Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q9UIJ5 (Rec)
 58,342 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Semen samples were collected at weekly intervals for six weeks from eight sexually mature beagles previously shown to produce normal ejaculates. Seminal plasma and sperm fractions were separated by centrifugation and the sodium, potassium, alanine and aspartate aminotransferases, acid and alkaline phosphatase concentrations in the two fractions determined. Regression analysis of the mean weekly values obtained from physical and biochemical examination of the ejaculates showed that sodium ion concentration was highest in seminal plasma. The highest levels of aminotransferases were found in sperm fractions. Those enzymes may be indices of abnormal or damaged spermatozoa. Acid and alkaline phosphatase activity was 100 times greater in seminal plasma than in sperm fractions. Phosphatase concentrations are likely to be dependent on prostate activity. Measurement of acid phosphatase in canine semen therefore may be a useful index of prostate function. The motility of the semen samples was independent of the potassium concentration in seminal plasma. However, there was some evidence of a correlation between sperm motility and the enzyme and sodium content of seminal plasma.
Vet Rec 1979 May 26
PMID:Biochemical observations on beagle dog semen. 47 66

Dipeptidyl peptidase II (DPP II), E.C. 3.4.14.2, a serine class endopeptidase, is widely used as a lysosomal marker in cytochemical studies. To date most ultrastructural studies of ameloblasts use the presence of acid phosphatase activity to identify cellular organelles to be lysosomal. Using decalcified rat mandibles, with kidney tissue as a positive control, DPP II activity, was assessed with specific substrate Lysyl-alanine-4-methoxy-2-naphthylamide in ameloblasts at an ultrastructural level. Reaction product (RP) indicative of DPP II activity was observed only within lysosome-like organelles. These RP-labelled organelles were only localized in the supra- or para-nuclear regions of the ameloblasts, which corresponds with previous studies using acid phosphatase cytochemistry. However, in contrast with these studies, RP was not detected in the distal region of the ameloblasts, viz., in the Tomes' processes of the secretory ameloblasts or near the ruffled border in the maturation ameloblasts. The transitional ameloblasts were notable for the intensity of staining of their RP-labelled organelles. We propose that DPP II may have a role in programmed cell death which is thought to occur in this transition zone. Biochemical analysis of rat incisor enamel organ homogenates, indicated tissue fixation resulted in an 82% reduction in DPP II activity, although the specific activity of DPP II was not affected.
Anat Rec 1992 Aug
PMID:Cytochemical localization of dipeptidyl peptidase II activity in rat incisor tooth ameloblasts. 162 9

Enterobacterial plasmid genes mucAB, which possess error-prone repair activity, were cloned and sequenced independently of a sequence previously determined (K.L. Perry, S.J. Elledge, B.B. Mitchell, L. Marsh, and G.C. Walker, Proc. Natl. Acad. Sci. USA 82:4331-4335, 1985). The survival- and mutation-enhancing activities of mucAB ligated to the MLSr promoter of a Bacillus subtilis plasmid in the shuttle vector pTE22R were expressed in B. subtilis as well as in Escherichia coli after mutagenic treatment. mucAB fragments with 5' deletions of various lengths up to the base sequence encoding Ala-26-Gly-27, the putative RecA-mediated cleavage site of the MucA protein, showed mutation-enhancing activity for noninducible lexA3 E. coli when ligated to the MLSr promoter in frame. This activity was lost by extending the deletion downstream. The formations of MucA and MucB proteins in B. subtilis and E. coli were demonstrated by Western blot (immunoblot) analysis. MucA cleavage in Rec+ B. subtilis was observed only after treatment with an alkylating agent and was not observed in RecA- and RecE- strains, whereas in E. coli cleavage was observed in Rec+ cells after treatment with either mitomycin C or an alkylating agent but was not detected in RecA- cells. Common activity of B. subtilis Rec and E. coli RecA in the induction of mutants is suggested.
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PMID:Heterospecific expression of misrepair-enhancing activity of mucAB in Escherichia coli and Bacillus subtilis. 190 11

A single endotracheal instillation of porcine pancreatic elastase into hamster lungs induces morphological changes that can be detected as early as 15 min after the instillation of enzyme. Lung tissue from animals sacrificed at six time points between 15 min and 3 hr after enzyme instillation was examined for ultrastructural alterations. There were few of these alterations and they were highly focal, but they included damaged epithelial cells and partially digested elastic fibers that occurred both in the parenchyma and the pleura. A cytochemical technique employing N-t-Boc-L-alanine-p-nitrothiophenyl ester as a substrate for elastase-like enzymes was also used in an effort to locate pancreatic elastase shortly after instillation into the lungs. Reaction product was observed on the alveolar surface and in pinocytotic vesicles of alveolar type I cells, in connective tissue areas, in fibroblasts, and in pinocytotic vesicles of capillary endothelial cells. The location of reaction product coupled with ultrastructural alterations in the tissue suggests that pancreatic elastase instilled into the trachea may reach the interstitium in two ways: First, transport may take place across intact alveolar type I cells via pinocytotic vesicles, and second, a small amount of enzyme may gain access to the connective tissue after the disruption of epithelium in a few highly focal areas.
Anat Rec 1986 Jun
PMID:Ultrastructural changes in hamster lung 15 min to 3 hr after exposure to pancreatic elastase. 363 57

An emphysemalike condition can be induced in animal lungs by the instillation of a single dose of elastase. Autoradiography was used to determine the location of 3H-methylated porcine pancreatic elastase in hamster lungs at four time points. Six hours after instillation of radiolabeled enzyme the distribution of silver grains was very patchy, but in heavily labeled areas grains were concentrated over macrophages, connective tissue areas and over some fibroblasts. By 24 hr the labeling of connective tissue areas was no longer evident and almost all silver grains were associated with macrophages or with the edema fluid that filled many alveoli at this time. By 4 days only macrophages exhibited concentrations of silver grains. The labeling of macrophages was still evident at 7 days. Elastase inactivated by N-acetyl-(L-alanyl)3-L-alanine chloromethyl ketone showed a different distribution 6 hr after instillation. Silver grains were concentrated over macrophages and alveolar type II cells but showed no affinity for connective tissue areas or fibroblasts. By 24 hr almost all grains were located over heavily labeled macrophages.
Anat Rec 1983 May
PMID:Autoradiographic study of 3H-methylated elastase in hamster lungs. 655 48

As part of a study of the metabolic effects of long distance riding the results of biochemical analyses of blood samples taken from horses before, immediately after and one hour after an 80 km ride are reported. The results show that the horses were moderately dehydrated, they were working aerobically using fats as metabolic substrates and blood glucose was reduced. There was no evidence of post exercise ketosis and circulating alanine levels fell. Metabolic hormone levels are reported and are related to the availability of substrates for gluconeogenesis. There was evidence of reduced kidney and liver function which was showing little sign of recovery in the first hour after the ride.
Vet Rec
PMID:Long distance exercise in the horse: Golden Horseshoe Ride 1978. 743 3

A RecA/Rad51 homologue from Pyrococcus kodakaraensis KOD1 (Pk-REC) is the smallest protein among various RecA/Rad51 homologues. Nevertheless, Pk-Rec is a super multifunctional protein and shows a deoxyribonuclease activity. This deoxyribonuclease activity was inhibited by 3 mM or more ATP, suggesting that the catalytic centers of the ATPase and deoxyribonuclease activities are overlapped. To examine whether these two enzymatic activities share the same active site, a number of site-directed mutations were introduced into Pk-REC and the ATPase and deoxyribonuclease activities of the mutant proteins were determined. The mutant enzyme in which double mutations Lys-33 to Ala and Thr-34 to Ala were introduced, fully lost both of these activities, indicating that Lys-33 and/or Thr-34 are important for both ATPase and deoxyribonuclease activities. The mutation of Asp-112 to Ala slightly and almost equally reduced both ATPase and deoxyribonuclease activities. In addition, the mutation of Glu-54 to Gln did not seriously affect the ATPase, deoxyribonuclease, and UV tolerant activities. These results strongly suggest that the active sites of the ATPase and deoxyribonuclease activities of Pk-REC are common. It is noted that unlike Glu-96 in Escherichia coli RecA, which has been proposed to be a catalytic residue for the ATPase activity, the corresponding residual Glu-54 in Pk-REC is not involved in the catalytic function of the protein.
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PMID:A unique DNase activity shares the active site with ATPase activity of the RecA/Rad51 homologue (Pk-REC) from a hyperthermophilic archaeon. 1006 83

Methlenetetrahydrofolate (CH2-H4folate) is required for the conversion of homocysteine to methionine and of dUMP to dTMP in support of DNA synthesis, and also serves as a major source of one carbon unit for purine biosynthesis. This review presents biochemical studies of a human polymorphism in methylenetetrahydrofolate reductase, which catalyzes the reaction shown below. The mutation decreases the flux of CH2-H4folate into CH3-H4folate, and is associated with both beneficial and deleterious effects that can be traced to the molecular effect of the substitution of alanine 222 by valine.
Chem Rec 2002
PMID:Methylenetetrahydrofolate reductase: a common human polymorphism and its biochemical implications. 1193 57

Based on the fact that RNA has not only a genetic function but also a catalytic function, the RNA world theory on the origin of life was first proposed about 20 years ago. The theory assumes that RNA was amplified by self-replication to increase RNA diversity on the primitive earth. Since then, the theory has been widely accepted as the most likely explanation for the emergence of life. In contrast, we reached another hypothesis, the [GADV]-protein world hypothesis, which is based on pseudo-replication of [GADV]-proteins. We reached this hypothesis during studies on the origins of genes and the genetic code, where [G], [A], [D], and [V] refer to Gly, Ala, Asp, and Val, respectively. In this review, possible steps to the emergence of life are discussed from the standpoint of the [GADV]-protein world hypothesis, comparing it in parallel with the RNA world theory. It is also shown that [GADV]-peptides, which were produced by repeated dry-heating cycles and by solid phase peptide synthesis, have catalytic activities, hydrolyzing peptide bonds in a natural protein, bovine serum albumin. These experimental results support the [GADV]-protein world hypothesis for the origin of life.
Chem Rec 2005
PMID:Possible steps to the emergence of life: the [GADV]-protein world hypothesis. 1582 60

The laminin alpha1 chain is a subunit of laminin-1, a heterotrimeric basement membrane protein. The LG4-5 module at the C terminus of laminin alpha1 contains major binding sites for heparin, sulfatide, and alpha-dystroglycan and plays a critical role in early embryonic development. We previously identified active synthetic peptides AG73 and EF-1 from the sequence of laminin alpha1 LG4 for binding to syndecan and integrin alpha2beta1, respectively. However, their activity and functional relationship within the laminin-1 and LG4 as well as the functional relation between these sites and alpha-dystroglycan binding sites in LG4 are not clear. To address these questions, we created mutant recombinant LG4 proteins containing alanine substitutions within the AG73 (M1), EF-1 (M2, M3), and alpha-dystroglycan binding sites (M4, M5) and analyzed their activities. We found that recombinant proteins rec-M1 and rec-M5, containing mutations within M1 and M5, respectively, did not bind heparin or lymphoid cell lines expressing syndecans. These results suggest that LG4 binds to heparin and syndecans through M1 and M5. Rec-M1 and rec-M5 reduced fibroblast attachment, whereas mutant rec-M2 and rec-M3 retained cell attachment activity but did not promote cell spreading. Fibroblast attachment to rec-LG4 was inhibited by heparin but not by integrin antibodies. Spreading of fibroblasts on rec-LG4 was inhibited by anti-integrin alpha2 and beta1 but not by anti-integrin alpha1 and alpha6. These results suggest that the M1 and M5 sites are necessary for cell attachment on LG4 through syndecans and that the EF-1 site is for cell spreading activity through integrin alpha2beta1. In contrast, laminin-1-mediated fibroblast attachment and spreading were not inhibited by heparin or anti-integrin alpha2. Our findings indicate that LG4 has a unique function distinct from laminin-1 and suggest that laminin alpha1 LG4-5 may also be produced by a proteolytic cleavage in certain tissues where it exerts its activity.
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PMID:Laminin alpha1 chain LG4 module promotes cell attachment through syndecans and cell spreading through integrin alpha2beta1. 1694 29


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