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Biomedical subjects

M O Jones

Publications and source records attributed to M O Jones.

27 records · Page 2Linked to original sources
PubMed1993

The metabolic response to operative stress in infants.

The aim of this study was to characterize energy metabolism and substrate utilization in infants following an operation. Nineteen infants (weight 3.2 +/- 0.2 kg) who had an operation were studied. Anesthesia was standardized and operative stress score (OSS) was recorded. Five infants had a minor operation (OSS < 7), and 14 infants had a major operation (OSS > or = 7). Energy and nitrogen intake were constant during the 48-hour study period. Respiratory gas exchange was measured by indirect calorimetry preoperatively, and postoperatively for the first 12 hours continuously and at 24 hours, 48 hours, and 5 days. Urinary nitrogen excretion rate was measured for the first 48 hours following the operation. Physical activity was scored. Resting energy expenditure (REE) and nonprotein respiratory quotient (NPRQ) were calculated. REE increased postoperatively, peaking at 2 to 4 hours, and returned to baseline levels by 12 to 24 hours. Peak REE was significantly higher than baseline REE (P < .001). Substrate utilization was not altered by operation. The increase in REE was significantly greater in infants having a major operation than in infants having a minor operation (P < .05). Among infants having a major operation, the increase in REE was significantly greater in those infants more than 48 hours old, than in those infants less than 48 hours old (P < .05).(ABSTRACT TRUNCATED AT 250 WORDS)

Calorimetry, Indirect↗
PubMed1993

A method for urine collection in infants.

A simple, inexpensive, non-invasive method for urine collection was used in 28 consecutive infants for periods of 48 hours (n = 10) and 72 hours (n = 18). The incidence of urine collector detachment was low on the first and second days (< 4%) and increased significantly on the third day (28%). Volume of urine leaked was < 4% of the total volume collected daily. This method is applicable to both sexes and is reliable for up to 48 hours.

Evaluation Studies as Topic↗
PubMed1992

Distribution of cells expressing myc proteins in human colorectal epithelium, polyps, and malignant tumors.

The myc gene family encodes nuclear phosphoproteins that are thought to play a role in the control of cellular proliferation and differentiation. We have undertaken an immunohistochemical study assessing the expression of myc gene family proteins in individual cells of normal colonic mucosa, colorectal polyps, and colorectal adenocarcinomas. We screened a panel of mouse monoclonal antibodies that we raised against recombinant human c-myc and N-myc proteins for recognition of myc proteins in paraffin tissue sections. Two of these antibodies, H120C69 and H8C150, were selected for indirect immunoperoxidase staining of tissue sections from 16 normal mucosas, 24 polyps, and 30 adenocarcinomas. In normal colon, about 25% of the cells in the lower one-third of the crypts of Lieberkühn stain for myc-related protein. This distribution resembles that of proliferating cells in the crypt. Benign hyperplastic polyps resemble normal mucosa in their myc staining pattern, with about 25% of the cells positive. In adenomatous polyps, the putative precursors of adenocarcinomas, from 50 to 100% of the cells stain positively for myc protein. In these cases, stained cells extend to the luminal surface, consistent with the previously reported expansion of the proliferation zone in these lesions. All adenocarcinomas examined had increased levels of myc protein relative to normal mucosa. The tumor cells exhibited markedly heterogeneous myc staining patterns, both among different tumors and, in some cases, within a single tumor. Comparison with Ki-67 monoclonal antibody staining indicates that myc protein expression in many tumors is uncoupled from cellular proliferation. Surprisingly, we observed increased numbers of myc-expressing cells and increased levels of myc protein in histologically normal colon directly adjacent to tumor, suggesting that many colorectal carcinomas secrete growth factors that activate gene expression in neighboring normal mucosa.

Adenocarcinoma↗
PubMed1987

Atomic structure of thymidylate synthase: target for rational drug design.

The atomic structure of thymidylate synthase from Lactobacillus casei was determined at 3 angstrom resolution. The native enzyme is a dimer of identical subunits. The dimer interface is formed by an unusual association between five-stranded beta sheets present in each monomer. Comparison of known sequences with the Lactobacillus casei structure suggests that they all have a common core structure around which loops are inserted or deleted in different sequences. Residues from both subunits contribute to each active site. Two arginine side chains can contribute to binding phosphate on the substrate. The side chains of several conserved amino acids can account for other determinants of substrate binding.

Amino Acid Sequence↗
PubMed1979

Location of the regulatory site for establishment of repression by bacteriophage lambda.

During the lysogenic response to infection by bacteriophage lambda, the phage-specified cII and cIII proteins provide for the coordinate establishment of repression and integration of the viral DNA. One critical regulatory function of cII/cIII is an activation of synthesis of the cI protein, the repressor that maintains lysogeny. The mechanism and site for regulation of the cI gene by cII/cIII have been a subject of controversy. The two principal hypotheses for cII/cIII action are: initiation of new RNA chains in the y region of lambda DNA just to the left of the cII gene; or antitermination of a short leader RNA (4S or oop RNA) initiated to the right of the cII gene. In an effort to distinguish between these hypotheses, we have studied the cII-mediated turn-on of cI protein synthesis in three classes of prophage deletion strains: deletions of the 4S RNA promoter but not the y region, deletions that remove both regions, and deletions that leave both intact. We find that an intact y region is required for normal regulation of the cI gene by cII, but the 4S RNA promoter is not. From experiments with other mutants, we conclude that rightward transcription from the early lytic promoter is also not necessary for positive regulation. Our results suggest that positive regulation by cII/cIII involves initiation of new RNA chains through activation of promoter sites.

Binding Sites↗