Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The role of sperm specific lactate dehydrogenase-C4 (LDH-C4) in allo-immune responses using mixed lymphocyte cultures (MLC) and cytotoxic T cell (CTL) generation in vitro and local graft versus host (LGVH) reaction and allograft enhancement in vivo has been ascertained. LDH was purified from testes (LDH-C4) and kidney (LDH-B4) of C57Bl/Ks mice. MLC and CTL were performed using C57Bl/Ks-anti A/J lymphocytes in presence of 10(-3)-1 micrograms LDH-B4 or LDH-C4 per culture. The MLC and CTL responses showed biphasic action depending on the dose of LDH-C4. Early MLC culture gave significantly low stimulation index at 10(-2)-10(-1) micrograms LDH-C4 as compared to non-treated control cultures. However, the MLC response in presence of LDH-C4 was not different from the LDH-B4 treated one which showed a similar biphasic trend. On the other hand, 51Cr release from YAC-222 target cells was practically abolished by LDH-C4 at 10(-3)-1(-1) micrograms, and this was strikingly different from LDH-B4 or non-treated cultures. LGVH reactivity as performed by using C57Bl/Ks lymphocytes along with LDH-C4 in (C57Bl/Ks x A/J) F1 hybrids indicated a suppression of stimulation index in primary and secondary (i.e. preimmunized in presence of LDH-C4 or LDH-B4) LGVH. Allograft enhancement of Sa I (A/J) in C57Bl/Ks mice in presence of LDH-C4, was delayed slightly but significantly during primary or secondary transplantation reaction.(ABSTRACT TRUNCATED AT 250 WORDS)
Mol Cell Biochem 1993 Aug 25
PMID:Modulation of allo-immune responses in vivo and in vitro by sperm specific lactate dehydrogenase-C4. 828 69

The D-lactate dehydrogenase (D-LDH) from Lactobacillus bulgaricus has been purified and co-crystallized with its cofactor NAD+. Crystals suitable for X-ray diffraction experiments have been obtained from an ammonium sulfate solution by the hanging-drop method. The crystals belong to the orthorhombic space group C222 (or C222(1)) with cell dimensions a = 76.5 A, b = 93.3 A, c = 118.4 A and one monomer of 37,000 daltons per asymmetric unit. They diffract beyond 3.0 A resolution. Sequence comparison suggests that D-LDHs have no evolutionary relationship to L-LDHs and belong instead to the family of the D-2-hydroxyacid dehydrogenases. The X-ray crystallographic structure of the D-LDH from Lactobacillus bulgaricus will be a decisive test of this hypothesis.
J Mol Biol 1994 Jan 07
PMID:Crystallization of D-lactate dehydrogenase from Lactobacillus bulgaricus. 828 59

The testis specific form of lactate dehydrogenase (LDH-C4) is encoded by a single locus, Ldh-c, and is tightly regulated in a tissue specific manner. Here we show differences in expression of Ldh-c between rat and mouse, and describe the levels at which regulation of this gene differs in the two species. Our results demonstrate that the Ldh-c message level is nearly nine fold greater in mouse testis and remains high post-meiotically. In contrast, rat Ldh-c mRNA is highest in primary spermatocytes and reduced in spermatids. The results of nuclear run-on assays indicate that the transcription rate of Ldh-c is only moderately higher in mouse than rat, and cannot account for a significant portion of the observed differences. Similar decay rates for both rat and mouse Ldh-c mRNA in actinomycin-D clearance assays indicate comparable cytoplasmic stabilities for the two messages. From these results we infer that nuclear prostranscriptional events contribute to the differences in Ldh-c message levels.
Mol Reprod Dev 1993 May
PMID:Differences in regulation of testis specifc lactate dehydrogenase in rat and mouse occur at multiple levels. 850 74

A Plasmodium falciparum gene is described which encodes lactate dehydrogenase activity (P. falciparum LDH). The P. falciparum LDH gene contains no introns and is present in a single copy on chromosome 13. P. falciparum LDH was expressed in all asexual blood stages as a 1.6-kb mRNA. The predicted 316 amino acid protein coding region of P. falciparum LDH was inserted into the prokaryotic expression vector pKK223-3 and a 33-kDa protein having LDH activity was synthesized in Escherichia coli. P. falciparum LDH primary structure displays high amino acid similarity (50-57%) to vertebrate and bacterial LDH, but lacks the amino terminal extension observed in all vertebrate LDH. The majority of amino acid residues implicated in substrate and coenzyme binding and catalysis of other LDH are well conserved in P. falciparum LDH. However, several notable differences in amino acid composition were observed. P. falciparum LDH contained several distinctive single amino acid insertions and deletions compared to other LDH enzymes, and most remarkably, it contained a novel insertion of 5 amino acids within the conserved mobile loop region near arginine residue 109, a residue which is known to make contact with pyruvate in the ternary complex of other LDH. These results suggest that novel features of P. falciparum LDH primary structure may be correlated with previously characterized and distinctive kinetic, biochemical, immunochemical, and electrophoretic properties of P. falciparum LDH.
Mol Biochem Parasitol 1993 May
PMID:Expression of Plasmodium falciparum lactate dehydrogenase in Escherichia coli. 851 77

Sprague-Dawley rat hearts were perfused under constant flow conditions, and a balloon was inserted into the left ventricle to measure heart rate (HR) and left ventricular pressures. Left ventricular generated pressure (LVGP) was calculated as peak systolic minus end diastolic pressure. Three substrate groups, pyruvate (5 mM), glucose (15 mM) and octanoate (0.5 mM), were employed. Oxidative stress was induced by perfusion with tertiary-butyl hydroperoxide (tBHP, 0.35 mM, 12 min) followed by 25 min of perfusion with control buffer. Hearts perfused with pyruvate showed no significant decrease in contractile function following tBHP treatment (HR x LVGP = 17666 +/- 585 mmHg/min, initial: 16414 +/- 2083 post-tBHP treatment). Glucose-perfused hearts had an intermediate decrease in function (19174 +/- 828 mmHg/min, initial; 4379 +/- 2083 post-tBHP), while octanoate-perfused hearts recovered no contractile function. Peak release of LDH was lowest in hearts perfused with pyruvate (115 +/- 17 mU/g wet wt/min), intermediate in glucose-perfused hearts (1575 +/- 380) and highest in octanoate-perfused hearts (3074 +/- 499). Thiobarbituric acid reactive substances (TBARS) were unchanged in hearts perfused with pyruvate (16.2 +/- 5 nmoles/g wet wt), but increased significantly in glucose-perfused hearts (36.1 +/- 1) and in octanoate-perfused hearts (45.5 +/- 9). Total glutathione levels were unchanged in hearts perfused with pyruvate (753 +/- 68 nmoles/g wet wt), but significantly decreased in glucose-perfused hearts (594 +/- 68) and in octanoate-perfused hearts (445 +/- 38) following tBHP-treatment. Pyruvate significantly reduced oxidative injury. In contrast, glucose provided a small reduction in injury while octanoate-perfused hearts had the most severe injury.(ABSTRACT TRUNCATED AT 250 WORDS)
J Mol Cell Cardiol 1995 Sep
PMID:Antioxidant effects of pyruvate in isolated rat hearts. 852 65

The ability of glycolytic enzymes, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), aldolase, pyruvate kinase (PK), and lactate dehydrogenase muscle-type (LDH(M)), to generate interactive microtubule networks was investigated. Bundles have previously been defined as the parallel alignment of several microtubules and are one form of microtubule networks. Utilizing transmission electron microscopy, interactive networks of microtubules as well as bundles were readily observed in the presence of GAPDH, aldolase, or PK. These networks appear morphologically as cross-linked microtubules, oriented in many different ways. Light scattering indicated that the muscle forms of GAPDH, aldolase, PK and LDH(m) caused formation of the microtubule networks. Triose phosphate isomerase (TPI) and lactate dehydrogenase heart-type (LDH(H)), glycolytic enzymes which do not interact with tubulin or microtubules, did not produce bundles, or interactive networks. Sedimentation experiments confirmed that the enzymes that cross-link also co-pellet with the microtubules. Such cross-linking of microtubules indicate that the enzymes are multivalent with the capability of simultaneous binding to more than one microtubule.
Comp Biochem Physiol B Biochem Mol Biol 1995 Nov
PMID:Glycolytic enzymes and assembly of microtubule networks. 852 27

The cDNA sequence of the lactate dehydrogenase-A (LDH-A) of the spiny dogfish was determined. The deduced amino acid sequence differed from a previously determined protein sequence by 5%. Separate maximum parsimony analyses of the two sequences along with LDHs of other vertebrates resulted in shorter trees with the sequence presented here, as well as fewer equally parsimonious trees. The new sequence also indicates a greater conservation of length among vertebrate LDHs than was previously suspected. Analyses of the phylogeny of vertebrate LDHs resulted in a monophyletic grouping of LDH-As, from within which mammalian LDH-C is derived. The phylogeny of LDH-As did not exactly match the phylogeny of the organisms, raising the possibility of multiple origins and losses of a muscle-predominant gene. LDH-Bs appear to have shared a single origin.
Mol Mar Biol Biotechnol 1995 Dec
PMID:The cDNA sequence of the lactate dehydrogenase-A of the spiny dogfish (Squalus acanthias): corrections to the amino acid sequence and an analysis of the phylogeny of vertebrate lactate dehydrogenases. 854 80

This study was aimed to determine whether singlet oxygen (1O2) attenuates 5'-nucleotidase activity in the ischemic myocardium. Isolated rat hearts were exposed to either exogenous 1O2 produced by irradiating rose bengal or 40-min ischemia and reperfusion. Ecto-5'-nucleotidase activity was inhibited by exogenous 1O2 (3.74 +/- 0.38 mumol/min/g dry weight), when compared with normal control (7.52 +/- 0.41 mumol/min/g dry weight; P < 0.05). The enzymatic activity was significantly preserved by histidine (25 mM)--a 1O2 scavenger (7.04 +/- 0.61 mumol/min/g dry weight; P < 0.05 v rose bengal group). After ischemia, the activity of ecto-5'-nucleotidase was greatly reduced (2.51 +/- 0.25 mumol/min/g dry weight), when compared with normal control. Histidine significantly enhanced ecto-5'-nucleotidase activity (6.55 +/- 0.52 mumol/min/g dry weight, P < 0.05 v ischemic control). Adenosine release was consistent with ecto-5'-nucleotidase activity. The time course studies of effects of 1O2 on coronary flow, cardiac function, and LDH release revealed that the damage by 1O2 to ecto-5'-nucleotidase activity and adenosine release primarily accounted for impaired coronary flow, cardiac dysfunction, and impaired cardiac metabolism. Lipid peroxidation induced by exogenous 1O2 or ischemia was in parallel with ecto-5'-nucleotidase deactivation by 1O2. It is concluded that 1O2 causes inactivation of ecto-5'-nucleotidase and attenuation of adenosine release which could possibly be one of the important mechanisms of oxygen radical-mediated myocardial injury.
J Mol Cell Cardiol 1995 Nov
PMID:Interaction of singlet oxygen with 5'-nucleotidase in rat hearts. 859 96

Regulatory effects on polyclonal activation of primed splenocytes have been studied following immunization through the intrarectal route with allogenic sperm specific lactate dehydrogenase (LDH-C4) and somatic LDH from kidney. Results indicate that LDH primed cell proliferation by mitogens is dependent on the nature of the isozyme and sex of donor cells. Compared to somatic LDH, LDH-C4 was immunosuppressive for T cell proliferation in vitro and the effect was more significant with female splenocytes as compared to male spleen cells. However, the suppressive effect of LDH-C4, on B cell function was identical in both males and females. In contrast to the somatic LDH which did not produce alloantibody in significant amount, LDH-C4 was highly immunogenic in production of humoral antibody in female mice. Alloantibody formation in dams was substantiated with a similar degree of immune regulation of B cell functions as shown by lipopolysaccharide stimulation. The role of LDH-C4 in protection of allogenic sperm in the female genital tract has been suggested. However, it is concluded that recipients of sperm constituents through the intrarectal route are at greater risk for immune suppression and bacterial/viral infection.
Mol Cell Biochem 1996 May 24
PMID:Sex dependent immune responses by allogenic LDH isozymes. 881 72

To examine the role of fibroblast growth factors on the proliferation present during angiogenic processes, we analyzed the effects of in vitro cell culture with acidic (FGF-1) and basic (FGF-2) fibroblast growth factors on murine peritoneal exudate cell survival. FGF-1 or FGF-2 in the presence of heparin resulted in a significantly greater cell viability for exudate cells at 24 hours of culture relative to heparin alone or medium controls. Cultures supplemented with FGF-1 or FGF-2 plus heparin showed a slight increase in tritiated[3H] thymidine uptake over heparin or medium alone. No specific change in [3H] uridine incorporation or LDH release was detectable between FGF-1, FGF-2, heparin or medium alone cultures. Our results suggest that FGF-1 and FGF-2 may enhance survival both in vitro and in vivo of a subset of peritoneal exudate cells. This attribute may play a role during inflammatory or tumor-like states.
Res Commun Mol Pathol Pharmacol 1996 Jun
PMID:Acidic and basic fibroblast growth factors prolong the in-vitro survival of murine peritoneal macrophages. 882 35


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