Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.6.1 (sulfatase)
 3,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The normal distribution of several lysosomal enzymes was studied in 20 guinea pigs. In the outer hair cells lysosomal enzymes are mainly localized at the apical cell pole, while in inner hair cells the distribution was uniform. Nonlysosomal enzymes like alcaline phosphatase are of predominantly basal localization. The concentration of some lysosomal enzymes like N-acetyl-beta-glucosaminidase was higher in outer than in inner hair cells while others like acid phosphatase, beta-glucuronidase and sulfatase showed a stronger reaction in the inner hair cells. After 10 days of sound overstimulation with 120 dB for 1 h a day, there was an increase of lysosomal enzyme content namely in the outer hair cells. There was no change of non-lysosomal enzymes. Under these conditions there might be a partial destruction of cellular organelles eliminated by lysosomal activity without loss of a total cell. In addition the distribution and possible function of lysosomal enzymes in other labyrinthine tissues was discussed.
 ...
PMID:Distribution and possible function of lysosomal enzymes in the inner ear under normal and pathophysiological conditions. 98 23

A transmission electron microscopic study of demineralized, methaphyseal bone of the young guinea pig is presented. Special attention is paid to the lysosomal system of the different cell types. Visualization of acid phosphatase and aryl sulfatase activity was used to identify tissue components as belonging thereto. The distribution of alkaline phosphatase activity, a plasma membrane marker, was also examined. Osteoblasts were distinguished by a marked development of the granular endoplasmic reticulum and the Golgi complex. Perivascular cells type A, morphologically resembled the osteoblasts, and are believed to represent an early stage in the specialization of the latter. A few lysosomes were normally found in the osteoblasts; they were less common in the type A cells. In contrasts to their regular occurrence in guinea pig epiphyseal cartilage, dense bodies of lysosomal nature ("type I vesicles") were only rarely seen in the bone matrix. Structures analogous to the type II vesicles in cartilage were, however, normally present. Their membrane showed activity of alkaline phosphatase. Possible functions of lysosomes and matrix vesicles in osteogenesis are discussed. Perivascular cells type B and chondroclasts both contained a prominent Golgi complex and large numbers of free ribosomes, mitochondria and lysosomes. In the type B cells, inclusion material of varying appearance often occurred in the lysosomes and in endocytic vesicles. The chondroclasts sometimes presented a ruffled border, with associated vacuoles and lysosomes in the subjacent cytoplasm. It is suggested that both cell types participate in the resorption of the epiphyseal cartilage. Chondroclasts presumably arise by fusion of type B cells and/or monocytic precursors from the peripheral blood.
 ...
PMID:Electron microscopie and enzyme cytochemical studies on the guinia pig metaphysis with special reference to the lysosomal system of different cell types. 109 55

After injection of Triton WR 1339 and dextran into mice, phagolysosomes containing both compounds were obtained from the liver regardless of the order of injection of these materials. This suggests that phagososomes containing the other material. The recoveries of various lysosomal enzymes differed in phagolysosomes after injection of Triton WR 1339 with or without dextran: recoveries of beta-glucuronidase, beta-N-acetylglucosaminidase and arylsulfatase were high, and that of acid phosphatase was low.
 ...
PMID:Formation of phagolysosomes containing dextran and Triton WR 1339 in mouse liver. 113 62

Acid hydrolase activities were compared in human leucocytes, guinea pig and human alveolar macrophages. Several enzymes were characterized: N-acetyl-beta-D-glucosaminidase, N-acetyl-alpha- and beta-D-galactosaminidase, alpha and beta-D-galactosidase, alpha-D-mannosidase, alpha-L-fucosidase, beta-D-glucuronidase, neuraminidase, acid phosphatase and arylsulfatase. The enzymatic activities were lower in leucocytes than in alveolar macrophages, higher in human macrophages than in guinea pig macrophages, except for beta-D-glucuronidase, acid phosphatase and arylsulfatase activities.
 ...
PMID:[Comparative studies of the acid hydrolases of human leucocytes and human and guinea pig alveolar macrophages. I. Study of the activities of glycosidases, arylsulfatase and acid phosphatase (author's transl)]. 117 6

Platelets secrete lysosmal enzymes during the "platelet release reaction" early in clot formation. This study was undertaken to identify primary lysosomes of platelets and to detemine their origin in megakaryocytes. Using electron microscopy and cytochemistry, we localized two lysosomal enzymes, arylsulfatase and acid phosphatase, in megakaryocytes and platelets of normal and thrombocytopenic rats. In platelets and mature megakaryocytes, reaction product for both enzymes is confined to vesicles measuring 175-250 nm. These vesicles, which are primary lysosmes, first appear in the earliest recognizable megakaryocytes and increase in number during cellular maturation. In immature and maturing megakaryocytes, arylsulfatase and acid phosphatase can also be demonstrated in an organell similar to GERL (Golgi-endoplasmic reticulumlysosome), i.e., single smooth-surfaced cisternal with associated vesicles near the stacked Golgi cisternae. Scant reaction product for acid phosphatase is also sometimes seen in Golgi cisternae and endoplasmic reticulum. No reaction product was found in alpha-granules at any stage of megakaryocyte maturation, nor in alpha- or serotonin granules of platelets. Thus, our findings indicate that the primay lysosomes of megakaryocytes and platelets are small vesicles derived from GERL early in megakaryocyte differentiation. They can be indentified only after cytochemical staining and are distinct from both alpha- and serotonin granules.
 ...
PMID:Cytochemical localization of lysosomal enzymes in rat megakaryocytes and platelets. 120 88

Aspects of the fine structure as well as electron cytochemical localization studies of certain hydrolytic enzymes were examined by electron microscopy of ultrathin sections of the vegatative hyphae and conidia of the phycomycetous fungus, Entomophthora coronata. This entomogenous fungal organism is of interest since it has been increasingly implicated as the etiologic agent of phycomycosis of man and animals. On thin section, hyphal cells were frequently observed with septa while the cytoplasm was multinucleate. The conidium was bound by a multilayered cell wall. The cytoplasm of ungerminated conidia characteristically contained large numbers of a class of cytoplasmic organelle found in loose aggregates with lipid storage bodies. Similar organelles were observed in the cytoplasm of hyphal cells from 7-day old cultures. This round to oval to slightly reniform structure was bound by a single limiting membrane and composed of an electron dense, slightly granular matrix without evidence of crystalloid formation. The limiting membrane of the lipid storage bodies was observed to be intimately associated with that of one or more of these microbody-like organelles. This intimate association of the two cytoplasmic organelles suggests that the microbody-like organelle may be involved in some manner with lipid metabolism during the life cycle of the fungus. Cautious interpretations of electron cytochemical localization studies suggested that lipase, nonspecific esterase, and possibly aryl sulfatase were associated with the microbody-like organelles. Neither peroxidatic nor acid phosphatase activity could be demonstrated with these organelles of the conidial cytoplasm.
 ...
PMID:Ultrastructural and electron cytochemical studies of Entomophthora coronata. 121 85

To evaluate lysosomal involvement in myocardial infarction, coronary artery thrombosis was induced by ligation in 16 dogs. Biopsies of infarcted and normal left ventricles were studied by ultrastructural cytochemistry and subcellular fractionation (0.25 M sucrose) from 30 min to 96 hrs post injury. Normal myocardium contained few "classical" (residual body) lysosomes: instead, acid phosphatase and aryl sulfatase were localized to longitudinal and to lateral sac elements of the sarcoplasmic reticulum. In postnuclear (450 X gm, 10 min) supernates, lysosomal acid phosphatase and beta-glucuronidase were divided 60:40 between sedimentable (98,000 X gm, 15 min) and non-sedimentable fractions of normal endocardium and epicardium (studied separately). At 2 hrs post infarction, ischemic muscle showed: 1) loss of membrane-bound acid phosphatase and aryl sulfatase; 2) mitochondrial damage; 3) loss of glycogen and disappearance of I but not A bands; and 4) entry into cells of colloidal lanthanum (= loss of plasma membrane integrity. Total lysosomal hydrolase did not increase until 6-5 hrs post infarct. At 2 hrs, significant increments (32 +/- 7%) were found in nonsedimentable acid phosphatase and beta-glucuronidase of endocardium (P less than 0.005 vs. normal) but the epicardium. In dogs given methylprednisolone (50 mg/k) 30 min post infarct, ultrastructural cytochemistry showed retention of lysosomal enzymes within endocardial sarcoplasmic reticulum and no significant redistribution of enzymes into non-sedimentable fractions (vs. eight paired, infarcted, untreated controls). Data show early disruption of lysosomes in myocardial infarction and their protection by steroid given after the acute insult.
 ...
PMID:Lysosomes in myocardial infarction: studies by means of cytochemistry and subcellular fractionation, with observations on the effects of methylprednisolone. 125 66

The mannose 6-phosphate (Man6P) residues that are necessary for the targeting of newly synthesized lysosomal proteins are dephosphorylated after delivery of lysosomal proteins to lysosomes. To examine the role of lysosomal acid phosphatase (LAP) for the dephosphorylation of Man6P residues in lysosomal proteins, the phosphorylation of endogenous lysosomal proteins and of internalized arylsulfatase A was analyzed in mouse L-cells that overexpress human LAP. Non-transfected L-cells dephosphorylate endogenous lysosomal proteins slowly (half time approximately 13 h) as well as internalized arylsulfatase A. A more than 100-fold overexpression of LAP in these cells did not affect the dephosphorylation rate. Control experiments showed that the internalized arylsulfatase A and overexpressed LAP partially colocalize and that under in vitro conditions purified LAP does not dephosphorylate arylsulfatase A. Taken together, these results indicate that LAP is not the mannose 6-phosphatase that dephosphorylates lysosomal proteins after their delivery to lysosomes.
 ...
PMID:Lysosomal acid phosphatase is not involved in the dephosphorylation of mannose 6-phosphate containing lysosomal proteins. 135 23

A new rapidly growing mycobacterium was isolated from human sputum. This organism grew at 22, 31, 37, and 41 degrees C and possessed catalase, acid phosphatase, acetamidase, urease, nicotinamidase, pyrazinamidase, and nitrate reductase activities. It did not produce nicotinic acid, hydrolyze Tween, or have benzamidase, isonicotinamidase, succinidamidase, and arylsulfatase activities. A mycolic acid analysis revealed a simple, unique pattern. The organism is susceptible to antituberculotic drugs. A comparative 16S rRNA sequence analysis placed this organism within the confines of the genus Mycobacterium, most closely related to the thermotolerant rapidly growing species. On the basis of the pattern of enzymatic activities and metabolic properties, as well as the unique 16S rRNA sequence, we propose that our single strain represents a new species, for which we propose the name Mycobacterium confluentis. The type strain is strain 1389/90; a culture of this strain has been deposited in the German Collection of Microorganisms and Cell Cultures as strain DSM 44017.
 ...
PMID:Mycobacterium confluentis sp. nov. 137 23

Lectin cytochemistry was performed to clarify the process of glycosylation and the localization of glycocalyx in osteoclasts. Microslicer sections of decalcified rat tibiae were incubated in the presence of HRP-conjugated lectins (Con A, PNA, MPA, WGA, UEA-1). Lectin reactions in cell organelles revealed that glucose (Glc) and mannose (Man) are transferred to carbohydrate chains in nuclear envelopes, rough endoplasmic reticuli, and the cis and medial sides of the Golgi apparatus. N-acetylgalactosamine (GalNAc), N-acetylglucosamine (GlcNAc), and/or N-acetylneuraminic acic (NANA) residues are transferred, in turn, in the Golgi apparatus. Lectin reactions detected in lysosomal structures suggest that some sugar residues are incorporated into carbohydrate chains of hydrolytic enzymes, such as acid phosphatase and arylsulfatase. Others would be transported to plasma membranes as glycocalyx. PNA and MPA reactions were most evident on ruffled borders of osteoclasts. On the other hand, cement-line-like structures on bone surfaces displayed Con A, MPA, and WGA positive reactions. The following factors suggest that osteoclasts actively metabolize sugar: characteristic localization of glycocalyx in osteoclasts reflect the polarity of osteoclasts, and carbohydrate complexes in cement-line-like structures seem to play an important role in the coupling phenomenon in bone tissue.
 ...
PMID:Characteristic localization of carbohydrates in osteoclasts by lectin cytochemistry. 147 18


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>