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Biomedical subjects

J Sy

Publications and source records attributed to J Sy.

At least 19 recordsLinked to original sources
PubMed1995

Hospitalized congestive heart failure patients with preserved versus abnormal left ventricular systolic function: clinical characteristics and drug therapy.

PURPOSE: To compare clinical characteristics of and pharmacologic therapy for hospitalized patients with congestive heart failure (CHF) and left ventricular systolic dysfunction or normal left ventricular systolic function. PATIENTS AND METHODS: Medical records were reviewed for all patients discharged with a principal diagnosis of CHF from a university hospital and a community hospital between September 1, 1991 and August 31, 1992. Pertinent medical history items and prescribed drug therapies at discharge were recorded for each patient's first calendar year admission. Patients were categorized as having either normal left ventricular systolic function or systolic dysfunction based on the results of echocardiography and radionuclide angiography or contrast ventriculogram. RESULTS: Of 298 patients with CHF, 92 (31%) had normal left ventricular systolic function. Patients with normal systolic function were older, were more often women, were less likely to have a history of coronary artery disease, and were more likely to have a history of hypothyroidism than patients with systolic dysfunction. However, the prevalence of clinical characteristics overlapped considerably between the two groups. Among patients with systolic dysfunction, 79% were discharged on a therapeutic regimen of digoxin, 65% on an angiotensin-converting enzyme inhibitor, and 26% on either a beta-blocker or a calcium channel blocker. Among patients with normal systolic function, 50% were discharged on a regimen of a beta-blocker or a calcium channel blocker and 38% were discharged on digoxin. Twenty-six percent of patients with normal systolic function and without a history of atrial fibrillation were discharged on a digoxin regimen. CONCLUSION: Hospitalized CHF patients with normal left ventricular systolic function and those with diminished left ventricular systolic function share many clinical features. Since recommended drug therapy and prognosis differ, our data underscore the importance of diagnostic testing to assess left ventricular systolic function. Drug therapy for CHF patients provides a major challenge for quality-of-care improvement.

Aged↗
PubMed1994

Identification of intraocular lens-adsorbed proteins in mammalian in vitro and in vivo systems.

OBJECTIVE: Mammalian in vitro and in vivo systems were used to study the protein-adsorbing potential of intraocular lenses (IOLs). METHODS: Intraocular lenses composed of polymethyl methacrylate optics with polypropylene haptics were incubated in rabbit plasma for 3 hours (in vitro grouping) or implanted in rabbit eyes for 48 hours (in vivo grouping). Lens-adsorbed proteins from both experimental groupings were eluted with sodium dodecyl sulfate and identified by Western Blot analyses. RESULTS: The adsorbed protein layer was composed of at least six different proteins: albumin, complement C3 fragments, IgG, fibrinogen/fibrin (as a fibrin clot in vivo), fibronectin, and transferrin. Of the identified components, albumin, IgG, fibronectin, and fibrinogen were the predominant protein species on the in vitro IOLs, while fibronectin and fibrin were on the in vivo IOLs. CONCLUSIONS: The composition of the protein layer has the potential to alter the biological property of IOLs.

Adsorption↗
PubMed1993

Nicardipine in heart failure: distinguishing its acute beneficial from its chronic effects.

Concern over negative inotropic effects has limited the use of calcium blockers in patients with congestive heart failure. Nicardipine, a second generation dihydropyridine calcium channel blocker, has demonstrated positive hemodynamic effects in short-term therapy in patients with congestive heart failure. Prolonged use of calcium channel blockers remains contraindicated in patients with congestive heart failure due to the potential for activation of the renin-angiotensin system. However, acute intravenous nicardipine administration has important clinical applications (as in the management of surgical hypertension or hypertensive emergencies). Nicardipine may be safely used for these indications even in the presence of congestive heart failure.

Acute Disease↗
PubMed1992

Dipeptide inhibitors of ubiquitin-mediated protein turnover prevent growth factor-induced neurite outgrowth in rat pheochromocytoma PC12 cells.

Dipeptide inhibitors of the ubiquitin-dependent proteolysis pathway governed by N-terminal recognition (N-end rule) in reticulocyte lysates significantly suppress NGF- and bFGF-induced neurite outgrowth in rat pheochromocytoma PC12 cells, but do not cause retraction of already formed neurites. Peptides which do not inhibit proteolysis are also without effect on PC12 cell differentiation. Suppression of neurite outgrowth is readily reversible upon removal of the inhibitors. These data demonstrate a requirement for specific protein turnover in the process of neuron-like differentiation in PC12 cells and provide the first demonstration of a physiological role for the N-end rule.

Animals↗
PubMed1987

Anomeric specificity of glucose effect on cAMP, fructose 1,6-bisphosphatase, and trehalase in yeast.

The addition of beta-D-glucose (final concentration, 50 mM) to a cell suspension of Saccharomyces cerevisiae in stationary phase caused a rapid 4-fold increase in the concentration of cAMP, while a 2-fold increase of cAMP was observed by the addition of alpha-D-glucose. beta -D-Glucose was also more effective than alpha-D-glucose in the inactivation of fructose 1,6-bisphosphatase and the activation of trehalase. These results, taken together with the previous report that alpha-D-glucose is transported more rapidly than beta-D-glucose in Saccharomyces cerevisiae, do not support the view currently proposed by some investigators that cotransport of D-glucose with protons causes the depolarization of the cell membrane, resulting in the activation of adenylate cyclase. The present data, however, provides supporting evidence for the view that cAMP-dependent protein kinase is implicated in the inactivation of fructose 1,6-bisphosphatase and the activation of trehalase.

Cyclic AMP↗
PubMed1986

An altered adenylate cyclase in cdc35-1 cell division cycle mutant of yeast.

Adenylate cyclase activity was studied in Saccharomyces cerevisiae's cell division cycle (cdc) mutant 35-1. The temperature sensitive mutant cdc35-1 was previously mapped as an allele of cyr, the adenylate cyclase gene. However, the adenylate cyclase activities of membranes prepared from cdc35-1 were not thermosensitive. The adenylate cyclase activity of cdc35-1 was found to have an altered Mn2+ dependency and did not respond to Gpp(NH)p stimulation. These results suggest that cdc35-1 mutation may not be at the catalytic site but at a site where adenylate cyclase interacts with regulatory proteins.

Adenylyl Cyclases↗
PubMed1985

Catabolite inactivation of fructose 1,6-bisphosphatase and cytoplasmic malate dehydrogenase in yeast.

Catabolite inactivation of fructose 1,6-bisphosphatase and cytoplasmic malate dehydrogenase was studied using the protease-deficient and vacuole-defective yeast strain pep4-3. The catabolite inactivation of fructose 1,6-bisphosphatase in pep4-3 was found to have a normal first inactivation step but with a defective second proteolytic step. In contrast, catabolite inactivation of cytoplasmic malate dehydrogenase was normal in pep4-3. These results suggest that the proteolytic pathways utilized in the hydrolysis of the two enzymes may be different and that proteolysis of fructose 1,6-bisphosphatase may require functional vacuoles while proteolysis of cytoplasmic malate dehydrogenase may not.

Cytoplasm↗
PubMed1985

Tyrosine sulfation of proteins from the human hepatoma cell line HepG2.

[35S]Sulfate labeling of the human hepatoma cell line HepG2 showed it to contain many sulfated proteins of diverse molecular weight range. The isolation of tyrosine O-sulfate indicated the supernatant fraction to contain a 5- to 7-fold higher level than the cellular fraction at the end of a 24-hr incubation. The proteins in the supernatant fraction were immunoprecipitated and examined for sulfation. Of 15 proteins tested, 7 were found to be sulfated as indicated by [35S]sulfate incorporation into proteins separated by NaDodSO4/PAGE and detected by autoradiography. The 35S-labeled bands were excised from the dried gel and subjected to extensive Pronase hydrolysis and the hydrolysates were analyzed for tyrosine [35S]sulfate by a two-dimensional procedure combining high-voltage electrophoresis and thin-layer chromatography [Liu, M. C. & Lipmann, F. (1984) Proc. Natl. Acad. Sci. USA 81, 3695-3698]. Of the sulfated proteins, three--fibrinogen, alpha-fetoprotein, and fibronectin--were found to contain tyrosine O-sulfate. The simultaneous presence of carbohydrate-bound sulfate, however, could not be exactly determined, but the other four [35S]sulfate-containing proteins--alpha 1-antitrypsin, alpha 1-antichymotrypsin, alpha 2-macroglobulin, and transferrin--did not reveal any tyrosine O-sulfate and might be sulfated on their carbohydrate moieties.

Carcinoma, Hepatocellular↗
PubMed1984

Purification and phosphorylation of fructose-1,6-bisphosphatase from Kluyveromyces fragilis.

Fructose-1,6-bisphosphatase from the yeast Kluyveromyces fragilis was found to have an apparent Mr = 155,000 and to be composed of four Mr = 35,000 subunits. The extent and rate of phosphorylation of fructose-1,6-bisphosphatase (Fru-1,6-P2) by yeast cAMP-dependent protein kinase were dependent on fructose-1,6-bisphosphatase inhibitors, 5'-AMP and fructose 2,6-bisphosphate (Fru-2,6-P2). In the absence of inhibitor, the enzyme was slowly phosphorylated with a maximum incorporation of 1 mol of phosphate/mol of enzyme. The presence of both inhibitors greatly increased the phosphorylation rate with a maximum incorporation of 2 mol of phosphate/mol of enzyme. The presence of only one inhibitor led to an intermediate rate of phosphorylation with 2 mol of phosphate incorporated/mol of enzyme. There was no significant change in enzymatic activity after phosphorylation. The estimated sedimentation coefficient of fructose-1,6-bisphosphatase was lowered by 5'-AMP from 8.2 to 5.7 while Fru-2,6-P2 increased the S value to 8.5. The presence of either Fru-1,6-P2 or Fru-2,6-P2 prevented the 5'-AMP lowering of S value. The susceptibility of enzyme to partial tryptic digestion was not changed by the presence of 5'-AMP. The presence of both Fru-2,6-P2 and 5'-AMP led to the protection of Mr = 35,000 subunit from tryptic digestion while Fru-2,6-P2 alone led to a protection of an Mr = 30,000 peptide fragment. This peptide fragment did not contain the phosphorylation sites. Our results suggest that the rapid regulation of fructose-1,6-bisphosphatase following glucose addition is controlled mainly by enzyme inhibitors.

Ascomycota↗
PubMed1983

Guanosine 5'-triphosphate, 3'-diphosphate 5'-phosphohydrolase. Purification and substrate specificity.

The regulatory nucleotide guanosine 5'-diphosphate, 3'-diphosphate (ppGpp) and its precursor guanosine 5'-triphosphate, 3'-diphosphate (pppGpp) are accumulated during stringent response in bacterial cells. The enzyme pppGpp-5'-phosphohydrolase, which catalyzes the conversion of pppGpp to ppGpp, was partially purified from Escherichia coli. It has Mr = 140,000 and an apparent Km of 0.11 mM for pppGpp. It requires Mg2+ and a monovalent cation. NH4+ is preferred over K+, while Na+ is inactive. The enzyme does not hydrolyze GTP, ATP, pppApp, or ppGpp. It is also not effectively inhibited by these nucleotides. pppGpp-5'-phosphohydrolase hydrolyzes the 3'-monophosphate analog pppGp equally well (apparent Km of 0.13 mM), yielding the recently identified MS III nucleotide (ppGp). pppGpp-5'-phosphohydrolase does not have RNA 5'-terminal gamma-phosphatase activity; however, 5'-terminal phosphates are released by pppGpp-5'-phosphohydrolase when the GTP-terminated RNA chains are first converted into oligonucleotides by RNase A treatment. pppGpp-5'-phosphohydrolase was found to actively hydrolyze the dinucleotide fragment pppGpNp but exhibited very low activity toward longer chain fragments. The 3'-unphosphorylated dinucleotide pppGpN was, however, not hydrolyzed. The ability of pppGpp-5'-phosphohydrolase to hydrolyze pppGpp, pppGp, and pppGpNp, but not pppG and pppGpN, indicates that pppGpp-5'-phosphohydrolase is rather nonspecific toward the 3'-OH substitutions of the substrates although a free, unsubstituted phosphate group at the 3'-OH position is essential.

Cations, Monovalent↗
PubMed1983

Enzymic synthesis and cofactor activity of 3'-pyrophosphocoenzyme A.

The 3'-pyrophosphate derivative of CoA was synthesized by using the excreted 5'-to-3' pyrophosphoryl-transferring enzyme from Streptomyces adephospholyticus and ATP as donor and dephospho-CoA as acceptor. Cofactor activity of this new coenzyme A derivative was tested with Clostridium kluyveri phosphotransacetylase and hog heart succinic thiokinase. With the phosphotransacetylase, 3'-pyrophospho-CoA was found to be twice as active as CoA whereas dephospho-CoA was inactive. However, succinic thiokinase utilized all three types of CoA equally well. Adenosine 5'-monophosphate 3'-pyrophosphate also was synthesized and used as an analog of adenosine 5'-monophosphate 3'-monophosphate in the dog liver's sulfotransferase-catalyzed sulfate transfer from p-nitrophenyl sulfate to phenol. In contrast to the pyrophospho derivative of coenzyme A, adenosine 5'-monophosphate 3'-pyrophosphate was inactive as a cofactor.

Animals↗
PubMed1982

Phosphorylation of the regulatory subunit of yeast cAMP-dependent protein kinase.

In vitro phosphorylation of the regulatory subunit of yeast cAMP-dependent protein kinase was studied. The cAMP-binding regulatory subunit (R subunit) can be multiply phosphorylated. Three distinct phosphorylation sites were inferred from the different ATP concentrations required for phosphorylation and from the presence of two discrete mobility shifts in NaDodSO4/polyacrylamide gel electrophoresis of the R subunit on phosphorylation. Limited tryptic digestion of the phosphorylated R subunit showed that a Mr 37,000 cAMP-binding peptide contained one of the phosphorylation sites and that a separate Mr 12,000 peptide contained another phosphorylation site. The yeast R subunit is therefore similar to the type II R subunit of mammalian origin, although it has a larger Mr (64,000 vs. 58,000) and is multiply phosphorylated. In vivo, both phosphorylated and unphosphorylated forms of the R subunit were found in cells grown in lactate or to stationary phase in 1.5% glucose, while cells grown in 5% glucose contained the unphosphorylated form.

Allosteric Regulation↗
PubMed1980

Activation of ppGpp-3'-pyrophosphohydrolase by a supernatant factor and ATP.

The breakdown of guanosine 5'-diphosphate, 3'-diphosphate (ppGpp) into GDP and PPi is catalyzed by a Mn2+-dependent 3'-pyrophosphohydrolase, the translation product of the spoT gene. The escherichia coli enzyme is normally found to be associated with the "crude" ribosome fraction. It is reported here that the guanosine 5'-diphosphate, 3'-diphosphate 3'-pyrophosphohydrolase activity in this fraction is activated by ATP in the presence of a relatively heat-stable, low molecular weight, supernatant factor (BS100). This stimulation is not due to a removal of reaction products such as by the phosphorylation of GDP to GTP or by the hydrolysis of PPi. Hydrolysis of ATP is probably required because neither adenosine 5'-(3-thio)triphosphate nor adenosine 5'-(beta, gamma-imido)triphosphate can substitute for ATP. Levallorphan, a morphine analog, which had been shown to inhibit in vivo ppGpp degradation, inhibits specifically the stimulation of ppGpp hydrolysis by ATP and the supernatant factor. The possible relationship of this system and the in vivo energy-dependent control of ppGpp degradation is discussed.

Adenosine Triphosphate↗
PubMed1977

In vitro degradation of guanosine 5'-diphosphate, 3'-diphosphate.

The degradation of guanosine 5'-diphosphate,3'-diphosphate (ppGpp) by the "crude" ribosomal fraction of Escherichia coli CP78 (rel+, spoT+) was demonstrated and characterized. When the 3'-pyrophosphoryl group of ppGpp was hydrolyzed, the primary degradation product was 5'-GDP. Phosphorylation of ppGpp to guanosine 5'-triphosphate,3'-diphosphate (pppGpp) prior to degradation was not necessary. The degradation process required Mn2+ and was inhibited by EDTA. Levallorphan, an inhibitor of in vivo ppGpp degradation, also inhibited ppGpp degradation by the crude ribosome. Thiostrepton and tetracycline did not have any inhibitory effect, indicating that the reaction is not a reversal of pyrophosphorylation catalyzed by the stringent factor/ribosome complex. Crude ribosome fractions from E. coli NF161 and NF162, both spoT-, contained little degrading activity, but similar fractions of E. coli CP79, a relA- and spoT+ strain, contained ppGpp degrading activity.

Cell-Free System↗