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J Tang

Publications and source records attributed to J Tang.

At least 541 records · Page 30Linked to original sources
PubMed1987

Evolution in the structure and function of aspartic proteases.

Aspartic proteases (EC3.4.23) are a group of proteolytic enzymes of the pepsin family that share the same catalytic apparatus and usually function in acid solutions. This latter aspect limits the function of aspartic proteases to some specific locations in different organisms; thus the occurrence of aspartic proteases is less abundant than other groups of proteases, such as serine proteases. The best known sources of aspartic proteases are stomach (for pepsin, gastricsin, and chymosin), lysosomes (for cathepsins D and E), kidney (for renin), yeast granules, and fungi (for secreted proteases such as rhizopuspepsin, penicillopepsin, and endothiapepsin). These aspartic proteases have been extensively studied for their structure and function relationships and have been the topics of several reviews or monographs (Tang: Acid Proteases, Structure, Function and Biology. New York: Plenum Press, 1977; Tang: J Mol Cell Biochem 26:93-109, 1979; Kostka: Aspartic Proteinases and Their Inhibitors. Berlin: Walter de Gruyter, 1985). All mammalian aspartic proteases are synthesized as zymogens and are subsequently activated to active proteases. Although a zymogen for a fungal aspartic protease has not been found, the cDNA structure of rhizopuspepsin suggests the presence of a "pro" enzyme (Wong et al: Fed Proc 44:2725, 1985). It is probable that other fungal aspartic proteases are also synthesized as zymogens. It is the aim of this article to summarize the major models of structure-function relationships of aspartic proteases and their zymogens with emphasis on more recent findings. Attempts will also be made to relate these models to other aspartic proteases.

Amino Acid Sequence↗
PubMed1987

7C3, a marker for the differentiation of human macrophage cell lines.

The induction of differentiation in the human monoblastlike cell line U937 by 1,25 dihydroxyvitamin D3, interferon gamma, or phorbol esters is associated with the expression of a novel surface antigen, 7C3. The expression of 7C3 is maximal after 24 hr and is dependent upon de novo protein synthesis. The appearance of 7C3 during U937 differentiation is inhibited by dexamethasone while the increased expression of the macrophage marker OKM1 is not affected. 7C3 antigen is also expressed on HL60 cells when induced along the macrophage pathway and is expressed weakly on peripheral blood monocytes but not on lymphoid cells or granulocytes. 7C3 expression is sensitive to trypsin and low concentrations of the nonionic detergents NP-40 and Triton X-100. The induction of 7C3 expression may serve as a useful model to understand the regulatory events involved during the early phases of monocyte-macrophage differentiation.

Animals↗
PubMed1987

Lack of spontaneous activity of cutaneous spinal dorsal horn neurons in awake, drug-free, spinally transected cats.

Extracellular single-unit activity was recorded from neurons with cutaneous input in the dorsal horn of the spinal cord (L4-L6) of awake, drug-free cats before (for several weeks) and after (day 1 through day 7) cord transection (T12). The spontaneous activity of the neurons was minimal or nonexistent in both recording conditions. The lack of spontaneous activity following spinal cord transection contrasts sharply with activity recorded in acute spinal-cord transected preparations in which high rates of spontaneous activity have been reported. This discrepancy may reflect an important difference between the chronic, awake, drug-free and acute preparations.

Action Potentials↗
PubMed1987

Plasmid profiles of multi-resistant Staphylococcus aureus at a children's hospital.

Twenty-six strains of multi-resistant Staphylococcus aureus (MRSA) recovered from November 1985 to February 1986 were screened for their plasmid profiles. Among them, 11 strains were recovered from 8 patients with definite nosocomial infections. The results showed that one MRSA strain carrying 5 plasmids with molecular weight ranging from 1.75 X 10(6) to 5 X 10(6) daltons was epidemic in our hospital while 3 other distinct strains caused cross infections in both the burn ward and the medical wards. The epidemic strain and two other hospital-acquired strains were found in identical form in the community, suggesting that the pattern of nosocomial MRSA can be affected by strains outside hospital. The plasmid profile analysis was employed to differentiate the epidemic isolates from the coisolates and to study the relation between clinical isolates. The method is apparently superior to antibiogram.

Bacteriological Techniques↗
PubMed1986

Antiopioid activity of the cardioexcitatory peptide in central modulation of cardiovascular functions.

Intracerebroventricular (i.c.v.) injection of [D-Ala2,Leu5]enkephalin produced depressor and bradycardiac responses which were prevented by naloxone or FMRF-NH2 pretreatment. Intrathecal injection of FMRF-NH2 to rats in hemorrhagic shock resulted in a slight but significant increase in blood pressure, and prevented the further decrease in heart rate which was observed in the control group. It is concluded that FMRF-NH2 may act as an antiopioid substance in central modulation of cardiovascular functions.

Animals↗
PubMed1986

Structure of Rhodopseudomonas sphaeroides R-26 reaction center.

The molecular replacement method has been successfully used to provide a structure for the photosynthetic reaction center of Rhodopseudomonas sphaeroides at 3.7 A resolution. Atomic coordinates derived from the R. viridis reaction center were used in the search structure. The crystallographic R-factor is 0.39 for reflections between 8 and 3.7 A. Validity of the resulting model is further suggested by the visualization of amino acid side chains not included in the R. viridis search structure, and by the arrangements of the reaction centers in the unit cell. In the initial calculations quinones or pigments were not included; nevertheless, in the resulting electron density map, electron density for both quinones QA and QB appears along with the bacteriochlorophylls and bacteriopheophytins. Kinetic analysis of the charge recombination shows that the secondary quinone is fully functional in the R. sphaeroides crystal.

Bacterial Proteins↗
PubMed1986

Porcine spleen cathepsin B is an exopeptidase.

The major cathepsin B isozyme CB-I purified from porcine spleens was studied for its specificity against various peptide and denatured protein substrates. The enzyme degraded all the peptide substrates by an exopeptidase activity. The substrates were degraded mainly by a dipeptidyl carboxypeptidase activity of the enzyme except for angiotensin I, from which a COOH-terminal leucine residue was released. The enzyme failed to hydrolyze peptides having a proline or cysteic acid in the COOH-terminal, penultimate, and antepenultimate positions. Reduced and carboxymethylated soybean trypsin inhibitor was degraded by the same dipeptidyl carboxypeptidase action of cathepsin B. No significant endopeptidase activity was observed. These results do not support the general assumption that cathepsin B has both endo- and exopeptidase activities, neither do these observations support the postulation that cathepsin B might be involved in the in vivo proteolytic processing of protein precursors. We propose that the biological role of this enzyme is mainly the degradation of tissue proteins in lysosomes.

Animals↗
PubMed1986

Comparative studies of two cathepsin B isozymes from porcine spleen. Isolation, polypeptide chain arrangements, and enzyme specificity.

Our previous studies on carbohydrate structures of purified porcine spleen cathepsin B indicated that there are two cathepsin B isozymes, each containing a different carbohydrate (Takahashi, T., Schmidt, P.G., and Tang, J. (1984) J. Biol. Chem. 259, 6059-6062). We have now isolated these two enzymes and carried out a comparative study on their structures and enzymic properties. The major isozyme (CB-I) is a two-chain enzyme (Mr = 28,000) with a light chain (Mr = 5,000) and a heavy chain (Mr = 23,000), whereas the minor enzyme (CB-II) is a single chain enzyme (Mr = 27,000). The NH2-terminal amino acid residues of CB-I were leucine and valine for the light and heavy chain, respectively. However, the NH2-terminal residue of CB-II was not available for automated Edman degradation. In addition, peptide mapping experiments indicated a difference in the primary structure of these two proteins. Despite such structural differences, they are similar in many enzymic properties. CB-I was more catalytically efficient than CB-II toward synthetic substrates, except for the substrate benzoyl-L-arginine beta-naphthylamide for which the relative catalytic efficiency is reversed. Both isozymes degraded glucagon by a dipeptidyl carboxypeptidase activity. Under the same conditions, CB-I was 4-5 times more efficient than CB-II. The results indicate that the cathepsin B isozymes are two separate gene products, but they are similar in enzymic properties.

Amino Acid Sequence↗
PubMed1986

Clonidine stimulated the release of dynorphin in the spinal cord of the rat: a possible mechanism for its depressor effects.

The decrease in blood pressure, heart rate and sympathetic nervous discharges (SND) induced by intrathecal injection of clonidine (1 microgram) in the rat was prevented by pretreatment with intrathecal injection of an antiserum against dynorphin. Clonidine (10(-4) M) added to the artificial cerebrospinal fluid perfusing the spinal subarachnoid space of the rat increased the amount of immunoreactive dynorphin in the perfusate. Intrathecal injection of dynorphin (30 micrograms) caused hypotension, bradycardia and a reduction in SND. These results suggest that the release of dynorphin in the spinal cord may constitute one of the mechanisms for the depressor effects of clonidine.

Animals↗
PubMed1986

Atriopeptin and spontaneous hypertension in rats.

The involvement of atriopeptin in hypertension was investigated in spontaneously hypertensive rats (SHR). It was found that intravenous injection of atriopeptin III (20-80 nmol/kg) markedly decreased the mean arterial pressure in anesthetized SHR in a dose dependent manner. The heart rate was not significantly affected. The contents of atriopeptin immunoreactive material in the rat atrium and plasma were measured with radioimmunoassay. Both the atrium and plasma contents of atriopeptin immunoreactive material were found to be significantly higher in SHR than in the normotensive control Wistar Kyoto (WKY), indicating an increase in the biosynthesis and release of atriopeptin in SHR. Whether this change was a compensatory response induced by hypertension remains to be investigated.

Animals↗
PubMed1986

Analgesic activity and release of [MET5]enkephalin-Arg6-Gly7-Leu8 from rat spinal cord in vivo.

Rat spinal cord contains the opioid peptide including [Met5]enkephalin-Arg6-Gly7-Leu8 (YGGFMRGL) and a higher molecular weight (HMW) immunoreactive peptide which is an N-terminal extended molecular form of YGGFMRGL. Since a high proportion of tissue immunoreactivity resides in the HMW component we have determined whether this form is released during perfusion of the spinal cord subarachnoid space in vivo while (1) electrically stimulating the sciatic nerves bilaterally or (2) superfusing with substance P. We have found that YGGFMRGL and the HMW immunoreactivity are released by both types of stimuli. The HMW material appeared to be the more stable of the two species of immunoreactivity; its presence in the superfusate was more consistently observed than that of YGGFMRGL itself. Injection of YGGFMRGL into the spinal subarachnoid space in chronically catheterized rats produced a suppression of the tail-flick response. This effect of YGGFMRGL was reversed by naloxone suggesting an action mediated by spinal opiate receptors. These data suggest that YGGFMRGL plays an integral role in the neurotransmission process between spinal neurons storing enkephalin and other neurons. The possibility that enkephalin-mediated neurotransmission includes multiple chemical signals can be entertained.

Analgesics↗
PubMed1986

Active streptokinase from the cloned gene in Streptococcus sanguis is without the carboxyl-terminal 32 residues.

The streptokinase expressed by the cloned gene in Streptococcus sanguis has a molecular weight of about 44 000 [Malke, H., Gerlach, D., Kohler, W., & Ferretti, J.J. (1984) MGG, Mol. Gen. Genet. 196, 360-365] while the molecular weight of the native streptokinase is 47 000. The structural and activity differences of the cloned streptokinase (cSK) as expressed by S. sanguis and the native streptokinase (nSK) were investigated. From a partially purified cSK, two active fractions were obtained by reversed-phase HPLC. The minor fraction cSKL was nearly as active as SK in plasminogen activation. The major fraction cSKs had only about one-fourth of the specific activity. The structures of cSKL and cSKs were studied and compared to the known amino acid sequence of SK [Jackson, K. W., & Tang, J. (1982) Biochemistry 21, 6620-6625]. From the NH2- and COOH-terminal sequences and amino acid composition of the cyanogen bromide (CNBr) fragments, it could be deduced that cSKL and cSKs are without 31 and 32 residues, respectively, from the COOH-terminal end of SK. Since the cloned gene contained the full SK structure, the missing structures must have been due to posttranslational proteolysis. An SK fragment similar in size to cSK was observed from a chymotryptic digest of SK.

Amino Acids↗
PubMed1986

Establishment and characterization of murine macrophage hybrids.

Proteose peptone-induced peritoneal macrophages from CBA/J (H-2k) mice have been fused to a hypoxanthine phosphoribosyltransferase-negative variant of the P388D1 (H-2d) murine macrophage cell line. Six hybrid clones were isolated following HAT selection and further characterized. Five of the six clones express class I antigens of both parental haplotypes by microelisa and by flow cytometric analysis. Class II antigen expression of both haplotypes was apparent following a 72-hr incubation of the hybrids with concanavalin A-stimulated rat spleen cell supernatant. However, I-Ad was expressed in all hybrids to a greater extent than I-Ak. Three clones with the highest level of I-Ak expression, E5, C2, and C4, were capable of antigen presentation to the I-Ak-restricted T-cell line, D10.G4.1. LPS induction of the hybrids resulted in a 2- to 15-fold increase in the amount of IL-1 produced relative to the P388D1 parent. Finally, in distinction to P388D1, all hybrids demonstrated increased Fc-mediated erythrophagocytosis of chromium-labeled antibody-coated erythrocytes. These murine macrophage hybrids appear stable and should serve as useful models in understanding the regulation of macrophage function.

Animals↗
PubMed1986

Murine thymocytes mediate a natural killer-like activity against herpes virus-infected target cells but not YAC-1 target cells.

In this report, we demonstrated a natural killer (NK)-like activity against HSV-1 infected cells mediated by CD-1 mouse thymocytes. This cytolytic activity is specific for HSV-1-infected MCN cells, since both uninfected MCN and YAC-1 target cells are not susceptible to thymocyte lysis. Antibody plus complement depletion experiments indicate that a portion of the activity is associated with the Lyt 2-/L3T4- thymocyte subpopulation. This NK-like activity cannot be enhanced by addition of interleukin 2 in vitro.

Animals↗