Cathepsin A: A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by protecting BETA-GALACTOSIDASE and NEURAMINIDASE from degradation. It was formerly classified as EC 3.4.12.1 and EC 3.4.21.13.Lysosomal Storage Diseases: Inborn errors of metabolism characterized by defects in specific lysosomal hydrolases and resulting in intracellular accumulation of unmetabolized substrates.Carboxypeptidases: Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.Lysosomes: A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Neuraminidase: An enzyme that catalyzes the hydrolysis of alpha-2,3, alpha-2,6-, and alpha-2,8-glycosidic linkages (at a decreasing rate, respectively) of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid, and synthetic substrate. (From Enzyme Nomenclature, 1992)beta-Galactosidase: A group of enzymes that catalyzes the hydrolysis of terminal, non-reducing beta-D-galactose residues in beta-galactosides. Deficiency of beta-Galactosidase A1 may cause GANGLIOSIDOSIS, GM1.Gangliosidosis, GM1: An autosomal recessive neurodegenerative disorder caused by the absence or deficiency of BETA-GALACTOSIDASE. It is characterized by intralysosomal accumulation of G(M1) GANGLIOSIDE and oligosaccharides, primarily in neurons of the central nervous system. The infantile form is characterized by MUSCLE HYPOTONIA, poor psychomotor development, HIRSUTISM, hepatosplenomegaly, and facial abnormalities. The juvenile form features HYPERACUSIS; SEIZURES; and psychomotor retardation. The adult form features progressive DEMENTIA; ATAXIA; and MUSCLE SPASTICITY. (From Menkes, Textbook of Child Neurology, 5th ed, pp96-7)Mucolipidoses: A group of inherited metabolic diseases characterized by the accumulation of excessive amounts of acid mucopolysaccharides, sphingolipids, and/or glycolipids in visceral and mesenchymal cells. Abnormal amounts of sphingolipids or glycolipids are present in neural tissue. INTELLECTUAL DISABILITY and skeletal changes, most notably dysostosis multiplex, occur frequently. (From Joynt, Clinical Neurology, 1992, Ch56, pp36-7)beta-N-Acetylhexosaminidases: A hexosaminidase specific for non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. It acts on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES. Two specific mammalian isoenzymes of beta-N-acetylhexoaminidase are referred to as HEXOSAMINIDASE A and HEXOSAMINIDASE B. Deficiency of the type A isoenzyme causes TAY-SACHS DISEASE, while deficiency of both A and B isozymes causes SANDHOFF DISEASE. The enzyme has also been used as a tumor marker to distinguish between malignant and benign disease.Isoflurophate: A di-isopropyl-fluorophosphate which is an irreversible cholinesterase inhibitor used to investigate the NERVOUS SYSTEM.Cathepsins: A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.GlucuronidaseMannosephosphates: Phosphoric acid esters of mannose.Acetylglucosaminidase: A beta-N-Acetylhexosaminidase that catalyzes the hydrolysis of terminal, non-reducing 2-acetamido-2-deoxy-beta-glucose residues in chitobiose and higher analogs as well as in glycoproteins. Has been used widely in structural studies on bacterial cell walls and in the study of diseases such as MUCOLIPIDOSIS and various inflammatory disorders of muscle and connective tissue.Receptor, IGF Type 2: A receptor that is specific for IGF-II and mannose-6-phosphate. The receptor is a 250-kDa single chain polypeptide which is unrelated in structure to the type 1 IGF receptor (RECEPTOR, IGF TYPE 1) and does not have a tyrosine kinase domain.Cathepsin D: An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).Acid Phosphatase: An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2.Microscopy, Immunoelectron: Microscopy in which the samples are first stained immunocytochemically and then examined using an electron microscope. Immunoelectron microscopy is used extensively in diagnostic virology as part of very sensitive immunoassays.Hexosaminidases: Enzymes that catalyze the hydrolysis of N-acylhexosamine residues in N-acylhexosamides. Hexosaminidases also act on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES.Glycoproteins: Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.alpha-Mannosidase: An enzyme that catalyzes the HYDROLYSIS of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides. The enzyme plays a role in the processing of newly formed N-glycans and in degradation of mature GLYCOPROTEINS. There are multiple isoforms of alpha-mannosidase, each having its own specific cellular location and pH optimum. Defects in the lysosomal form of the enzyme results in a buildup of mannoside intermediate metabolites and the disease ALPHA-MANNOSIDOSIS.Fibroblasts: Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.Cerebroside-Sulfatase: An enzyme that catalyzes the hydrolysis of cerebroside 3-sulfate (sulfatide) to yield a cerebroside and inorganic sulfate. A marked deficiency of arylsulfatase A, which is considered the heat-labile component of cerebroside sulfatase, has been demonstrated in all forms of metachromatic leukodystrophy (LEUKODYSTROPHY, METACHROMATIC). EC 3.1.6.8.Arylsulfatases: Enzymes that catalyze the hydrolysis of a phenol sulfate to yield a phenol and sulfate. Arylsulfatase A, B, and C have been separated. A deficiency of arylsulfatases is one of the causes of metachromatic leukodystrophy (LEUKODYSTROPHY, METACHROMATIC). EC 3.1.6.1.Molecular Weight: The sum of the weight of all the atoms in a molecule.Mannosidases: Glycoside hydrolases that catalyze the hydrolysis of alpha or beta linked MANNOSE.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Transferases (Other Substituted Phosphate Groups): A class of enzymes that transfers substituted phosphate groups. EC 2.7.8.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.alpha-L-Fucosidase: An enzyme that catalyzes the hydrolysis of an alpha L-fucoside to yield an alcohol and L-fucose. Deficiency of this enzyme can cause FUCOSIDOSIS. EC 3.2.1.51.Kinetics: The rate dynamics in chemical or physical systems.Hydrolases: Any member of the class of enzymes that catalyze the cleavage of the substrate and the addition of water to the resulting molecules, e.g., ESTERASES, glycosidases (GLYCOSIDE HYDROLASES), lipases, NUCLEOTIDASES, peptidases (PEPTIDE HYDROLASES), and phosphatases (PHOSPHORIC MONOESTER HYDROLASES). EC 3.beta-Glucosidase: An exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of GLUCOSE.SulfatasesHexosephosphatesMutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Galactosidases: A family of galactoside hydrolases that hydrolyze compounds with an O-galactosyl linkage. EC 3.2.1.-.alpha-Galactosidase: An enzyme that catalyzes the hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-galactosides including galactose oligosaccharides, galactomannans, and galactolipids.ZymosanIduronidase: An enzyme that hydrolyzes iduronosidic linkages in desulfated dermatan. Deficiency of this enzyme produces Hurler's syndrome. EC 3.2.1.76.Glucosidases: Enzymes that hydrolyze O-glucosyl-compounds. (Enzyme Nomenclature, 1992) EC 3.2.1.-.Cathepsin B: A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.Glucosylceramidase: A glycosidase that hydrolyzes a glucosylceramide to yield free ceramide plus glucose. Deficiency of this enzyme leads to abnormally high concentrations of glucosylceramide in the brain in GAUCHER DISEASE. EC 3.2.1.45.Glycoside HydrolasesProtective Agents: Synthetic or natural substances which are given to prevent a disease or disorder or are used in the process of treating a disease or injury due to a poisonous agent.Ammonium Chloride: An acidifying agent that has expectorant and diuretic effects. Also used in etching and batteries and as a flux in electroplating.Gaucher Disease: An autosomal recessive disorder caused by a deficiency of acid beta-glucosidase (GLUCOSYLCERAMIDASE) leading to intralysosomal accumulation of glycosylceramide mainly in cells of the MONONUCLEAR PHAGOCYTE SYSTEM. The characteristic Gaucher cells, glycosphingolipid-filled HISTIOCYTES, displace normal cells in BONE MARROW and visceral organs causing skeletal deterioration, hepatosplenomegaly, and organ dysfunction. There are several subtypes based on the presence and severity of neurological involvement.Mucopolysaccharidosis I: Systemic lysosomal storage disease caused by a deficiency of alpha-L-iduronidase (IDURONIDASE) and characterized by progressive physical deterioration with urinary excretion of DERMATAN SULFATE and HEPARAN SULFATE. There are three recognized phenotypes representing a spectrum of clinical severity from severe to mild: Hurler syndrome, Hurler-Scheie syndrome and Scheie syndrome (formerly mucopolysaccharidosis V). Symptoms may include DWARFISM; hepatosplenomegaly; thick, coarse facial features with low nasal bridge; corneal clouding; cardiac complications; and noisy breathing.alpha-Glucosidases: Enzymes that catalyze the exohydrolysis of 1,4-alpha-glucosidic linkages with release of alpha-glucose. Deficiency of alpha-1,4-glucosidase may cause GLYCOGEN STORAGE DISEASE TYPE II.Cathepsin L: A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.Endocytosis: Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.Cytochalasin B: A cytotoxic member of the CYTOCHALASINS.Pinocytosis: The engulfing of liquids by cells by a process of invagination and closure of the cell membrane to form fluid-filled vacuoles.Glycogen Storage Disease Type II: An autosomal recessively inherited glycogen storage disease caused by GLUCAN 1,4-ALPHA-GLUCOSIDASE deficiency. Large amounts of GLYCOGEN accumulate in the LYSOSOMES of skeletal muscle (MUSCLE, SKELETAL); HEART; LIVER; SPINAL CORD; and BRAIN. Three forms have been described: infantile, childhood, and adult. The infantile form is fatal in infancy and presents with hypotonia and a hypertrophic cardiomyopathy (CARDIOMYOPATHY, HYPERTROPHIC). The childhood form usually presents in the second year of life with proximal weakness and respiratory symptoms. The adult form consists of a slowly progressive proximal myopathy. (From Muscle Nerve 1995;3:S61-9; Menkes, Textbook of Child Neurology, 5th ed, pp73-4)Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Oligosaccharides: Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.Fabry Disease: An X-linked inherited metabolic disease caused by a deficiency of lysosomal ALPHA-GALACTOSIDASE A. It is characterized by intralysosomal accumulation of globotriaosylceramide and other GLYCOSPHINGOLIPIDS in blood vessels throughout the body leading to multi-system complications including renal, cardiac, cerebrovascular, and skin disorders.Methylmannosides: Mannosides formed by the reaction of the hydroxyl group on the anomeric carbon atom of mannose with methyl alcohol. They include both alpha- and beta-methylmannosides.N-Acetylgalactosamine-4-Sulfatase: An arylsulfatase that catalyzes the hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate. A deficiency of this enzyme is responsible for the inherited lysosomal disease, Maroteaux-Lamy syndrome (MUCOPOLYSACCHARIDOSIS VI). EC 3.1.6.12.Galactosylceramidase: An enzyme that hydrolyzes galactose from ceramide monohexosides. Deficiency of this enzyme may cause globoid cell leukodystrophy (LEUKODYSTROPHY, GLOBOID CELL). EC 3.2.1.46.Phagocytosis: The engulfing and degradation of microorganisms; other cells that are dead, dying, or pathogenic; and foreign particles by phagocytic cells (PHAGOCYTES).Aspartylglucosylaminase: An enzyme that catalyzes the conversion of N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine and water to N-acetyl-beta-D-glucosaminylamine and L-aspartate. It acts only on asparagine-oligosaccharides containing one amino acid, i.e. the ASPARAGINE has free alpha-amino and alpha-carboxyl groups. (From Enzyme Nomenclature, 1992)Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase: A group of related enzymes responsible for the endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose-content glycopeptides and GLYCOPROTEINS.Gangliosidoses: A group of autosomal recessive lysosomal storage disorders marked by the accumulation of GANGLIOSIDES. They are caused by impaired enzymes or defective cofactors required for normal ganglioside degradation in the LYSOSOMES. Gangliosidoses are classified by the specific ganglioside accumulated in the defective degradation pathway.Cathepsin C: A papain-like cysteine protease that has specificity for amino terminal dipeptides. The enzyme plays a role in the activation of several pro-inflammatory serine proteases by removal of their aminoterminal inhibitory dipeptides. Genetic mutations that cause loss of cathepsin C activity in humans are associated with PAPILLON-LEFEVRE DISEASE.Neutrophils: Granular leukocytes having a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Dictyostelium: A genus of protozoa, formerly also considered a fungus. Its natural habitat is decaying forest leaves, where it feeds on bacteria. D. discoideum is the best-known species and is widely used in biomedical research.Macrophages: The relatively long-lived phagocytic cell of mammalian tissues that are derived from blood MONOCYTES. Main types are PERITONEAL MACROPHAGES; ALVEOLAR MACROPHAGES; HISTIOCYTES; KUPFFER CELLS of the liver; and OSTEOCLASTS. They may further differentiate within chronic inflammatory lesions to EPITHELIOID CELLS or may fuse to form FOREIGN BODY GIANT CELLS or LANGHANS GIANT CELLS. (from The Dictionary of Cell Biology, Lackie and Dow, 3rd ed.)Protective Clothing: Clothing designed to protect the individual against possible exposure to known hazards.Golgi Apparatus: A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990)Microscopy, Electron: Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.Chondro-4-Sulfatase: An enzyme from the sulfuric ester hydrolase class that breaks down one of the products of the chondroitin lyase II reaction. EC 3.1.6.9.Mucopolysaccharidosis IV: Genetic disorder of mucopolysaccharide metabolism characterized by skeletal abnormalities, joint instability, development of cervical myelopathy, and excessive urinary keratan sulfate. There are two biochemically distinct forms, each due to a deficiency of a different enzyme.Mannose: A hexose or fermentable monosaccharide and isomer of glucose from manna, the ash Fraxinus ornus and related plants. (From Grant & Hackh's Chemical Dictionary, 5th ed & Random House Unabridged Dictionary, 2d ed)L-Lactate Dehydrogenase: A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.Cell Compartmentation: A partitioning within cells due to the selectively permeable membranes which enclose each of the separate parts, e.g., mitochondria, lysosomes, etc.Leukodystrophy, Globoid Cell: An autosomal recessive metabolic disorder caused by a deficiency of GALACTOSYLCERAMIDASE leading to intralysosomal accumulation of galactolipids such as GALACTOSYLCERAMIDES and PSYCHOSINE. It is characterized by demyelination associated with large multinucleated globoid cells, predominantly involving the white matter of the central nervous system. The loss of MYELIN disrupts normal conduction of nerve impulses.Mucopolysaccharidoses: Group of lysosomal storage diseases each caused by an inherited deficiency of an enzyme involved in the degradation of glycosaminoglycans (mucopolysaccharides). The diseases are progressive and often display a wide spectrum of clinical severity within one enzyme deficiency.Cell Fractionation: Techniques to partition various components of the cell into SUBCELLULAR FRACTIONS.Enzyme Replacement Therapy: Therapeutic replacement or supplementation of defective or missing enzymes to alleviate the effects of enzyme deficiency (e.g., GLUCOSYLCERAMIDASE replacement for GAUCHER DISEASE).Dipeptidyl-Peptidases and Tripeptidyl-Peptidases: A subclass of exopeptidases that includes enzymes which cleave either two or three AMINO ACIDS from the end of a peptide chain.Mice, Inbred C57BLTime Factors: Elements of limited time intervals, contributing to particular results or situations.Iduronate Sulfatase: An enzyme that specifically cleaves the ester sulfate of iduronic acid. Its deficiency has been demonstrated in Hunter's syndrome, which is characterized by an excess of dermatan sulfate and heparan sulfate. EC 3.1.6.13.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Hexosaminidase A: A mammalian beta-hexosaminidase isoform that is a heteromeric protein comprized of both hexosaminidase alpha and hexosaminidase beta subunits. Deficiency of hexosaminidase A due to mutations in the gene encoding the hexosaminidase alpha subunit is a case of TAY-SACHS DISEASE. Deficiency of hexosaminidase A and HEXOSAMINIDASE B due to mutations in the gene encoding the hexosaminidase beta subunit is a case of SANDHOFF DISEASE.Enzyme Precursors: Physiologically inactive substances that can be converted to active enzymes.Leukodystrophy, Metachromatic: An autosomal recessive metabolic disease caused by a deficiency of CEREBROSIDE-SULFATASE leading to intralysosomal accumulation of cerebroside sulfate (SULFOGLYCOSPHINGOLIPIDS) in the nervous system and other organs. Pathological features include diffuse demyelination, and metachromatically-staining granules in many cell types such as the GLIAL CELLS. There are several allelic and nonallelic forms with a variety of neurological symptoms.Mucopolysaccharidosis II: Systemic lysosomal storage disease marked by progressive physical deterioration and caused by a deficiency of L-sulfoiduronate sulfatase. This disease differs from MUCOPOLYSACCHARIDOSIS I by slower progression, lack of corneal clouding, and X-linked rather than autosomal recessive inheritance. The mild form produces near-normal intelligence and life span. The severe form usually causes death by age 15.Thiolester HydrolasesAntipain: An oligopeptide produced by various bacteria which acts as a protease inhibitor.Histocytochemistry: Study of intracellular distribution of chemicals, reaction sites, enzymes, etc., by means of staining reactions, radioactive isotope uptake, selective metal distribution in electron microscopy, or other methods.EsterasesDisease Models, Animal: 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.Tay-Sachs Disease: An autosomal recessive neurodegenerative disorder characterized by the onset in infancy of an exaggerated startle response, followed by paralysis, dementia, and blindness. It is caused by mutation in the alpha subunit of the HEXOSAMINIDASE A resulting in lipid-laden ganglion cells. It is also known as the B variant (with increased HEXOSAMINIDASE B but absence of hexosaminidase A) and is strongly associated with Ashkenazic Jewish ancestry.Muramidase: A basic enzyme that is present in saliva, tears, egg white, and many animal fluids. It functions as an antibacterial agent. The enzyme catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. EC 3.2.1.17.Colchicine: A major alkaloid from Colchicum autumnale L. and found also in other Colchicum species. Its primary therapeutic use is in the treatment of gout, but it has been used also in the therapy of familial Mediterranean fever (PERIODIC DISEASE).Chediak-Higashi Syndrome: A form of phagocyte bactericidal dysfunction characterized by unusual oculocutaneous albinism, high incidence of lymphoreticular neoplasms, and recurrent pyogenic infections. In many cell types, abnormal lysosomes are present leading to defective pigment distribution and abnormal neutrophil functions. The disease is transmitted by autosomal recessive inheritance and a similar disorder occurs in the beige mouse, the Aleutian mink, and albino Hereford cattle.Biological Transport: The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.Subcellular Fractions: Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163)alpha-N-Acetylgalactosaminidase: A hexosaminidase with specificity for terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides.Mucopolysaccharidosis III: Mucopolysaccharidosis characterized by heparitin sulfate in the urine, progressive mental retardation, mild dwarfism, and other skeletal disorders. There are four clinically indistinguishable but biochemically distinct forms, each due to a deficiency of a different enzyme.N-Formylmethionine: Effective in the initiation of protein synthesis. The initiating methionine residue enters the ribosome as N-formylmethionyl tRNA. This process occurs in Escherichia coli and other bacteria as well as in the mitochondria of eucaryotic cells.Neuronal Ceroid-Lipofuscinoses: A group of severe neurodegenerative diseases characterized by intracellular accumulation of autofluorescent wax-like lipid materials (CEROID; LIPOFUSCIN) in neurons. There are several subtypes based on mutations of the various genes, time of disease onset, and severity of the neurological defects such as progressive DEMENTIA; SEIZURES; and visual failure.Mice, Inbred BALB CEndosomes: Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. Endosomes internalize macromolecules bound by receptors on the cell surface.
... lysosomal protective protein, deamidase, lysosomal carboxypeptidase A, phaseolin) is an enzyme. This enzyme catalyses the ... lysosomal protective protein)". J. Biol. Chem. 267: 2872-2875. PMID 1737744. Miller, J.J.; Changaris, D.G.; Levy, R.S. (1992 ... Valls, L.A.; Hunter, C.P.; Rothman, J.H.; Stevens, T.H. (1987). "Protein sorting in yeast: the localization determinant of ... following chemical reaction Release of a C-terminal amino acid with broad specificity This enzyme is a carboxypeptidase with ...
1991). "Human lysosomal protective protein has cathepsin A-like activity distinct from its protective function". J. Biol. Chem ... This gene encodes a glycoprotein that associates with lysosomal enzymes beta-galactosidase and neuraminidase to form a complex ... 1992). "Human lysosomal protective protein. Glycosylation, intracellular transport, and association with beta-galactosidase in ... Probable identity with the lysosomal "protective protein"". J. Biol. Chem. 265 (19): 11265-72. PMID 1694176. Zhou XY, Galjart ...
The protein encoded by this gene encodes the lysosomal enzyme, which cleaves terminal sialic acid residues from substrates such ... protective protein'). Mutations in this gene can lead to sialidosis. Deficiencies in the human enzyme NEU1 leads to sialidosis ... Sialidase 1 (lysosomal sialidase), also known as NEU1 is a mammalian lysosomal neuraminidase enzyme which in humans is encoded ... "Transport of human lysosomal neuraminidase to mature lysosomes requires protective protein/cathepsin A". EMBO J. 17 (6): 1588- ...
Secretory products: Hormones, mucus, digestives enzymes, neurotransmitters, fibrous proteins, and hydrochloric acid are all ... These pigments have protective functions in skin and aid in the sense of sight in the retina but their functions in neurons is ... some believed that they have lysosomal activity. ... that these structures are crystalline forms of certain proteins ... The enzymes responsible for glycogenolysis degrade glycogen into individual molecules of glucose and can be utilized by ...
There is no one protein in semen responsible for the reaction. Symptoms can appear after first intercourse or after subsequent ... The seminal plasma provides a nutritive and protective medium for the spermatozoa during their journey through the female ... In humans, seminal fluid contains several components besides spermatozoa: proteolytic and other enzymes as well as fructose are ... The ductuli efferentes possess cuboidal cells with microvilli and lysosomal granules that modify the ductal fluid by ...
Welsh IR, Spitznagel JK (1973). "Distribution of lysosomal enzymes, cationic proteins, and bactericidal substances in ... "Entrez Gene: SPACA3 sperm acrosome associated 3". Niyonsaba F, Ogawa H (2006). "Protective roles of the skin against infection ... Sperm acrosome membrane-associated protein 3 is a protein that in humans is encoded by the SPACA3 gene. It may be involved in ... 2005). "The spermatozoa protein, SLLP1, is a novel cancer-testis antigen in hematologic malignancies". Clin. Cancer Res. 10 (19 ...
... lysosomal proteins, and the exoplasmic domains of membrane proteins. There are notable exceptions to this rule. For example, ... Disulfide bonds play an important protective role for bacteria as a reversible switch that turns a protein on or off when ... Feathers have similar keratins and are extremely resistant to protein digestive enzymes. The stiffness of hair and feather is ... The in vivo oxidation and reduction of protein disulfide bonds by thiol-disulfide exchange is facilitated by a protein called ...
... lysosomal proteins, and the exoplasmic domains of membrane proteins. There are notable exceptions to this rule. For example, ... Disulfide bonds play an important protective role for bacteria as a reversible switch that turns a protein on or off when ... Feathers have similar keratins and are extremely resistant to protein digestive enzymes. Different parts of the hair and ... The native form of a protein is usually a single disulfide species, although some proteins may cycle between a few disulfide ...
The protein encoded by this gene is a lysosomal cysteine proteinase and member of the peptidase C1 family. It exhibits both ... Cathepsin Z has an exposed integrin-bindign Arg-Gly-Asp motif within the propeptide of the enzyme, through which cathepsin Z ... Cathepsin Z is also reported to have a protective, but not proteolytic, function in inflammatory gastric disease. It is ... Cathepsin Z, also called cathepsin X or cathepsin P, is a protein that in humans is encoded by the CTSZ gene. It is a member of ...
"Alternative splicing of beta-galactosidase mRNA generates the classic lysosomal enzyme and a beta-galactosidase-related protein ... Activation, stabilization and association with beta-galactosidase and its protective protein". European Journal of Biochemistry ... Structure-function studies of lysosomal beta-galactosidase and the non-lysosomal beta-galactosidase-like protein". Biochimica ... In corn (Zea mays), Glb1 is a gene coding for the storage protein globulin. GM1-gangliosidosis is a lysosomal storage disease ...
Increased AP-1 and NF-κB obviously also result in an up-regulation of mdm2 protein, which decreases p53 protein levels. Thus, ... With the enzyme inhibited, the energy system of the cell is disrupted resulting in cellular apoptosis. Biochemically, arsenic ... Although arsenic causes toxicity, it can also play a protective role. Arsenite inhibits not only the formation of acetyl-CoA ... 3 As concentrations substantially lower than concentrations required for inhibition of the lysosomal protease cathepsin L in B ...
MacIcková, T; Navarová, J; Urbancíkova, M; Horáková, K (1999). "Comparison of isoproterenol-induced changes in lysosomal enzyme ... Horáková, K; Vlcková, A; Lukácová, D (1993). "Expression of disodium cromoglygate 'protective' effects observed during V79 cell ... protein content measurement and direct cell counting". Biologia. 51 (3): 305-11. Kocáková, P.; Leško, J.; Horáková, K.; Golais ... Navarová, Jana; Mačičková, Tatiana; Horáková, Katarina; Urbančíková, Miroslava (1999). "Stobadine inhibits lysosomal enzyme ...
... indicating that this protein plays a protective role in neuroendocrine cells and illustrating a link between diabetes and ... Parkin has been demonstrated to bind and ubiquitinylate UCH-L1 to promote lysosomal degradation of UCH-L1. Ubiquitin carboxyl- ... Ubiquitin carboxy-terminal hydrolase L1 (EC 3.1.2.15, ubiquitin C-terminal hydrolase, UCH-L1) is a deubiquitinating enzyme. UCH ... Human UCH-L1 and the closely related protein UCHL3 have one of the most complicated knot structure yet discovered for a protein ...
Some lysosomal enzymes are elevated, including tartrate-resistant acid phosphatase, hexosaminidase, and a human chitinase, ... The enzyme is a 55.6-kilodalton, 497-amino acid-long protein that catalyses the breakdown of glucocerebroside, a cell membrane ... Type III (also one or two copies of L444P, possibly delayed by protective polymorphisms) occurs in Swedish patients from the ... Last reviewed 8 August 2014 Clinical Policy Bulletin Number: 0442: Enzyme-replacement Therapy for Lysosomal Storage Disorders ...
The lysosomal enzymes cleave the T4 from the iodinated thyroglobulin. The thyroid hormones cross the follicular cell membrane ... Triiodothyronine bound to proteins in the PDB Thyroxine bound to proteins in the PDB T4 at Lab Tests Online Thyroid hormone ... which causes the brain to enter a protective cycle, useful in preventing damage during ischemic shock. Synthetic thyroxine was ... The thyroglobulin protein accounts for approximately half of the protein content of the thyroid gland.[citation needed] Each ...
Lysosomal integrity was well preserved until late, and the destruction of the cell did not appear to be caused by lytic enzymes ... This protective effect of hypothermia on renal ischaemic damage was confirmed by Bogardus who showed a protective effect from ... In Cohen's study there was a progressive increase in urinary protein concentration during 8 day preservation until the protein ... Measurements of lysosomal enzyme release from kidneys subjected to sham anastomoses, when either in or out of the cooling ...
The lysosomal enzymes cleave the T4 from the iodinated thyroglobulin.. *The thyroid hormones cross the follicular cell membrane ... The thyroglobulin protein accounts for approximately half of the protein content of the thyroid gland.[citation needed] Each ... which causes the brain to enter a protective cycle, useful in preventing damage during ischemic shock. ... in the first reaction catalysed by the enzyme thyroperoxidase, tyrosine residues in the protein thyroglobulin are iodinated on ...
Lewy bodies may not cause cell death and they may be protective (with the abnormal protein sequestered or walled off). Other ... The gene used leads to the production of an enzyme that helps to manage PD symptoms or protects the brain from further damage. ... Other cell-death mechanisms include proteasomal and lysosomal system dysfunction and reduced mitochondrial activity. Iron ... At the same time, regimens for PD restrict proteins during breakfast and lunch, allowing protein intake in the evening. PD ...
Although most serpins control proteolytic cascades, some proteins with a serpin structure are not enzyme inhibitors, but ... One, SRP-6, performs a protective function and guards against stress-induced calpain-associated lysosomal disruption. Further, ... The serpin barley protein Z is highly abundant in barley grain, and one of the major protein components in beer. The genome of ... This covalent complex between enzyme and substrate is called an acyl-enzyme intermediate. For standard substrates, the ester ...
... the substrate protein gets unfolded and it is translocated across the lysosome membrane with the assistance of the lysosomal ... There are four pathways of autophagy and these are mediated by the autophagy-related genes and their associated enzymes.[6][7][ ... These results suggest autophagy is a normal protective process (chondroprotection) in the joint. ... WIPI2, a PtdIns(3)P binding protein of the WIPI (WD-repeat protein interacting with phosphoinositides) protein family, was ...
... the substrate protein gets unfolded and it is translocated across the lysosome membrane with the assistance of the lysosomal ... The degradation of betaine homo-cysteine methyltransferase (BHMT), a metabolic enzyme, could be used to assess autophagy flux ... These results suggest autophagy is a normal protective process (chondroprotection) in the joint. ... WIPI2, a PtdIns(3)P binding protein of the WIPI (WD-repeat protein interacting with phosphoinositides) protein family, was ...
These enzymes are primarily localized in lysosomes and function in terminal protein degradation and processing. Cathepsins also ... This finding was credited to the protective properties PAI-1 imparts against excessive degradation of the surrounding ECM by ... Turk, V; Turk, B; Turk, D (2003). "Lysosomal cysteine proteases: facts and opportunities". EMBO J. 20 (17): 4629-4633. doi: ... which is cleaved to activate the enzyme Catalytic domain, which contains the conserved Zn2+ binding region and mediates enzyme ...
Ataxin-3 is the protein that, in the deubiquitinating enzyme function, forms SCA type-1 and 2 DRPLA intranuclear inclusions ( ... Finally, it is shown that aggresome-forming proteins become membrane-bound and associate with lysosomal structures. Together, ... overexpression of an insoluble or mutant protein, etc. The formation of the aggresome is largely believed to be a protective ... Parkin is the protein that, in the protein ligase function, forms Lewy bodies (the regular wild-type protein localized to ...
The coagulation system or clotting cascade, which forms a protective protein mesh over sites of injury. The fibrinolysis system ... Elevations in plasma enzymes, myoglobinemia, and abnormal muscle histology and ultrastructure are concluded to be associated ... enhancing the lysosomal elimination of the infective agent. * non-exhaustive list Specific patterns of acute and chronic ... These proteins include C-reactive protein, serum amyloid A, and serum amyloid P, which cause a range of systemic effects ...
Enzyme Various, e.g., alkaline phosphatase, patatin Cell attachment-recognition site Various proteins involved in cell-cell (e. ... of lysosomal enzymes. *Mucolipidosis: I-cell disease (ML II). *Pseudo-Hurler polydystrophy (ML III) ... Lubricant and protective agent Mucins Transport molecule Transferrin, ceruloplasmin Immunologic molecule Immunoglobulins,[11] ... Antifreeze protein Certain plasma proteins of coldwater fish Interact with specific carbohydrates Lectins, selectins (cell ...
... it may be evolutionarily desirable for an organism to avoid reproduction and to up-regulate protective and repair enzyme ... Commonly consumed food components containing calories are carbohydrates, proteins and fat. In preliminary research, some non- ... "The anti-ageing effects of caloric restriction may involve stimulation of macroautophagy and lysosomal degradation, and can be ... brain and heart proteins, and mice placed on CR at 19 months of age show an increases in life span.[44] ...
Ganesan B, Rajesh R, Anandan R, Dhandapani N. Protective effect of betaine on changes in the levels of protein, glycoproteins ... Protective effect of betaine on changes in the levels of lysosomal enzyme activities in heart tissue in isoprenaline-induced ... The lysosomal pellets were resuspended in about 2 mL of sucrose for use as the enzyme sources were stored on ice until required ... Kalra J, Chaudhary AK, Prasad K. Role of oxygen free radicals and pH on the release of cardiac lysosomal enzymes. J Mol Cell ...
... lysosomal protective protein, deamidase, lysosomal carboxypeptidase A, phaseolin) is an enzyme. This enzyme catalyses the ... lysosomal protective protein)". J. Biol. Chem. 267: 2872-2875. PMID 1737744. Miller, J.J.; Changaris, D.G.; Levy, R.S. (1992 ... Valls, L.A.; Hunter, C.P.; Rothman, J.H.; Stevens, T.H. (1987). "Protein sorting in yeast: the localization determinant of ... following chemical reaction Release of a C-terminal amino acid with broad specificity This enzyme is a carboxypeptidase with ...
... and neuraminidase secondary to a defect of a lysosomal enzyme protective protein/cathepsin A (PPCA) and mutation in CTSA gene. ... lysosomal protective protein , protective protein for beta-galactosidase , protective protein for beta-galactosidase ( ... Protein Überblick This gene encodes a glycoprotein which associates with lysosomal enzymes beta-galactosidase and neuraminidase ... lysosomal carboxypeptidase A , protective protein cathepsin A , urinary kininase ...
... is a multifunctional enzyme with distinct protective and catalytic function. CTSA that is present in the lysosomal multienzyme ... is a multifunctional enzyme with distinct protective and catalytic function. CTSA that is present in the lysosomal multienzyme ... complex facilitates correct lysosomal routing, stability and activation of betagalactosidase and alpha-neuraminidase. In ... complex facilitates correct lysosomal routing, stability and activation of betagalactosidase and alpha-neuraminidase. In ...
Rat model experiments in portal hypertensions have also shown a lower level of protective antioxidant enzymes and, on the other ... raising the level of lysosomal enzymes and of harm-free radicals in gastric mucosal homogenates. ... An experiment in which a protein - p53-upregulated modulator of apoptosis (PUMA) - induced in gastric mucosa of PHG patients as ...
Inhibition of protein synthesis separates autophagic sequestration from the delivery of lysosomal enzymes. J. Cell Sci. ... Inhibition of protein synthesis separates autophagic sequestration from the delivery of lysosomal enzymes. J. Cell Sci. ... p62 forms a shell around huntingtin protein aggregates The p62 protein is associated with protein aggregates in a number of ... Short-lived proteins are degraded by the proteasome, whereas long-lived proteins are degraded by autophagy. Protein aggregates ...
... including qualitative/quantitative urinary GAG analysis and a determination of enzyme activities, and then the molecular ... are rare inherited disorders caused by a deficit of the lysosomal hydrolases involved in the degradation of mucopolysaccharides ... β-galactosidase lysosomal enzyme or GLB1 is stabilised in a lysosomal multienzyme complex with protective protein/cathepsin A ( ... Alternative splicing of β-galactosidase mRNA generates the classic lysosomal enzyme and a β-galactosidase-related protein. J ...
Rudenko G, Bonten E, dAzzo A and Hol WGJ (1995) Three‐dimensional structure of the human protective protein: structure of ... such as that between a lysosomal enzyme and the phosphotransferase. Other examples of specific protein-protein interactions are ... Baranski TJ, Faust PL and Kornfeld S (1990) Generation of a lysosomal enzyme targeting signal in the secretory protein ... Baranski TJ, Cantor AB and Kornfeld S (1992) Lysosomal enzyme phophorylation. I. Protein recognition determinants in both lobes ...
... beta-Galactosidase Protective Protein; beta Galactosidase Protective Protein; Carboxypeptidase C; Carboxypeptidase Y; Lysosomal ... Enzymes: 34502*Hydrolases: 639*Peptide Hydrolases: 7577*Serine Proteases: 3067*Cathepsin A: 56*human CTSA protein ... 02/01/2000 - "However, up to now no information on the role of cathepsin A, a lysosomal multifunctional peptidase, in the ... 09/01/2013 - "The purified protein was effective in spermatophore wall rupture, and the subsequent HPLC-ESI-MS/MS shotgun ...
Stable expression of protective protein/cathepsin A-green fluorescent protein fusion genes in a fibroblastic cell line from a ... Model system for revealing the intracellular transport of normal and mutated lysosomal enzymes Yasunori NAGANAWA, Kohji ITOH, ... Identification of peroxisomal proteins by using M13 phage protein VI phage display: molecular evidence that mammalian ... Involvement of the core protein in the first β-N-acetylgalactosamine transfer to the glycosaminoglycan-protein linkage-region ...
"Protective role of the lipid phosphatase Fig4 in the adult nervous system, Human Molecular Genetics" on DeepDyve, the largest ... and the scaffold protein VAC14. The complex is maintained by protein-protein interaction and is destabilized by loss of FIG4 or ... Cellular levels of PI(3,5)P2 are regulated by an enzyme complex comprised of the kinase PIKFYVE, the phosphatase FIG4, and the ... Cells were fixed and stained for lysosomal marker LAMP1 (Abcam, 1: 1000) and MAG (Millipore, 1: 200) as described previously ( ...
Protective effect of prostaglandin E 1 (PGE 1 ) on lysosomal enzyme release in serotonin-induced gastric ulceration. ... The deduced amino acid sequences demonstrate that the HA of ts-61S varied from the wild type protein by three amino acids while ... Vardenafil works by blocking the PDE5 enzyme, which increases blood flow. By slowing these enzymes down, Vardenafil helps men ... from the enzyme of adult pigs, which is still insufficient to make sure the existence of two different forms of the enzyme. ...
However, unlike other members of this family, lysosomal neuraminidase requires the carboxypeptidase protective protein/ ... The enzyme is only catalytically active when it is bound to PPCA and is a component of a high molecular weight, multi protein ... Over 280,000 products but you cant find the right antibody for your protein or application?. Acris will do the search for you! ... Three types of neuraminidase are found in mammals and are defined as lysosomal, plasma membrane and cytosolic on the basis of ...
... "lysosomal protective protein" that is identical with lysosomal carboxypeptidase A. The protective function of lysosomal ... Human lysosomal beta-galactosidase and neuraminidase exist as a high molecular weight enzyme complex, in which there is also ... lysosomal carboxypeptidase A, lysosomal protective protein, protective protein, urinary kininase. ... Mutations in the gene encoding lysosomal carboxypeptidase A are the cause of the lysosomal disorder galactosialidosis. ...
1991). "Human lysosomal protective protein has cathepsin A-like activity distinct from its protective function". J. Biol. Chem ... This gene encodes a glycoprotein that associates with lysosomal enzymes beta-galactosidase and neuraminidase to form a complex ... 1992). "Human lysosomal protective protein. Glycosylation, intracellular transport, and association with beta-galactosidase in ... Probable identity with the lysosomal "protective protein"". J. Biol. Chem. 265 (19): 11265-72. PMID 1694176. Zhou XY, Galjart ...
Cathepsins are proteolytic enzymes with a broad spectrum of substrates. They are known to reside within endo-lysosomes where ... Stable expression of protective protein/cathepsin A-green fluorescent protein fusion genes in a fibroblastic cell line from a ... Lysosomal carboxypeptidase A. In: Barrett AJ, Rawlings ND, Woessner JF, editors. Handbook of proteolytic enzymes. 2nd ed. ... von Figura K. Molecular recognition and targeting of lysosomal proteins. Curr Opin Cell Biol. 1991;3(4):642-6.CrossRefGoogle ...
Renal Protective Effects of TM in db/db Mice. NAG is a lysosomal enzyme in proximal tubular cells and serves as an index of ... Protein concentrations were determined by the Bradford method, and 40 μg of protein was separated using 12% SDS-PAGE gel and ... The data on quantified protein expressions were normalized to the levels of GAPDH and related total proteins. The data were ... which encode detoxifying and antioxidant enzymes in consort with relevant proteins [68, 69]. Subsequently, the overproduced ROS ...
... but the implicated loci comprise multiple variants in linkage disequilibrium and rarely alter protein-coding sequence, which ... which encodes a lysosomal enzyme that processes antigens for MHC presentation23. Although dozens of SNPs at the locus are ... The most strongly associated SNP at the locus is rs11554159 (R76Q, G,A; minor allele is protective), a missense variant in ... However, as is typical of GWAS, the implicated loci comprise multiple variants in LD and rarely alter protein-coding sequence, ...
The endosomal-lysosomal system degrades accumulated proteins and functions as a protective factor in the central nervous system ... MicroRNA-339-5p down-regulates protein expression of β-Site Amyloid precursor protein-cleaving enzyme 1 (BACE1) in human ... 1998). Insu- lin-degrading enzyme regulates extracel- lular levels of amyloid beta-protein by deg- radation. J. Biol. Chem. 273 ... 2014) found that upregulated miR-128 could impair the clearance of Aβ through the targeting of lysosomal system enzymes in ...
Apocrine glands perform a crucial function by secreting enzymes such as lysosomal enzymes, cathepsin B, chymotrypsin, and ... Apocrine glands also produce cytokine,[21] which is a very important non-antibody protein that generates immune response when ... The protective and hygienic function of the foreskin. The foreskin, like the eyelid, also serves an important protective and ... The foreskin is designed by nature to be self cleaning and to provide significant natural immunological and protective function ...
... for 15 min and protein block (Dako serum-free protein block) for 10 min at RT to reduce nonspecific staining. Monoclonal rat ... we now must develop methods for counteracting immune and other protective responses of the host. In this context the prospects ... Lysosomal enzymes are ubiquitously expressed; deficiency of any one of these enzymes results in intralysosomal accumulation of ... Lysosomal enzyme quantification. IDUA and GUSB activities were measured in tissue homogenates and plasma using 4- ...
Lysosomal proteases of the cathepsin family exhibit up-regulation in response to accumulating proteins including Aβ1-42. ... to 10-fold increases in the enzymes activity in lysosomal fractions, while neprilysin and insulin-degrading enzyme remained ... Protective Effects of Positive Lysosomal Modulation in Alzheimers Disease Transgenic Mouse Models Jon Hasfjord ... Lysosomal proteases of the cathepsin family exhibit up-regulation in response to accumulating proteins including Aβ1-42. Here, ...
The elevated activity of lysosomal enzymes in various conditions was suggested to be due to increased synthesis of the enzymes ... Stevens L. Buffers and the determination of protein concentration. In : Enzyme Assays - A Practical Approach. Eisenthal R. and ... Earlier it has been suggested that this elevated ACP activity can be regarded as one of the protective mechanisms against ... Laske V., Stein B., Muller A., Fleck C., and Linss W. The effect of chronic aluminum leading on lysosomal enzymes in serum and ...
The protective effect of Scu on ISO-induced MI was evaluated by measuring markers of heart injury in serum, levels of lipid ... The purpose of this study was to investigate the protective effect of Scu on myocardial infarction (MI) induced by isoprenaline ... Chlorogenic acid ameliorates isoproterenol-induced myocardial injury in rats by stabilizing mitochondrial and lysosomal enzymes ... 2. Meena B, Anbu Rajan L, Anandan R. Protective effect of betaine on protein, glycoproteins and amino acids in isoprenaline- ...
The cancer tissue page shows antibody staining of the protein in 20 different cancers. ... Lysosomal protective protein Lysosomal protective protein 32 kDa chain Lysosomal protective protein 20 kDa chain. ... Enzymes. ENZYME proteins. Hydrolases. Peptidases. Serine-type peptidases. MEMSAT3 predicted membrane proteins. MEMSAT-SVM ... Lysosomal protective protein Lysosomal protective protein 32 kDa chain Lysosomal protective protein 20 kDa chain. ...
  • Studies indicate the transcript accumulation of the beta-galactosidases (BGAL) genes AtBGAL1 (At3g13750), AtBGAL2 (At3g52840), AtBGAL3 (At4g36360), AtBGAL4 (At5g56870), AtBGAL5 (At1g45130) and AtBGAL12 (At4g26140) along the plant development, as well as their subcellular location by the construction of transgenic plants producing the enhanced green fluorescent protein (eGFP) fused to the six BGAL proteins. (antikoerper-online.de)
  • deficiency of any one of these enzymes results in intralysosomal accumulation of substrate thereby causing development of progressive systemic and central nervous system disease [ 1 ]. (pubmedcentralcanada.ca)
  • Here, the lysosomal modulator Z-Phe-Ala-diazomethylketone (PADK) was used to test whether proteolytic activity can be enhanced to reduce the accumulation events in AD mouse models expressing different levels of Aβ pathology. (bioquant.com)
  • These findings indicate that pharmacologically-controlled lysosomal modulation reduces Aβ1-42 accumulation, possibly through intracellular truncation that also influences extracellular deposition, and in turn offsets the defects in synaptic composition and cognitive functions. (bioquant.com)
  • The selective modulation promotes clearance at different levels of Aβ pathology and provides proof-of-principle for small molecule therapeutic development for AD and possibly other protein accumulation disorders. (bioquant.com)
  • Thus, by promoting autophagic protein clearance, PSA helps protect against accumulation of aggregation-prone proteins and proteotoxicity. (harvard.edu)
  • A reliable, characterized and validated model of synucleinopathies (disorders in which there is an excessive accumulation of the protein alpha-synuclein) would provide a critical tool with which to study the pathophysiology of Parkinson's disease (PD) and test potential neuroprotective therapies. (michaeljfox.org)
  • Neuroprotective Role - Brahmi is neuroprotective, prevents oxidative stress and reverses this as well as the ultra structural changes in the hippocampus, prevents the accumulation of lipid and protein damage. (devang.house)
  • Impaired protein clearance likely increases the risk of protein accumulation disorders including Alzheimer's disease (AD). (uncg.edu)
  • The lysosomal storage disease GM1-gangliosidosis, an autosomal recessive deficiency of lysosomal acid β-galactosidase is biochemically characterized by accumulation of GM1-ganglioside in the central nervous system (CNS), and partially degraded glycoproteins, keratan sulfate and oligosaccharides in visceral organs. (uu.nl)
  • Those with Gaucher disease are deficient in an enzyme that breaks down glucoslyceramide, which leads to the accumulation of waste products. (wordpress.com)
  • Protective role of the lipid phosphatase Fig4 in the adult nervous system 2018-04-24 00:00:00 Abstract The signaling lipid phosphatidylinositol 3,5-bisphosphate, PI(3,5)P2, functions in vesicular trafficking through the endo-lysosomal compartment. (deepdyve.com)
  • Endo-lysosomal pathways are essential in maintaining protein homeostasis in the cell. (uncg.edu)
  • Interestingly, an interaction of cytosolic LDLR C-terminus with AMPK blocks ALDH2 phosphorylation and subsequent nuclear translocation, whereas ALDH2 rs671 mutant in human macrophages attenuates this interaction, which releases ALDH2 to the nucleus to suppress ATP6V0E2 expression, resulting in increased foam cells due to impaired lysosomal function. (jci.org)
  • Puromycin-sensitive aminopeptidase (PSA) is the only cytosolic enzyme able to digest polyQ sequences. (harvard.edu)
  • While the mutant CTSA protein retained its ability to form a complex with β-gal and Neu1, it has abolished enzymatic activity. (frontiersin.org)
  • In this study, we aimed to clarify significance of lysosomal CTSA in the regulation of several endogenous bioactive peptides including bradykinin, substances P, oxytocin, angiotensin I as well as endothelin-I in different tissues from CTSA S190A mice model at two different age groups. (frontiersin.org)
  • Inhibition of autophagy led to an increase in the size and number of p62 bodies and p62 protein levels. (rupress.org)
  • We suggest that p62 may, via LC3, be involved in linking polyubiquitinated protein aggregates to the autophagy machinery. (rupress.org)
  • Transcriptome analysis of the epidermis of Hes1(-/-) mouse revealed the direct relationship between Hes1 (hairy and enhancer of split-1) and BNIP3 (BCL2 and adenovirus E1B 19-kDa-interacting protein 3), a potent inducer of autophagy. (jove.com)
  • Keratinocyte differentiation is going along with activation of lysosomal enzymes and organelle clearance, expecting the contribution of autophagy in this process. (jove.com)
  • wherein optionally the protein comprises or consists of a Tat-Atg5K130R (Tat-Atg5 K130R ) (inhibitor of autophagy), a Tat-Beclin 1 (stimulates or increases autophagy), or a peptidomimetic or synthetic form thereof, or an equivalent thereof. (freepatentsonline.com)
  • As the most stable and specific of the known autophagy components, the ubiquitin E1-like activating enzyme Atg8/LC3 is currently the field's gold standard diagnostic tool ( 10 , 11 , 12 ). (jimmunol.org)
  • Cellular levels of PI(3,5)P2 are regulated by an enzyme complex comprised of the kinase PIKFYVE, the phosphatase FIG4, and the scaffold protein VAC14. (deepdyve.com)
  • Introduction The biosynthetic complex that generates phosphatidylinositol-3,5-bisphosphate [PI(3,5)Pis evolutionarily conserved in eukaryotes and includes the 5-phosphate kinase PIKFYVE, the 5-phosphatase FIG4, and the scaffold protein VAC14. (deepdyve.com)
  • Additionally, TM increased the expression of nuclear respiratory factor 2 (Nrf2), catalase, heme oxygenase 1, heme oxygenase 2, and manganese superoxide dismutase 2 and decreased the expression of protein kinase C alpha, phosphor-janus kinase 2, phosphor-signal transducer and activator of transcription 3, and phosphor-nuclear factor- κ B in the kidneys. (hindawi.com)
  • Phosphorylation of Bcl-2 seems to be required for this anti-apoptotic effect because the protection is amplified by pre-treatment with phorbol 12-myristate 13-acetate, which promotes protein kinase C (PKC)-dependent phosphorylation of Bcl-2. (diva-portal.org)
  • Analogous to typical inflammatory signaling response such as those mediated through classical immune receptors, b-amyloid and prion proteins activate a common tyosine kinase-dependent pathway. (artscolumbia.org)
  • Microglial treated with inhibitors of specific protein in the tyrosine kinase-based pathway successfully blocked amyloid-stimulated secretion of neurotoxins and reduced the number of cell death. (artscolumbia.org)
  • One important function of LRRK2 is to modify itself and proteins called Rab GTPases in a process known as a kinase activity. (michaeljfox.org)
  • B. monnieri enhances protein kinase activity in the hippocampus which may also contribute to its nootropic action and thus it would aids in repair of damaged neurons by enhancing kinase activity, neuronal synthesis and restoration of synaptic activity and ultimately nerve impulse transmission. (devang.house)
  • When AllerFree from Pure Essence Labs is taken between meals, the protease (protein digesting) enzymes help digest proteins (from yeasts, molds, pollen, animal dander, etc.) before the immune system reacts to them, thus preventing the release of histamine. (needs.com)
  • Steroidal and nonsteroidal antiinflammatory drugs inhibited the enzyme release process but not neutral protease activity, whereas goid and chloroquine inhibited the enzyme activity without affecting the release process. (docme.ru)
  • This delayed cell death seems to arise from activation of phospholipases, in particular phospholipase A2 (PLA2), which may dcstabilize lysosomal as well as mitochondrial membranes. (diva-portal.org)
  • 2. Released lysosomal enzymes, and activated PLA2, cause enhanced mitochondrial production of reactive oxygen as wel1 as release of cytochrome c. (diva-portal.org)
  • however, flavin-dependent enzymes in the mitochondrial matrix may produce the reactive oxygen species at much higher rates than complex I [ 3 ]. (hindawi.com)
  • There are five major types of primary intracellular antioxidant enzymes, that is, Cu/Zn-superoxide dismutase (Cu/Zn-SOD, SOD1) in the cytosol, manganese superoxide dismutase (Mn-SOD, SOD2) in the mitochondrial matrix, catalase, glutathione peroxidase (GPx), and glutathione reductase (GR). The SODs dismute superoxide to oxygen and hydrogen peroxide, while catalase and GPx convert hydrogen peroxide into H 2 O and O 2 . (hindawi.com)
  • These events may promote damage to cells by causing alterations in mitochondrial and sarcoplasmic reticular membranes and breakdown of lysosomal membranes. (biomedcentral.com)
  • 2000 ). Betaine is nonperturbing to cellular metabolism, highly compatible with enzyme function, and stabilizes cellular metabolic function under different kinds of stress in various organisms and animal tissues (Hanson et al. (pubmedcentralcanada.ca)
  • We investigated the function of the GLB1 and EBP mutated proteins by analyzing the clinical, genetic, and cellular data of 11 G(M1)-gangliosidosis patients. (unisi.it)
  • Composition Organic matrix Type-I collagen (90%) Non collagenous protein (osteocalcin) Cellular 4/19/12 Minerals Calcium. (scribd.com)
  • Under physiological conditions there is a cellular balance between ROS generation and clearance, since eukaryotic cells have several antioxidative defense mechanisms, including enzymes and antioxidants. (hindawi.com)
  • These proteins participate in a broad array of cellular functions and implicate new pathways in the viral life cycle. (sciencemag.org)
  • The enzymes contained in the lysosome sac are hydrolytic enzymes, which break down a variety of biomolecules, including: proteins, carbohydrates, fats, and other cellular debris. (wordpress.com)
  • In doing so, active enzymes are supplied, reducing the aggregation of waste of cellular products. (wordpress.com)
  • Another intra‐Golgi enzyme, N ‐acetylglucosamine 1‐phosphodiester α‐ N ‐acetylglucosaminidase later exposes the Man 6‐P marker by removing the covering GlcNAc. (embopress.org)
  • Edema of the Golgi body occurs, preventing the transport of proteins out of the cell. (stuvia.com)
  • Further analysis revealed previously unknown roles for retrograde Golgi transport proteins (Rab6 and Vps53) in viral entry, a karyopherin (TNPO3) in viral integration, and the Mediator complex (Med28) in viral transcription. (sciencemag.org)
  • The protective effect of Scu on ISO-induced MI was evaluated by measuring markers of heart injury in serum, levels of lipid peroxidation, and antioxidants in heart tissue, observing pathological changes of tissue, and detecting quantified expression of apoptotic-related family members and inflammation. (ac.ir)
  • HOCl and HOSCN were shown to modify both the protein and lipid component of LDL, with HOSCN contributing to significant lipid peroxidation, while HOCl mainly led to apoB100 modification. (edu.au)
  • through sequential enzymes digested by β-secretase (beta-site amyloid precursor protein cleaving enzyme1, BACE1) and γ-secretase (consisting of presenilin1 and presenilin2) ( Querfurth and LaFerla, 2010 ). (frontiersin.org)
  • Amyloid proteins are a distinct class of proteins that can misfold into β-sheet rich structures that later mature to form the characteristic species known as amyloid fibrils, and accumulate in tissues in the human body. (diva-portal.org)
  • However, the APP(Amyloid Precursor Protein) and its proteolytic fragments have been implicated more often than not and is the focus of most current studies. (artscolumbia.org)
  • Disease, b-Amyloid proteins derived from APP are the main component of neuritic plaques. (artscolumbia.org)
  • Many earlier studies found that prion peptides and b-amyloid proteins activate microglial cells by secreting cytokines, reactive oxygen species, and other neurotoxins. (artscolumbia.org)
  • Amyloidosis is a disease that occurs when amyloid proteins build up in your organs. (bensfriends.org)
  • Amyloid is an abnormal protein usually produced by cells in your bone marrow that can be deposited in any tissue or organ. (bensfriends.org)
  • In this study, we report that polymerization of the polyubiquitin-binding protein p62/SQSTM1 yields protein bodies that either reside free in the cytosol and nucleus or occur within autophagosomes and lysosomal structures. (rupress.org)
  • Inflammasomes are multimeric self-assembling protein complexes within the cytosol of mammalian cells, pattern-recognizing components of the innate immune system. (anti-agingfirewalls.com)
  • This enzyme catalyzes the hydrolysis of a terminal beta-linked galactose residue from ganglioside substrates and other glycoconjugates. (genecards.org)
  • Defective enzyme activity leading to the different types of mucopolysaccharidosis (MPS) is indicated in blue. (biomedcentral.com)
  • Baruch A, Jeffery DA, Bogyo M. Enzyme activity-it's all about image. (springer.com)
  • Activity-based protein profiling of host-virus interactions. (springer.com)
  • We studied the duration of expressed therapeutic enzyme activity, transgene presence by PCR, lysosomal pathology by toluidine blue staining and cell-mediated immune response histologically and by immunohistochemical staining. (pubmedcentralcanada.ca)
  • In immunomodulated transposon-treated MPS I mice plasma IDUA persisted for over 3 months at up to 100-fold WT activity in one-third of MPS I mice, which was sufficient to reverse lysosomal pathology in the liver and, partially, in distant organs. (pubmedcentralcanada.ca)
  • Although the activities of the enzymes may not be completely stable, a surprising amount of activity remained after 15 months. (aaccjnls.org)
  • Under these conditions, caspase-3 like activity was reduced 40-55%, suggesting that lysosomal enzymes could be upstream activators of caspase-3. (diva-portal.org)
  • Adamek E, Palowska-Goral K, Bober K (2005) In vitro and in vivo effects of fluoride ions on enzyme activity. (fluoridealert.org)
  • Without lysosomal activity, clearance of damaged mitochondria appears to be impaired, further exacerbating stress within the cell. (massgeneral.org)
  • 2009). The omega-3 fatty acid has protective effects are by induction of cytochrome CYP7A1 expression and the activity of cholesterol catabolism to bile acids (Kim et al. (academicjournals.org)
  • The study featured two primary goals: (1) to determine the free radical scavenging activity of PCOs and (2) to determine the inhibitory effects of PCOs on xanthine oxidase) and the lysosomal enzyme system which governs the release of enzymes which can damage the connective tissue framework which acts as a protective sheath surrounding capillary walls. (pdfmedsearch.com)
  • Non collagenous protein 1% of total protein in human bone During bone formation 10-30% of OC synthesized from osteoblast is released in circulation Synthesis stimulated by vit-D Excreted by kidney Half life is 5 min. (scribd.com)
  • For example, a future part will likely be concerned with the frequent decoupling of transcription and translation in protein synthesis, the code for what goes on at the Internal Ribosome Entry Sites " (or IRES ). (anti-agingfirewalls.com)
  • Hexa −/− mice, depleted of β-hexosaminidase A, remain asymptomatic to 1 year of age, because they catabolise G M2 ganglioside via a lysosomal sialidase into glycolipid G A2 , which is further processed by β-hexosaminidase B to lactosyl-ceramide, thereby bypassing the β-hexosaminidase A defect. (prolekare.cz)
  • It has been shown however that extracts of human leukocytes contain enzymes capable of reducing the viscosity of protein polysaccharide solutions at neutral pH (3) and we have demonstrated that these enzymes, also under physiologic conditions, can degrade the mucopolysaccharide matrix of rabbit ear cartilage (4). (docme.ru)
  • The changes in brain weight, acid and alkaline phosphoesterases, aspartate and alanine aminotransferases, reduced glutathione, thiobarbituric acid reactive substances, DNA, RNA and protein contents suggested a nonspecific impact of dietary protein status on the response of brain to aluminum exposure. (ispub.com)
  • According to animal research, brahmi extracts modulate the expression of certain enzymes involved in generation and scavenging of reactive oxygen species in the brain. (devang.house)
  • 2009 ) . Signals such as reactive O species ( ROS ) , cytotoxic lysosomal enzymes, and cytoskeletal changes could trip Hsps look in the cell. (yogurtlandsweettreats.com)
  • βG and β-hexosaminidase (EC 3.2.1.52 ), as a control enzyme, were measured (Chamoles NA, Blanco MB, Gaggioli D, Casentini C. Hurler-like phenotype: enzymatic diagnosis in dried blood spots on filter paper. (aaccjnls.org)
  • which resulted in complete correction of enzymatic deficiency and lysosomal storage throughout the GM1-gangliosidosis mouse forebrain. (uu.nl)
  • This paper stresses the central role of the laboratory in completing and confirming the clinical suspicion of MPS according to a standardized procedure: first, a biochemical evaluation of the patient samples, including qualitative/quantitative urinary GAG analysis and a determination of enzyme activities, and then the molecular diagnosis. (biomedcentral.com)
  • The autophagic marker light chain 3 (LC3) colocalized with p62 bodies and coimmunoprecipitated with p62, suggesting that these two proteins participate in the same complexes. (rupress.org)