and purification of wild-type human T-cell leukemia virus type 1 (HTLV-1) proteinase to attain sufficient quantities for structural, kinetic, and biophysical investigations. However, similar to the human immunodeficiency virus type 1 (HIV-1) proteinase, HTLV-1 proteinase also undergoes autoproteolysis rapidly upon renaturation to produce two products. The site of this autoproteolytic cleavage was mapped, and a resistant HTLV-1 proteinase construct (L40I) as well as another construct, wherein the two cysteine residues were exchanged to alanines, were expressed and purified. Oligopeptide substrates representing the naturally occurring cleavage sites in HTLV-1 were good substrates of the HTLV-1 proteinase. The kinetic parameters kcat and Km were nearly identical for all the three enzymes. Although three of four peptides representing HTLV-1 proteinase cleavage sites were fairly good substrates of HIV-1 proteinase, only two of nine peptides representing HIV-1 proteinase cleavage sites were hydrolyzed by the HTLV-1 proteinase, suggesting substantial differences in the specificity of the two enzymes. The large difference in the specificity of the two enzymes was also demonstrated by inhibition studies. Of the several inhibitors of HIV-1 or other retroviral proteinases that were tested on HTLV-1 proteinase, only two inhibit the enzyme with a Ki lower than 100 nM. (+info)Fus3p and Kss1p control G1 arrest in Saccharomyces cerevisiae through a balance of distinct arrest and proliferative functions that operate in parallel with Far1p. (2/2015)
In Saccharomyces cerevisiae, mating pheromones activate two MAP kinases (MAPKs), Fus3p and Kss1p, to induce G1 arrest prior to mating. Fus3p is known to promote G1 arrest by activating Far1p, which inhibits three Clnp/Cdc28p kinases. To analyze the contribution of Fus3p and Kss1p to G1 arrest that is independent of Far1p, we constructed far1 CLN strains that undergo G1 arrest from increased activation of the mating MAP kinase pathway. We find that Fus3p and Kss1p both control G1 arrest through multiple functions that operate in parallel with Far1p. Fus3p and Kss1p together promote G1 arrest by repressing transcription of G1/S cyclin genes (CLN1, CLN2, CLB5) by a mechanism that blocks their activation by Cln3p/Cdc28p kinase. In addition, Fus3p and Kss1p counteract G1 arrest through overlapping and distinct functions. Fus3p and Kss1p together increase the expression of CLN3 and PCL2 genes that promote budding, and Kss1p inhibits the MAP kinase cascade. Strikingly, Fus3p promotes proliferation by a novel function that is not linked to reduced Ste12p activity or increased levels of Cln2p/Cdc28p kinase. Genetic analysis suggests that Fus3p promotes proliferation through activation of Mcm1p transcription factor that upregulates numerous genes in G1 phase. Thus, Fus3p and Kss1p control G1 arrest through a balance of arrest functions that inhibit the Cdc28p machinery and proliferative functions that bypass this inhibition. (+info)Pregnancy detection and the effects of age, body weight, and previous reproductive performance on pregnancy status and weaning rates of farmed fallow deer (Dama dama). (3/2015)
Fallow does (n = 502) of different ages (mature, 2-yr-old, and yearling) were maintained with bucks for a 60-d breeding season to determine whether previous reproductive performance and changes in BW affect doe pregnancy rates and to compare the effectiveness of ultrasonography and serum pregnancy-specific protein B (PSPB) for the detection of pregnancy in fallow does. Ultrasonography was performed, blood samples collected, and BW recorded at buck removal (d 0) and at 30 and 90 d after buck removal. Lactational status (lactating = WET; nonlactating = DRY) were determined from farm records taken at weaning prior to each breeding season (autumn 1990 through autumn 1994). Ultrasonography and PSPB for determining pregnancy were in agreement 93% of the time. Overall pregnancy rates did not differ (P>.10) relative to age of the doe; the combined pregnancy rate was 92%. We also determined that 82.9% of does conceived early in the breeding season and that the incidence of embryonal-fetal mortality during the first 90 d after buck removal was 2.8%. In general, mature and 2-yr-old DRY does were heavier and had lower pregnancy rates than WET does. The overall weaning rate for all does was 77.9%. Loss in the number of fawns from pregnancy detection to weaning was equivalent to 14.8% for mature does, 24.7% for 2 yr old does, and 42.5% for yearling does. These data indicate that even though pregnancy rates were relatively high, further study is needed to determine the causes associated with subsequent fawn losses, particularly among yearling does. As a production tool, lactational WET/ DRY status testing was found to be an acceptable means for determining the reproductive potential of individual does within the herd. In addition, serum PSPB may be used in place of ultrasonography for pregnancy diagnosis in fallow deer as early as d 30 after buck removal. (+info)Endothelin-1 and its mRNA in the wall layers of human arteries ex vivo. (4/2015)
BACKGROUND: The participation of endothelin-1 (ET-1) in the control of vascular tone in humans has been questioned, on the basis of the finding of subthreshold immunoreactive (ir) ET-1 plasma levels. However, because most ET-1 is secreted abluminally, it might attain a higher concentration in the tunica media than in plasma. Furthermore, evidence indicates that vascular smooth muscle cells (VSMCs) can synthesize ET-1 on stimulation in vitro. We therefore looked for irET-1 in the different layers of the wall of human arteries, including renal, gastric, and internal thoracic artery wall, obtained ex vivo from consenting patients with coronary artery disease and/or high blood pressure undergoing surgery, as well as from young organ donors. METHODS AND RESULTS: We performed immunohistochemistry with specific anti-ET-1 and anti-vWF antibodies followed by detection with an avidin-biotin complex ultrasensitive kit. The presence of preproET-1 and human endothelin-converting enzyme-1 (hECE-1) mRNA was also investigated by reverse transcription-polymerase chain reaction in homogenates of vessel wall, including preparations deprived of both endothelium and adventitia, and in isolated VSMCs. We detected irET-1 in the endothelium of all arteries and in the tunica media of internal thoracic artery from most patients with coronary artery disease. PreproET-1 and hECE-1 mRNA was also detected in VSMCs isolated from these vessels. irET-1 and irvWF staining in endothelium and tunica media was measured by use of microscope-coupled computer-assisted technology. Significant correlations between the amount of irET-1 in the tunica media and mean blood pressure (P<0.05), total serum cholesterol (P<0.05), and number of atherosclerotic sites (P<0.001) were found. Thus, in organ donors, irET-1 was detectable almost exclusively in endothelial cells, whereas in patients with coronary artery disease and/or arterial hypertension, sizable amounts of irET-1 were detectable in the tunica media of different types of arteries. In addition, VSMCs isolated from these vessels coexpressed the preproET-1 and hECE-1 genes. CONCLUSIONS: Collectively, these findings are consistent with the contention that endothelial damage occurs in most patients with atherosclerosis and/or hypertension and that ET-1 is synthesized in VSMCs of these patients. (+info)Intranephron distribution and regulation of endothelin-converting enzyme-1 in cyclosporin A-induced acute renal failure in rats. (5/2015)
Endothelin-1 (ET-1) is thought to play a significant role in acute renal failure induced by cyclosporin A (CsA). The cDNA sequence encoding endothelin-converting enzyme-1 (ECE-1), which produces the active form of ET-1 from big ET-1, was recently reported. To elicit the role of ECE-1 in the glomerular and tubular dysfunction induced by CsA, the effects of CsA on mRNA and protein expression of ECE-1 in rat kidney and on mRNA expression of prepro-ET-1 and ET A- and B-type receptors in glomeruli were studied. ECE-1 mRNA was detected in glomeruli and in whole nephron segments. ECE-1 mRNA expression was downregulated in all nephron segments at 24 h after CsA injection. Protein levels were also downregulated in glomeruli and in the outer and inner medulla. CsA rapidly increased prepro-ET-1 mRNA expression in glomeruli at 30 to 60 min after injection; this rapid increase was followed by an increase in plasma ET-1 levels. These increases were followed by decreased expression of ECE-1, ET A-type receptor, and ET B-type receptor mRNA at 6 h after injection, and serum creatinine levels were increased at 24 h after CsA injection. It is suggested that downregulation of glomerular and tubular ECE-1 expression may be caused by increased ET-1 synthesis in CsA-induced acute renal failure. (+info)Renin inhibition by substituted piperidines: a novel paradigm for the inhibition of monomeric aspartic proteinases? (6/2015)
BACKGROUND: The aspartic proteinase renin catalyses the first and rate-limiting step in the conversion of angiotensinogen to the hormone angiotensin II, and therefore plays an important physiological role in the regulation of blood pressure. Numerous potent peptidomimetic inhibitors of this important drug target have been developed, but none of these compounds have progressed past clinical phase II trials. Limited oral bioavailability or excessive production costs have prevented these inhibitors from becoming new antihypertensive drugs. We were interested in developing new nonpeptidomimetic renin inhibitors. RESULTS: High-throughput screening of the Roche compound library identified a simple 3, 4-disubstituted piperidine lead compound. We determined the crystal structures of recombinant human renin complexed with two representatives of this new class. Binding of these substituted piperidine derivatives is accompanied by major induced-fit adaptations around the enzyme's active site. CONCLUSIONS: The efficient optimisation of the piperidine inhibitors was facilitated by structural analysis of the renin active site in two renin-inhibitor complexes (some of the piperidine derivatives have picomolar affinities for renin). These structural changes provide the basis for a novel paradigm for inhibition of monomeric aspartic proteinases. (+info)Mechanism of the cleavage specificity of Alzheimer's disease gamma-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein. (7/2015)
Proteolytic processing of the amyloid precursor protein by beta-secretase yields A4CT (C99), which is cleaved further by the as yet unknown gamma-secretase, yielding the beta-amyloid (Abeta) peptide with 40 (Abeta40) or 42 residues (Abeta42). Because the position of gamma-secretase cleavage is crucial for the pathogenesis of Alzheimer's disease, we individually replaced all membrane-domain residues of A4CT outside the Abeta domain with phenylalanine, stably transfected the constructs in COS7 cells, and determined the effect of these mutations on the cleavage specificity of gamma-secretase (Abeta42/Abeta40 ratio). Compared with wild-type A4CT, mutations at Val-44, Ile-47, and Val-50 led to decreased Abeta42/Abeta40 ratios, whereas mutations at Thr-43, Ile-45, Val-46, Leu-49, and Met-51 led to increased Abeta42/Abeta40 ratios. A massive effect was observed for I45F (34-fold increase) making this construct important for the generation of animal models for Alzheimer's disease. Unlike the other mutations, A4CT-V44F was processed mainly to Abeta38, as determined by mass spectrometry. Our data provide a detailed model for the active site of gamma-secretase: gamma-secretase interacts with A4CT by binding to one side of the alpha-helical transmembrane domain of A4CT. Mutations in the transmembrane domain of A4CT interfere with the interaction between gamma-secretase and A4CT and, thus, alter the cleavage specificity of gamma-secretase. (+info)In vivo expression and localization of Candida albicans secreted aspartyl proteinases during oral candidiasis in HIV-infected patients. (8/2015)
Isoforms of aspartyl proteinase (Sap), which are encoded by at least nine related SAP genes, have been implicated to be a major virulence factor of the opportunistic yeast Candida albicans in experimental infections. Although it is generally assumed that proteinases are important for infections, detailed information on the pathogenetic role of Saps is still lacking. The same applies to the question whether the genes and corresponding isoforms of the enzyme are expressed during oral infection. For in vivo investigations, parts of the lesional oral epithelium were collected from three HIV-infected patients with oropharyngeal candidiasis. Immunoelectron microscopy was performed (pre- and post-embedding gold labeling with silver enhancement) using an anti-Sap murine monoclonal antibody directed against the gene products Sap1-3. It was possible to demonstrate expression of Sap antigens in each of the three samples of human oral candidiasis. This suggests that at least one of the genes SAP1-3 was expressed at the time of sample collection. Furthermore, a possible role of the enzymes during the interaction of yeast cells and mucosal cells is suggested: the majority of Sap antigens is secreted by those C. albicans cells that adhere directly to the epithelial surface. Sap immunoreactivity can be detected in particular at the site of close contact between C. albicans and epithelial cells, suggesting a pathogenetic role of the Saps in host-fungal interaction. Thus, inhibition of the enzyme might prove to be an important alternative in the prevention and treatment of candidiasis. (+info)Causes of Hypophosphatemia
-----------------------
There are several possible causes of hypophosphatemia, including:
1. Malnutrition or a poor diet that is deficient in phosphorus.
2. Gastrointestinal disorders such as celiac disease, inflammatory bowel disease, or gastrointestinal surgery.
3. Kidney problems such as chronic kidney disease, renal tubular acidosis, or distal renal tubular phosphate loss.
4. Hormonal imbalances such as hypoparathyroidism (underactive parathyroid glands) or hyperparathyroidism (overactive parathyroid glands).
5. Medications such as diuretics, antacids, and certain antibiotics.
6. Chronic alcoholism.
7. Genetic disorders such as X-linked hypophosphatemic rickets or familial hypophosphatemic rickets.
Symptoms of Hypophosphatemia
-------------------------
The symptoms of hypophosphatemia can vary depending on the severity and duration of the condition, but may include:
1. Weakness, fatigue, or muscle cramps.
2. Bone pain or joint stiffness.
3. Difficulty healing from injuries or infections.
4. Numbness or tingling sensations in the extremities.
5. Seizures or other neurological symptoms.
6. Respiratory problems such as shortness of breath or difficulty breathing.
7. Heart arrhythmias or cardiac failure.
Diagnosis and Treatment of Hypophosphatemia
---------------------------------------
Hypophosphatemia can be diagnosed through blood tests that measure the levels of phosphate in the blood. Treatment for hypophosphatemia typically involves correcting any underlying causes, such as stopping medications that may be causing the condition or treating underlying medical conditions.
In some cases, treatment may involve supplements to increase phosphate levels in the blood. Vitamin D and calcium supplements may also be prescribed to help maintain bone health. In severe cases of hypophosphatemia, hospitalization may be necessary to manage symptoms and prevent complications.
Prognosis and Complications of Hypophosphatemia
-----------------------------------------------
The prognosis for hypophosphatemia is generally good if the underlying cause is identified and treated promptly. However, untreated hypophosphatemia can lead to a number of complications, including:
1. Osteomalacia or osteoporosis.
2. Rickets in children.
3. Weakened immune system.
4. Increased risk of infections.
5. Nerve damage or neuropathy.
6. Cardiovascular problems such as heart arrhythmias or cardiac failure.
7. Respiratory failure.
8. Kidney damage or kidney failure.
It is important to seek medical attention if symptoms persist or worsen over time, as hypophosphatemia can lead to serious complications if left untreated.
Conclusion
----------
Hypophosphatemia is a condition characterized by low levels of phosphate in the blood. It can be caused by a variety of factors and may present with symptoms such as weakness, bone pain, and respiratory problems. Treatment typically involves correcting any underlying causes and supplements to increase phosphate levels in the blood.
Early detection and treatment are important to prevent complications of hypophosphatemia, which can include osteomalacia or osteoporosis, nerve damage, cardiovascular problems, respiratory failure, and kidney damage. If you suspect you may have hypophosphatemia, it is important to seek medical attention as soon as possible to receive proper diagnosis and treatment.
The symptoms of familial hypophosphatemic rickets typically appear during infancy or early childhood and may include:
* Bowed legs
* Delayed closure of the fontanelles (soft spots on the skull)
* Difficulty walking or standing
* Growth retardation
* Increased risk of fractures
* Thickening of the bones (hyperostosis)
* Tooth decay and gum disease (dental caries and periodontal disease)
If left untreated, familial hypophosphatemic rickets can lead to severe complications such as:
* Permanent skeletal deformities
* Increased risk of bone fractures
* Dental problems
* Growth retardation
* Intellectual disability
* Death in rare cases
The diagnosis of familial hypophosphatemic rickets is based on a combination of clinical findings, laboratory tests, and genetic analysis. Laboratory tests may include measurements of serum phosphate levels, urinary phosphate excretion, and assessment of bone density using imaging techniques such as X-rays or computed tomography (CT) scans. Genetic testing can identify mutations in the PHEX gene that confirm the diagnosis.
Treatment for familial hypophosphatemic rickets typically involves a combination of dietary modifications and medication. Dietary modifications may include increasing phosphate intake through supplements or high-phosphate foods, while medications such as vitamin D analogues and bisphosphonates can help to improve bone density and reduce the risk of fractures. In severe cases, surgery may be necessary to correct skeletal deformities.
In conclusion, familial hypophosphatemic rickets is a rare genetic disorder that affects the development of bones and teeth, leading to a range of symptoms including bowed legs, thickened skin, and dental problems. The diagnosis is based on a combination of clinical findings, laboratory tests, and genetic analysis, while treatment involves a combination of dietary modifications and medication. With appropriate management, individuals with familial hypophosphatemic rickets can lead active and productive lives, although some may experience ongoing health issues throughout their lifetime.
Nodavirus endopeptidase
Protein metabolism
Glutamyl endopeptidase I
Rhizopuspepsin
LGMN
Nepenthesin
Glutamyl endopeptidase GluV8
Candidapepsin
Aspartic protease
Metalloproteinase
Subtilase
Osteopontin
Pepsin
Protease
Scytalidopepsin B
Death regulator Nedd2-like caspase
Protease inhibitor (biology)
Signal peptide peptidase
Ecadotril
Asparagine peptide lyase
Proteases in angiogenesis
Saccharopepsin
Renin
Serine protease
Chymosin
Cysteine protease
Osteoclast
List of EC numbers (EC 3)
Picornain 3C
List of MeSH codes (D08)
Active site
Papain-like protease
DeCS
Glioma/patologia
DeCS 2008 - versión 17 de Marzo de 2008
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Proteinases2
- The hydrogen bonding interactions and the conformation adopted by pepstatin are very similar to those found in complexes of pepstatin with other aspartic proteinases. (nih.gov)
- By comparing the residues on the binding surface with those of the other human aspartic proteinases, it has been possible to rationalize some of the experimental data concerning the different specificities. (nih.gov)
Peptides1
- The product peptides derived from the endopeptidase activities of BoNTs are detected by matrix-assisted laser-desorption ionization time-of-flight mass spectrometry. (cdc.gov)
Family1
- HN - 2010 MH - Aerococcaceae UI - D056567 MN - B3.510.550.30 MS - A family of gram-positive lactic acid-producing bacteria in the order LACTOBACILLALES. (nih.gov)