Medical malpractice in gastroenterology.

Background & Aims: Gastroenterologists commonly perceive themselves to be at increased legal risk because they perform invasive procedures. However, there is little published information about gastroenterology (GI) malpractice claims. The goal of this study was to evaluate available malpractice claim data within GI.

Communication errors in radiology: a liability cost analysis.

Purpose: We evaluated the economic effect on radiologists involved in litigation of failures in communication of results.

Method: We examined claims data from the Physicians Insurers Association of America 2002 report on breast cancer and identified malpractice cases in which miscommunication, rather than misdiagnosis, was the primary cause for litigation.

Results: The average indemnity payment for primary errors in communication by radiologists was between $228,000 and $236,000, or twice as high as when appropriate communication occurred.

Properties of P-glycoprotein with mutations in the "catalytic carboxylate" glutamate residues.

It is known from earlier work that two conserved Glu residues, designated "catalytic carboxylates," are critical for function in P-glycoprotein (Pgp). Here the role of these residues (Glu-552 and Glu-1197 in mouse MDR3 Pgp) was studied further. Mutation E552Q or E1197Q reduced Pgp-ATPase to low but still measurable rates.

Combined mutation of catalytic glutamate residues in the two nucleotide binding domains of P-glycoprotein generates a conformation that binds ATP and ADP tightly.

Combined mutation of "catalytic carboxylates" in both nucleotide binding domains (NBDs) of P-glycoprotein generates a conformation capable of tight binding of 8-azido-ADP (Sauna, Z. E., Müller, M.

Synergy between conserved ABC signature Ser residues in P-glycoprotein catalysis.

Functional roles of the two ABC signature sequences ("LSGGQ") in the N- and C-terminal nucleotide binding domains of P-glycoprotein were studied by mutating the conserved Ser residues to Ala. The two single mutants (S528A; S1173A) each impaired ATPase activity mildly, and showed generally symmetrical effects on function, consistent with equivalent mechanistic roles of the two nucleotide sites. Synergy between the two mutations when combined was remarkable and resulted in strong catalytic impairment.

Total extracellular surfactant is increased but abnormal in a rat model of gram-negative bacterial pneumonia.

An in vivo rat model was used to evaluate the effects of Escherichia coli pneumonia on lung function and surfactant in bronchoalveolar lavage (BAL). Total extracellular surfactant was increased in infected rats compared with controls. BAL phospholipid content in infected rats correlated with the severity of alveolar-capillary leak as reflected in lavage protein levels (R(2) = 0.