Rural and urban differences in physician resource use for low-risk obstetrics

OBJECTIVE: To explore the hypothesis that rural obstetricians (OBs) and family physicians (FPs) utilized fewer resources during the care of the low-risk women who initially booked with them than did their urban counterparts of the same specialties. DATA SOURCES/STUDY DESIGN: A stratified random sample of Washington state rural and urban OBs and FPs was selected during 1989. A participation rate of 89 percent yielded 209 participating physicians. The prenatal and intrapartum medical records of a random sample of the low-risk patients who initiated care with the sampled providers during a one-year period were abstracted in detail and analyzed with the physician as the unit of analysis. Complete data for 1,683 patients were collected. Resource use elements (e.g., urine culture) were combined by standardizing them with average charge data so that aggregate resource use could be analyzed. Intraspecialty comparisons for resource use by category and overall were performed. FINDINGS/CONCLUSIONS: Results show that rural physicians use fewer overall resources in caring for nonreferred low-risk-booking obstetric patients than do their urban colleagues. Resource use unit expenditures showed the hypothesized pattern for both specialties for total, intrapartum, and prenatal care with the exception of FPs for prenatal care. Approximately 80 percent of the resource units used by each physician type were related to hospital care. No differences were shown in patterns of care for most clinically important aspects of care (e.g., cesarean delivery rates), and no evidence suggested that outcomes differed. The overall differences were due to specific components of care (e.g., fewer intrapartum hospital days and less epidural anesthesia).     

Embolization with temporary balloon occlusion of the internal carotid artery and in vivo proton spectroscopy improves radical removal of petrous-tentorial meningioma

A highly vascular petroclival meningioma supplied by tentorial branches of the internal carotid artery was embolized by temporary balloon occlusion of the parent vessel distal to the tumor, followed by obliteration of the tumor vascularity with polyvinyl alcohol particles. Subsequently, in vivo proton spectroscopy showed necrosis of a large portion of the tumor and helped determine the timing of surgery. Both innovative techniques considerably facilitated the subsequent radical excision of the tumor with no neurological morbidity.     

Small cardioactive peptide B increases the responsiveness of the neural system underlying prey capture reactions in the pteropod mollusc, Clione limacina

Effects of small cardioactive peptide B (SCPB) on cerebral neurons which underlie prey capture in the carnivorous pteropod mollusc, Clione limacina, were investigated. SCPB in concentrations of 10 microM and higher produced direct activation of cerebral ganglion neurons underlying extrusion of buccal cones used in prey capture. SCPB in lower concentrations, between 1 and 5 microM, did not have a noticeable effect on the membrane potentials of these neurons; however, it significantly increased their responsiveness to sensory inputs from the tactile stimulation of the head, and their ability to generate afterdischarge activity. SCPB immunoreactivity was observed in cell bodies in buccal, cerebral, pedal, and intestinal ganglia, as well as in the anterior esophagus and in buccal cones where fibers stained intensely. These electrophysiological and immunohistochemical data suggest that SCPB may have a physiological role in feeding arousal in Clione.     

Identification of serines-1035/1037 in the kinase domain of the insulin receptor as protein kinase C alpha mediated phosphorylation sites

A new site of serine phosphorylation (Ser-1035/1037) has been identified in the kinase domain of the insulin receptor. Mutant receptors missing these two serines were expressed in Chinese hamster ovary cells overexpressing protein kinase C alpha. These mutant receptors lacked a phorbol ester-stimulated phosphoserine containing tryptic peptide as demonstrated by both high percentage polyacrylamide/urea gel electrophoresis and two-dimensional tlc. Moreover, a synthetic peptide with the sequence of this tryptic peptide was phosphorylated by isolated protein kinase C alpha and co-migrated with the phosphopeptide from in vivo labeled receptor. These results indicate that serine-1035 and/or 1037 in the kinase domain of the insulin receptor are phosphorylated in response to activation of protein kinase C alpha.     

Reduced HIV-1 infectability of CD4+ lymphocytes from exposed-uninfected individuals: association with low expression of CCR5 and high production of beta-chemokines

Escherichia coli leader peptidase, an integral membrane protein, is responsible for the cleavage of the signal sequence of many exported proteins. Recent studies suggest that it is a novel serine protease that utilizes a serine-lysine catalytic dyad. In an effort to further understand the mechanism of this enzyme, an internally quenched fluorescent peptide substrate incorporating the leader peptidase cleavage site of maltose binding protein signal peptide, Y(NO2)-F-S-A-S-A-L-A-K-I-K(Abz) (anthraniloyl), was designed and synthesized. In the intact peptide, the fluorescence of the anthraniloyl group is quenched by the 3-nitrotyrosine. This quenched fluorescence is liberated upon cleavage of the peptide by the leader peptidase, resulting in increased fluorescence that could then be monitored fluorometrically. The designed substrate can be cleaved effectively by E. coli leader peptidase as detected by both HPLC and fluorescent spectroscopy. Mass spectra of cleavage products demonstrated that the cleavage occurs at the predicted site (A-K). The cleavage of the peptide substrate has a linear dependence on the enzyme concentration (0.1 to 1.9 microM) and the kcat/K(m) was calculated to be 71.1 M-1 s-1. These data are comparable with the unmodified peptide substrate. This report represents the first direct continuous assay based on fluorescence resonance energy transfer for E. coli leader peptidase.     

The two steps of group II intron self-splicing are mechanistically distinguishable

The two transesterification reactions catalyzed by self-splicing group II introns take place in either two active sites or two conformations of a single active site involving rearrangements of the positions of the reacting groups. We have investigated the effects on the rates of the chemical steps of the two reactions due to sulfur substitution of nonbridging oxygens at both the 5' and 3' splice sites as well as the deoxyribose substitution of the ribose 2' hydroxyl group at the 5' splice site. The data suggest that the two active sites differ in their interactions with several of these groups. Specifically, sulfur substitution of the pro-Sp nonbridging oxygen at the 5' splice site reduces the chemical rate of the step one branching reaction by at least 250-fold, whereas substitution of the pro-Sp oxygen at the 3' splice site has only a 4.5-fold effect on the chemical rate of step two. Previous work demonstrated that the Rp phosphorothioate substitutions at both the 5' and 3' splice sites reduced the rate of both steps of splicing to an undetectable level. These results suggest that either two distinct active sites catalyze the two steps or that more significant alterations must be made in a single bifunctional active site to accommodate the two different reactions.