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)

Freeze-fracture combined with quantitative electron microscopy of the intact human erythrocyte (RBC) and ghost revealed significant differences in their intramembranous particle coefficients. External (E) fracture-faces of unfixed ghost membranes were found to contain 40% fewer particles than those of intact unfixed RBC. The particle distribution of the intact RBC membrane depended on the use of glutaraldehyde fixation and glycerol cryoprotection. Whereas glutaraldehyde- and glycerol-treated cells disclosed 70% fewer E-face particles than did intact unfixed cells, poly-L-lysine-treated, intact, unfixed RBC showed no such differences. Treatment with a combination of poly-L-lysine and glutaraldehyde, however, increased the amount of E-face particles while reducing those of the protoplasmic (P) face. The poly-L-lysine effect varied with its concentration and was unaffected by previous application of neuraminidase. Nor did the lectin phytohemagglutinin induce particle rearrangement in intact cells. Our data demonstrate that the processes of glutaraldehyde fixation and glycerol cryoprotection modify the RBC membrane by decreasing the number of E-face particles present. In addition, the combination of poly-L-lysine and glutaraldehyde alters the affinity of some particles for one half of the membrane, suggesting that in freeze-fractured RBC, chemical bonds formed at the extracellular surface of the membrane can influence particle partitioning.
Anat Rec 1977 Dec
PMID:Intramembranous particle distribution in human erythrocytes: effects of lysis, glutaraldehyde, and poly-L-lysine. 41 58

Two pregnant sows were fed on a basal diet consisting of equal amounts of ground barley and ground wheat with or without addition of L-lysine hydrochloride. Plasma amino acid and blood urea levels varied according to the time after feeding. Almost all the essential amino acids reached a maximum level after one hour and then declined at four hours after feeding. The results suggested that samples taken at between one and four hours after feeding were responsive to changes in dietary composition and could provide a measure to evaluate the amino acid pattern in relation to feeding. Both plasma amino acid and blood urea data suggested that lysine was the first limiting amino acid in the basal diet.
Vet Rec 1978 Jan 21
PMID:The variation in the concentration of plasma amino acids and blood urea in pregnant sows. 63 24

The product of the mouse Rec-1 locus is an integral membrane protein that determines susceptibility to infection by murine ecotropic retroviruses. Recently it has been determined that its role in normal cell metabolism is transport of the cationic amino acids, arginine, lysine, and ornithine across the plasma membrane. Southern blot analysis of genomic DNA from a panel of 48 mouse-human somatic cell hybrids assigned the human version of this gene, ATRC1, to chromosome 13. Chromosomal in situ hybridization localized the gene to 13q12-q14. A restriction fragment length polymorphism (RFLP) was detected with TaqI. There were two alleles with frequencies of 0.29 and 0.71. Pairwise linkage analysis established linkage between ATRC1 and ATP1AL1, D13S1, D13S6, D13S10, D13S11, D13S21, D13S22, D13S33, D13S36, and D13S37. Multilocus linkage analysis of five of the loci indicated that the most likely order of loci in this region was D13S11-ATP1AL1-ATRC1-D13S6-D13S33.
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PMID:The human cationic amino acid transporter (ATRC1): physical and genetic mapping to 13q12-q14. 134 89

Immunoreactivity to serotonin was observed in Merkel cells as well as the afferent type I nerves terminating upon them in touch domes excised from the belly skin of rats. Type I nerves were strongly immunoreactive and could be traced through the dermis of the domal papilla. Merkel cell immunoreactivity was sometimes seen in the entire cell, but was often localized in the Merkel cell cytoplasm adjacent to nerve terminals and may have been in the terminals themselves. Domes were fixed by immersion in 4% paraformaldehyde-lysine-sodium-m-periodate (PLP) fixative at 4 degrees C for 2.5-3 hours and cryoprotected in 30% sucrose overnight. Sections were processed with the avidin-biotin complex peroxidase (ABC), peroxidase-antiperoxidase (PAP), and indirect immunofluorescence techniques with rabbit antiserum generated against serotonin.
Anat Rec 1992 Jan
PMID:Serotonin-like immunoreactivity in Merkel cells and their afferent neurons in touch domes from the hairy skin of rats. 153 55

The extent of the odontoblast cell process has been the subject of controversy for many years. Using SEM we have examined the extent and morphology of the process on dentine surfaces of human teeth which were partially demineralized and collagenase digested. Third molars were extracted and split; the dentine surface was demineralized, digested by bacterial collagenase, fixed with glutaraldehyde, postfixed in osmium tetroxide, and prepared for SEM investigation. The SEM study revealed the presence of many processlike structures which extended from the odontoblast cell bodies up to the dentinoenamel junction (DEJ). These processes demonstrated lateral and terminal branching and some of them terminated in distended spheres. We have also applied an immunofluorescence technique at the light microscope level to these exposed dentinal surfaces to localize the intracellular microtubules. For this, a second series of third molars was processed in the same manner as for the SEM up to the fixation stage. Teeth were then fixed in periodate-lysine-paraformaldehyde, postfixed in -20 degrees C acetone, and then incubated with affinity-purified rabbit antitubulin antibodies, followed by fluorescein-conjugated goat antirabbit IgGs. Intratubular immunofluorescence labelling for tubulin was evident from the odontoblast cell bodies up to the DEJ. The presence of the tubulin-containing structures extending to the DEJ supports the hypothesis that the structures observed with the SEM are odontoblast processes and that the odontoblast processes do extend to the DEJ.
Anat Rec 1984 Nov
PMID:A combined scanning electron microscopy and immunofluorescence study demonstrating that the odontoblast process extends to the dentinoenamel junction in human teeth. 639 20

Cheviot sheep from the Neuropathogenesis Unit flock were examined for PrP in brain sections using immunocytochemistry in order to aid scrapie diagnosis. Brains were collected from sheep which had been naturally or experimentally infected with scrapie and fixed in periodate-lysine-paraformaldehyde or in formalin. Immunolabelling was achieved using a monoclonal antibody (FH11) raised to the N-terminus of recombinant PrP protein. Several pre-treatments were studied in an effort to enhance PrP immunolabelling such as trypsin, formic acid and hydrated autoclaving. Trypsin was successful in highlighting PrP staining in formalin-fixed tissue. PrP staining was regularly observed in the dorsal vagus nucleus of the medulla oblongata and in the thalamus. Differences in the distribution and intensity of PrP immunostaining were apparent between the scrapie sources ME7 and SSBP/I.
Vet Rec 1996 Nov 23
PMID:Immunolocalisation of the prion protein (PrP) in the brains of sheep with scrapie. 895 91

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

The aim of this work was to compare biochemical, two-dimensional biomechanical and calorimetric parameters of diabetic skin vs. control skin. Skin specimens taken from the palms and backs of the hands of aged persons with non-insulin-dependent diabetes mellitus (NIDDM) and of controls (CO) were compared (age range 68-85 years). Only skin specimens from individuals with diabetes mellitus (DM) showed an increased fluorescence specific for the formation of advanced glycation end-products (AGEs) and the presence of tissue AGEs, such as N(e)-(Carboxymethyl)lysine (CML). Differential scanning calorimetry (DSC) revealed an elevation of the heat flow per unit mass during collagen denaturation in diabetic skin samples. However, the temperatures of the heat flow maximum and the onset of the phase transformation were not uniformly altered. Young's moduli were found to be increased in diabetic skin and correlated with AGE-fluorescence and tissue AGEs. The ratio between the Young's moduli, which defines a measure for the degree of anisotropy, was higher for dorsal skins from hands. In dorsal skin specimens from diabetic subjects the degree of anisotropy was more pronounced than in healthy controls. In general, neither of the measured parameters showed any correlation with age. However, E(1) moduli were clearly associated with the duration of diabetes.
Anat Rec 2000 07 01
PMID:Differential scanning calorimetry, biochemical, and biomechanical analysis of human skin from individuals with diabetes mellitus. 1086 65

Research on the mechanism of action of coenzyme B12, adenosylcobalamin, as a graduate student introduced the author to the field of organic free radicals in enzymology. Twenty years later, related work on S-adenosylmethionine (SAM) as a "poor man's coenzyme B12" was initiated in a detailed analysis of the mechanism of action of lysine 2,3-aminomutase (LAM). The interconversion of L-lysine and L-beta-lysine is catalyzed by LAM, which requires SAM, pyridoxal-5'-phosphate (PLP), and a [4Fe-4S] cluster as coenzymes. The mechanism of this reaction has been delineated as a radical isomerization, in which radical formation is initiated by the [4Fe-4S]-dependent cleavage of the SAM into methionine and the 5'-deoxyadenosyl radical. The mechanism of this process is discussed, together with the role of this radical in hydrogen abstraction from lysine to initiate the substrate radical isomerization. The chemistry underlying the functions of SAM, PLP, and [4Fe-4S] in the action of LAM is novel in all respects, except for the formation of a lysine-PLP aldimine at the active site. Of the four free radicals in the mechanism, three have been characterized by EPR spectroscopy. In the suicide inactivation of adenosylcobalamin-dependent dioldehydrase (DDH) by glycolaldehyde, the formation of cob(II)alamin and 5'-deoxyadenosine is accompanied by the conversion of glycolaldehyde to cis-ethanesemidione radical at the active site. The cis-ethanesemidione radical has been characterized by EPR spectroscopy. Its exceptional stability at the active site is the basis for the inactivation of DDH by glycolaldehyde.
Chem Rec 2001
PMID:The role of radicals in enzymatic processes. 1189 68

Electrostatic interactions and other weak interactions between amino acid side chains on protein surfaces play important roles in molecular recognition, and the mechanism of their intermolecular interactions has gained much interest. We established that charged peptides are useful for investigating the molecular recognition character of proteins and their molecular interaction induced structural changes. Positively charged lysine peptides competitively inhibited electron transfer from reduced cytochrome f (cyt f or cytochrome c (cyt c) to oxidized plastocyanin (PC), due to neutralization of the negatively charged site of PC by formation of PC-lysine peptide complexes. Lysine peptides also inhibited electron transfer from cyt c to cytochrome c peroxidase. Likewise, negatively charged aspartic acid peptides interacted with the positively charged sites of cytfand cyt c, and competitively inhibited electron transfer from reduced cytfor cyt c to oxidized PC and from [Fe(CN)6]4- to oxidized cyt c. Changes in the geometry and a shift to a higher redox potential of the active site Cu of PC on oligolysine binding were detected by spectroscopic and electrochemical measurements, owing to the absence of absorption in the visible region for lysine peptides. Structural and redox potential changes were also observed for cyt f and cyt c by interaction with aspartic acid peptides.
Chem Rec 2001
PMID:Weak interactions and molecular recognition in systems involving electron transfer proteins. 1189 69


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