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Biomedical subjects

M Cross

Publications and source records attributed to M Cross.

At least 181 records · Page 10Linked to original sources
PubMed1993

Code comfort.

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Abstracting and Indexing↗
PubMed1993

The trans-spliceosomal U2 snRNP protein 40K of Trypanosoma brucei: cloning and analysis of functional domains reveals homology to a mammalian snRNP protein.

Through immunoscreening we have isolated a cDNA encoding the trans-spliceosomal U2 snRNP-specific 40 kDa protein of Trypanosoma brucei. The protein has a predicted molecular weight of 36.6 kDa and shows 31% amino acid identity with the human U2 snRNP A' protein of 28.4 kDa. The homology between the trypanosome and human protein sequences is restricted to the N-terminal half where they share a series of six leucine repeat motifs. Sequence alignment revealed three 40K-specific regions: a C-terminal extension and two insertions, one of which makes up a seventh leucine repeat. Bacterially expressed 40K protein efficiently bound RNA by itself in a nonspecific manner; this general RNA binding activity was located to a region in the C-terminal half overlapping with the leucine repeat domain. U2 RNA-specific interaction required the presence of other trypanosome proteins and depended upon the loop IV sequence of U2 RNA. Deletion analysis of the 40K protein demonstrated the leucine repeats, including the 40K-specific, seventh repeat, to be essential for specific U2 RNP assembly, most likely through their role as an interface for protein-protein interaction.

Amino Acid Sequence↗
PubMed1993

23Na-NMR detects hypoxic injury in intact kidney: increases in sodium inhibited by DMSO and DMTU.

Hypoxic injury in the isolated perfused rat kidney (IPRK) was monitored using 23Na-NMR in the presence or absence of 1.5 and 15 mM dimethylthiourea (DMTU) or 15 mM dimethylsulphoxide (DMSO) before and after inducing hypoxia. Hypoxia induced a prompt exponential increase in total renal 23Na+, renal vascular resistance, and sodium excretion and decreased inulin clearance and adenine nucleotides and reduced glutathione concentrations. Lipid peroxide metabolites were unaltered. The increase in 23Na+ was significantly reduced (P < 0.001) by both DMTU and DMSO although hypoxic perturbations of function and biochemical parameters were not. Posthypoxic increases in renal 23Na+ include approximately 10% from the intratubular compartment, but principally reflect the intracellular and interstitial compartments. The results demonstrate that 23Na-NMR is a sensitive indicator of hypoxic renal injury in intact kidney and suggest that DMTU and DMSO protect against hypoxic injury by a mechanism independent of free radical-binding.

Animals↗
PubMed1992

Against all odds.

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Computer Communication Networks↗
PubMed1992

The mouse M-lysozyme gene domain: identification of myeloid and differentiation specific DNasel hypersensitive sites and of a 3'-cis acting regulatory element.

The mouse M-lysozyme gene is exclusively expressed in myeloid cells of the blood system being progressively turned on upon cell differentiation. In this study the mechanism controlling this tissue- and differentiation stage-specific gene expression was analyzed at the level of chromatin structure. A complex pattern consisting of constitutive and differentiation dependent DNasel hypersensitive sites (HSs) was found in a set of various myeloid cell lines, representing different stages of maturity. The chromatin of a lymphoid cell line, which does not express the lysozyme gene, is completely insensitive to DNasel digestion. Chromatin analysis of two multipotent hematopoietic stem cell lines which can be differentiated in vitro to mature myeloid cells confirmed that these identified DNasel HSs are specific for distinct differentiation stages, rather than being a characteristic feature of the cell lines. Additionally, the stem cell studies revealed that the hypersensitivity of the chromatin domain is already established at the multipotent stage. DNA fragments spanning a cell type- and differentiation stage-specific cluster of HSs in the 3' region of the gene showed enhancer activity in all cell types tested. In the light of this lack of specificity, we suggest that cell type-specific modification of the chromatin structure in this region may play a role in determining the binding of a widespread transcription factor, and hence contribute to the time specificity of lysozyme M gene expression.

Animals↗
PubMed1992

Spoil for choice.

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Decision Making↗
PubMed1992

A simple model of crack propagation in dental restorations.

Although natural teeth often exhibit microcracks, they rarely demonstrate bulk fracture. However, conventional full-crown restorations periodically exhibit failure due to fracture. Presented here is evaluation of a simple model of crack propagation that estimates crack growth during cyclic loading. A finite element model of a premolar tooth provides the tensile stresses adjacent to cusp loading. If the crack propagation rates for natural teeth, porcelain-fused-to-metal crowns and composite crowns are compared with the wear rates of their respective materials as determined in an artificial mouth, it is evident that the low wear rate of composites may predispose them to fracture. Natural teeth disperse occlusal stresses throughout the dentin so that the effect of high occlusal stress is minimized. Porcelain tends to wear the opposing dentition, which reduces areas of high occlusal stress. Composite, however, demonstrates crack propagation rates higher than those of either natural teeth or porcelain. This, in addition to its low wear rate, might predispose the material to fracture. This model should be used only as a qualitative indicator of fracture tendency. The high calculated crack propagation rates in composites may explain the observed clinical failures and microchipping at the area of occlusal contact, as noted in SEM analysis.

Composite Resins↗
PubMed1992

Domain structure of U2 and U4/U6 small nuclear ribonucleoprotein particles from Trypanosoma brucei: identification of trans-spliceosomal specific RNA-protein interactions.

Maturation of mRNAs in trypanosomes involves trans splicing of the 5' end of the spliced leader RNA and the exons of polycistronic pre-mRNAs, requiring small nuclear ribonucleoproteins (snRNPs) as cofactors. We have mapped protein-binding sites in the U2 and U4/U6 snRNPs by a combination of RNase H protection analysis, native gel electrophoresis, and CsCl density gradient centrifugation. In the U2 snRNP, protein binding occurs primarily in the 3'-terminal domain; through U2 snRNP reconstitution and chemical modification-interference assays, we have identified discrete positions within stem-loop IV of Trypanosoma brucei U2 RNA that are essential for protein binding; significantly, some of these positions differ from the consensus sequence derived from cis-spliceosomal U2 RNAs. In the U4/U6 snRNP, the major protein-binding region is contained within the 3'-terminal half of U4 RNA. In sum, while the overall domain structure of the U2 and U4/U6 snRNPs is conserved between cis- and trans-splicing systems, our data suggest that there are also trans-spliceosomal specific determinants of RNA-protein binding.

Animals↗