Autolysis
Bacteriolysis
N-Acetylmuramoyl-L-alanine Amidase
Calpain
Cell Wall
Trypsinogen
Teichoic Acids
Cefotiam
Enteropeptidase
Staphylococcus aureus
Octoxynol
Endopeptidases
Muramidase
Enterococcus faecalis
Chymosin
Caseins
Phosphotungstic Acid
Lysostaphin
Penicillins
Streptolysins
Mutation
Molecular Sequence Data
Chloramphenicol
Clostridium perfringens
Foodborne Diseases
Fatal Outcome
Autolysosomal membrane-associated betaine homocysteine methyltransferase. Limited degradation fragment of a sequestered cytosolic enzyme monitoring autophagy. (1/238)
We compared the membrane proteins of autolysosomes isolated from leupeptin-administered rat liver with those of lysosomes. In addition to many polypeptides common to the two membranes, the autolysosomal membranes were found to be more enriched in endoplasmic reticulum lumenal proteins (protein-disulfide isomerase, calreticulin, ER60, BiP) and endosome/Golgi markers (cation-independent mannose 6-phosphate receptor, transferrin receptor, Golgi 58-kDa protein) than lysosomal membranes. The autolysosomal membrane proteins include three polypeptides (44, 35, and 32 kDa) whose amino-terminal sequences have not yet been reported. Combining immunoblotting and reverse transcriptase-polymerase chain reaction analyses, we identified the 44-kDa peptide as the intact subunit of betaine homocysteine methyltransferase and the 35- and 32-kDa peptides as two proteolytic fragments. Pronase digestion of autolysosomes revealed that the 44-kDa and 32-kDa peptides are present in the lumen, whereas the 35-kDa peptide is not. In primary hepatocyte cultures, the starvation-induced accumulation of the 32-kDa peptide occurs in the presence of E64d, showing that the 32-kDa peptide is formed from the sequestered 44-kDa peptide during autophagy. The accumulation is induced by rapamycin but completely inhibited by wortmannin, 3-methyladenine, and bafilomycin. Thus, detection of the 32-kDa peptide by immunoblotting can be used as a streamlined assay for monitoring autophagy. (+info)Developmental aspects of secondary palate formation. (2/238)
Research on development of the secondary palate has, in the past, dealt primarily with morphological aspects of shelf elevation and fusion. The many factors thought to be involved in palatal elevation, such as fetal neuromuscular activity and growth of the cranial base and mandible, as well as production of extracellular matrix and contractile elements in the palate, are mostly based on gross, light microscopic, morphometric or histochemical observations. Recently, more biochemical procedures have been utilized to described palatal shelf elevation. Although these studies strongly suggest that palatal extracellular matrix plays a major role in shelf movement, interpretation of these data remains difficult owing to the complexity of tissue interactions involved in craniofacial development. Shelf elevation does not appear to involve a single motive factor, but rather a coordinated interaction of all of the abovementioned developmental events. Further analysis of mechanisms of shelf elevation requires development of new, and refinement of existing, in vitro procedures. A system that enables one to examine shelf elevation in vitro would allow more meaningful analysis of the relative importance of the various components in shelf movement. Much more is known about fusion of the palatal shelves, owing in large part to in vitro studies. Fusion of the apposing shelves, both in vivo and in vitro, is dependent upon adhesion and cell dealth of the midline epithelial cells. Adhesion betweeen apposing epithelial surfaces appears to involve epithelial cell surface macromolecules. Further analysis of palatal epithelial adhesion should be directed towards characterization of those cell surface components responsible for this adhesive interaction. Midline epithelial cells cease DNA synthesis 24-36 h before shelf elevation and contact, become active in the synthesis of cell surface glycoproteins, and subsequently manifest morphological signs of necrosis. Death of the midline epithelial cells is thought to involve a programmed, lysosomal-mediated autolysis... (+info)Suppression of the lytic and bactericidal effects of cell wallinhibitory antibiotics. (3/238)
The bacteriolytic effect of beta-lactam antibiotics on Bacillus subtilis and on Streptococcus pneumoniae was found to be a function of the pH; lysis was suppressed if the pH of the pneumococcal culture was below 6.0 during penicillin treatment. In the case of B. subtilis, growth at pH 6.6 prevented penicillin-induced lysis. In pneumococci, the addition of trypsin to the growth medium also protected against lysis. The pH-dependent protection phenomenon resembled in several respects the antibiotic "tolerance" of pneumococci with a defective autolytic system. (i) At the pH nonpermissive for lysis, the bacteria retained their normal sensitivity to beta-lactam and to other cell wall inhibitors; however, instead of lysis, the drug-treated bacteria simply stopped growing. Loss of viability of the cells was also greatly reduced. (ii) Protection against lysis was independent of the dose and chemical nature of the cell wall inhibitors. (iii) The protection effect was reversible; lysis and loss of viability could be triggered by a postincubation of the drug-treated bacteria at the pH permissive for lysis. (+info)The autolysis loop of activated protein C interacts with factor Va and differentiates between the Arg506 and Arg306 cleavage sites. (4/238)
The anticoagulant human plasma serine protease, activated protein C (APC), inactivates blood coagulation factors Va (FVa) and VIIIa. The so-called autolysis loop of APC (residues 301-316, equivalent to chymotrypsin [CHT] residues 142-153) has been hypothesized to bind FVa. In this study, site-directed mutagenesis was used to probe the role of the charged residues in this loop in interactions between APC and FVa. Residues Arg306 (147 CHT), Glu307, Lys308, Glu309, Lys311, Arg312, and Arg314 were each individually, or in selected combinations, mutated to Ala. The purified recombinant protein C mutants were characterized using activated partial thromboplastin time (APTT) clotting assays and FVa inactivation assays. Mutants 306A, 308A, 311A, 312A, and 314A had mildly reduced anticoagulant activity. Based on FVa inactivation assays and APTT assays using purified Gln506-FVa and plasma containing Gln506-FV, it appeared that these mutants were primarily impaired for cleavage of FVa at Arg506. Studies of the quadruple APC mutant (306A, 311A, 312A, and 314A) suggested that the autolysis loop provides for up to 15-fold discrimination of the Arg506 cleavage site relative to the Arg306 cleavage site. This study shows that the loop on APC of residues 306 to 314 defines an FVa binding site and accounts for much of the difference in cleavage rates at the 2 major cleavage sites in FVa. (Blood. 2000;96:585-593) (+info)The D-alanine residues of Staphylococcus aureus teichoic acids alter the susceptibility to vancomycin and the activity of autolytic enzymes. (5/238)
Recently, Staphylococcus aureus strains with intermediate resistance to vancomycin, the antibiotic of last resort, have been described. Multiple changes in peptidoglycan turnover and structure contribute to the resistance phenotype. Here, we describe that structural changes of teichoic acids in the cell envelope have a considerable influence on the susceptibility to vancomycin and other glycopeptides. S. aureus cells lacking D-alanine esters in teichoic acids exhibited an at least threefold-increased sensitivity to glycopeptide antibiotics. Furthermore, the autolytic activity of the D-alanine mutant was reduced compared to the wild-type, and the mutant was more susceptible to the staphylolytic enzyme lysostaphin. Vancomycin inhibited autolysis at very high concentrations but neither in the wild-type nor in the mutant was the autolytic activity influenced in the range of the MIC. Mutant cells had a considerably higher capacity to bind vancomycin. (+info)Description of staphylococcus serine protease (ssp) operon in Staphylococcus aureus and nonpolar inactivation of sspA-encoded serine protease. (6/238)
Signature tagged mutagenesis has recently revealed that the Ssp serine protease (V8 protease) contributes to in vivo growth and survival of Staphylococcus aureus in different infection models, and our previous work indicated that Ssp could play a role in controlling microbial adhesion. In this study, we describe an operon structure within the ssp locus of S. aureus RN6390. The ssp gene encoding V8 protease is designated as sspA, and is followed by sspB, which encodes a 40.6-kDa cysteine protease, and sspC, which encodes a 12.9-kDa protein of unknown function. S. aureus SP6391 is an isogenic derivative of RN6390, in which specific loss of SspA function was achieved through a nonpolar allelic replacement mutation. In addition to losing SspA, the culture supernatant of SP6391 showed a loss of 22- to 23-kDa proteins and the appearance of a 40-kDa protein corresponding to SspB. Although the 40-kDa SspB protein could degrade denatured collagen, our data establish that this is a precursor form which is normally processed by SspA to form a mature cysteine protease. Culture supernatant of SP6391 also showed a new 42-kDa glucosaminidase and enhanced glucosaminidase activity in the 29 to 32 kDa range. Although nonpolar inactivation of sspA exerted a pleiotropic effect, S. aureus SP6391 exhibited enhanced virulence in a tissue abscess infection model relative to RN6390. Therefore, we conclude that SspA is required for maturation of SspB and plays a role in controlling autolytic activity but does not by itself exert a significant contribution to the development of tissue abscess infections. (+info)Increasing the thermal stability of euphauserase. A cold-active and multifunctional serine protease from Antarctic krill. (7/238)
A molecular model of Antarctic krill euphauserase based on the known crystal structure of its fiddler crab analog, collagenase I, indicates that the core structure of these enzymes is almost identical. Euphauserase is a cold-active and thermally sensitive enzyme with a high affinity for Lys, Arg and large hydrophobic amino acids. Residue Phe137 in euphauserase, localized in loop D (autolysis loop), is highly exposed on the surface of the molecule. Therefore, it appeared to be an easy target for autolysis. The broadly specific euphauserase has a low affinity for negatively charged residues. In order to increase the stability of the enzyme, two mutants were created in which residue Phe137 was replaced by a Glu and an Asp residue. Both mutations resulted in increased stability of the recombinant euphauserase towards thermal inactivation. (+info)The AbcA transporter of Staphylococcus aureus affects cell autolysis. (8/238)
Increased production of penicillin-binding protein PBP 4 is known to increase peptidoglycan cross-linking and contributes to methicillin resistance in Staphylococcus aureus. The pbp4 gene shares a 400-nucleotide intercistronic region with the divergently transcribed abcA gene, encoding an ATP-binding cassette transporter of unknown function. Our study revealed that methicillin stimulated abcA transcription but had no effects on pbp4 transcription. Analysis of abcA expression in mutants defective for global regulators showed that abcA is under the control of agr. Insertional inactivation of abcA by an erythromycin resistance determinant did not influence pbp4 transcription, nor did it alter resistance to methicillin and other cell wall-directed antibiotics. However, abcA mutants showed spontaneous partial lysis on plates containing subinhibitory concentrations of methicillin due to increased spontaneous autolysis. Since the autolytic zymograms of cell extracts were identical in mutants and parental strains, we postulate an indirect role of AbcA in control of autolytic activities and in protection of the cells against methicillin. (+info)In the medical field, autolysis is a term used to describe the self-destruction or breakdown of cells or tissues within an organism. This process occurs naturally in response to various forms of cellular stress, such as exposure to radiation or certain chemicals, and it is also involved in the immune system's removal of dead cells and debris. Autolysis can be triggered by a variety of factors, including oxidative stress, heat shock, and exposure to certain enzymes or toxins.
There are several types of autolysis, including:
1. Autophagy: a process by which cells break down and recycle their own components, such as proteins and organelles, in order to maintain cellular homeostasis and survive under conditions of limited nutrient availability.
2. Necrosis: a form of autolysis that occurs as a result of cellular injury or stress, leading to the release of harmful substances into the surrounding tissue and triggering an inflammatory response.
3. Apoptosis: a programmed form of cell death that involves the breakdown of cells and their components, and is involved in various physiological processes, such as development and immune system function.
4. Lipofuscinogenesis: a process by which lipid-rich organelles undergo autolysis, leading to the formation of lipofuscin, a type of cellular waste product.
5. Chaperone-mediated autophagy: a process by which proteins are broken down and recycled in the presence of chaperone proteins, which help to fold and stabilize the target proteins.
Autolysis can be studied using various techniques, including:
1. Light microscopy: a technique that uses visible light to visualize cells and their components, allowing researchers to observe the effects of autolysis on cellular structures.
2. Electron microscopy: a technique that uses a beam of electrons to produce high-resolution images of cells and their components, allowing researchers to observe the ultrastructure of cells and the effects of autolysis at the molecular level.
3. Biochemical assays: techniques that measure the levels of specific cellular components or metabolites in order to assess the progress of autolysis.
4. Gene expression analysis: a technique that measures the levels of specific messenger RNAs (mRNAs) in order to assess the activity of genes involved in autolysis.
5. Proteomics: a technique that measures the levels and modifications of specific proteins in order to assess the effects of autolysis on protein turnover and degradation.
Autolysis plays an important role in various cellular processes, including:
1. Cellular detoxification: Autolysis can help to remove damaged or misfolded proteins, which can be toxic to cells, by breaking them down into smaller peptides and amino acids that can be further degraded.
2. Cellular renewal: Autolysis can help to remove old or damaged cellular components, such as organelles and protein aggregates, and recycle their building blocks to support the synthesis of new cellular components.
3. Cellular defense: Autolysis can help to protect cells against pathogens, such as bacteria and viruses, by breaking down and removing infected cellular components.
4. Apoptosis: Autolysis is involved in the execution of apoptosis, a programmed form of cell death that is important for maintaining tissue homeostasis and preventing cancer.
Dysregulation of autolysis has been implicated in various diseases, including:
1. Cancer: Autolysis can promote the growth and survival of cancer cells by providing them with a source of energy and building blocks for protein synthesis.
2. Neurodegenerative diseases: Autolysis can contribute to the degeneration of neurons in neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, and Huntington's disease.
3. Infectious diseases: Autolysis can help pathogens to evade the host immune system by breaking down and removing infected cellular components.
4. Aging: Dysregulation of autolysis has been implicated in the aging process, as it can lead to the accumulation of damaged or misfolded proteins and the degradation of cellular components.
Overall, autolysis is a complex and highly regulated process that plays a critical role in maintaining cellular homeostasis and responding to environmental stressors. Further research is needed to fully understand the mechanisms of autolysis and its implications for human health and disease.
Early Postmortem Changes:
1. Cessation of metabolic processes: After death, the body's metabolic processes come to a standstill, leading to a decrease in body temperature, cellular respiration, and other physiological functions.
2. Decline in blood pressure: The heart stops pumping blood, causing a rapid decline in blood pressure.
3. Cardiac arrest: The heart stops beating, leading to a lack of oxygen supply to the body's tissues.
4. Brain death: The brain ceases to function, causing a loss of consciousness and reflexes.
5. Rigor mortis: The muscles become stiff and rigid due to the buildup of lactic acid and other metabolic byproducts.
6. Livor mortis: Blood settles in the dependent parts of the body, causing discoloration and swelling.
7. Algor mortis: The body's temperature cools, causing the skin to feel cool to the touch.
Late Postmortem Changes:
1. Decomposition: Bacteria and other microorganisms begin to break down the body's tissues, leading to putrefaction and decay.
2. Autolysis: Enzymes within the body's cells break down cellular components, causing self-digestion and softening of the tissues.
3. Lipid decomposition: Fats and oils in the body undergo oxidation, leading to the formation of offensive odors.
4. Coagulative necrosis: Blood pools in the body's tissues, causing damage to the cells and tissues.
5. Putrefaction: Bacteria in the gut and other parts of the body cause the breakdown of tissues, leading to the formation of gases and fluids.
It is important to note that postmortem changes can significantly impact the interpretation of autopsy findings and the determination of cause of death. Therefore, it is essential to consider these changes when performing an autopsy and interpreting the results.
Foodborne diseases, also known as food-borne illnesses or gastrointestinal infections, are conditions caused by eating contaminated or spoiled food. These diseases can be caused by a variety of pathogens, including bacteria, viruses, and parasites, which can be present in food products at any stage of the food supply chain.
Examples of common foodborne diseases include:
1. Salmonella: Caused by the bacterium Salmonella enterica, this disease can cause symptoms such as diarrhea, fever, and abdominal cramps.
2. E. coli: Caused by the bacterium Escherichia coli, this disease can cause a range of symptoms, including diarrhea, urinary tract infections, and pneumonia.
3. Listeria: Caused by the bacterium Listeria monocytogenes, this disease can cause symptoms such as fever, headache, and stiffness in the neck.
4. Campylobacter: Caused by the bacterium Campylobacter jejuni, this disease can cause symptoms such as diarrhea, fever, and abdominal cramps.
5. Norovirus: This highly contagious virus can cause symptoms such as diarrhea, vomiting, and stomach cramps.
6. Botulism: Caused by the bacterium Clostridium botulinum, this disease can cause symptoms such as muscle paralysis, respiratory failure, and difficulty swallowing.
Foodborne diseases can be diagnosed through a variety of tests, including stool samples, blood tests, and biopsies. Treatment typically involves antibiotics or other supportive care to manage symptoms. Prevention is key to avoiding foodborne diseases, and this includes proper food handling and preparation practices, as well as ensuring that food products are stored and cooked at safe temperatures.
Autolysis
Autolysis (biology)
Autolysis (alcohol fermentation)
Lester Dragstedt
Traditional method
Decomposition
GC-content
Fixation (histology)
Lepidium coronopus
Marmite
Protease
Pxr sRNA
Phi11 holin family
Botrytis allii
Propionibacterium freudenreichii
Autophagy
Horseradish
Erysimum cheiranthoides
Ficain
Calpain-2
Insecticide
Belinda Ferrari
Chemical process of decomposition
Endomembrane system
John Torrington
Pseudomonas aeruginosa hol holin family
Hemicellulose
Cia-dependent small RNAs
Dissolved organic carbon
Elcatonin
O-glycosylation regulates autolysis of cellular membrane type-1 matrix metalloproteinase (MT1-MMP) - PubMed
Increased pathogenicity of pneumococcal serotype 1 is driven by rapid autolysis and release of pneumolysin - PubMed
Innovative methods of extracting mannoproteins from lees and accelerating autolysis
Exp. 1 (T[ransforming]. P[rinciple].) Effect of Fluoride on Autolysis of Pneumococcus Type III and on Preservation of the...
Exp. 1 (T[ransforming]. P[rinciple].) Effect of Fluoride on Autolysis of Pneumococcus Type III and on Preservation of the...
Exp. 1 (T[ransforming]. P[rinciple].) Effect of Fluoride on Autolysis of Pneumococcus Type III and on Preservation of the...
Inhibition of ultraviolet-induced sea cucumber (Stichopus japonicus) autolysis by maintaining coelomocyte intracellular calcium...
Guide to Use the Atlas
Nicotine Enhances Staphylococcus epidermidis Biofilm Formation by Altering the Bacterial Autolysis, Extracellular DNA Releasing...
Exp. 1 (T[ransforming]. P[rinciple].) Effect of Fluoride on Autolysis of Pneumococcus Type III and on Preservation of the...
Fatal Foodborne Clostridium perfringens Illness at a State Psychiatric Hospital - Louisiana, 2010
Genotype-Tissue Expression (GTEx) - Agenda
RFA-RM-12-009: Enhancing GTEx with molecular analyses of stored biospecimens (U01)
Biomarkers Search
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Leptospirosis
Henriot, Blanc de Blancs, Champagne, France NV
Race, Richard 2004 - Office of NIH History and Stetten Museum
Western Tufted Deer (Elaphodus cephalophus cephalophus) | IVIS
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SCE Presentation
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What Are the Stages of Decomposition?
Putrefaction2
- In most circumstances, autolysis and putrefaction occur in tandem. (medscape.com)
- Decomposition mainly involves two processes known as Autolysis and Putrefaction. (affinitybioaz.com)
Staphylococcus1
- Reduced expression of the atl autolysin gene and susceptibility to autolysis in clinical heterogeneous glycopeptide-intermediate Staphylococcus aureus (hGISA) and GISA strains. (harvard.edu)
Tissue1
- Autolysis of living tissue. (nih.gov)
Place1
- After milling, the autolysis process takes place in this tank. (thefishsite.com)
Animal1
- Animal 3 had advanced autolysis, which precluded pathologic analysis. (cdc.gov)