Inflammatory myofibroblastic tumours of the liver - a systematic review.

BACKGROUND: Hepatic inflammatory myofibroblastic tumours (HIMTs) are rare and poorly described in the literature. Most publications are single patient case reports and lack detailed reporting on characteristics, management, and outcomes. This systematic review aimed to assess the demography, clinical presentation, typical imaging features, histopathology, treatment, and outcomes of patients presenting with HIMTs. METHODS: A systematic literature search was performed in MEDLINE (PubMed), EMBASE (Scopus), JSTOR, Cochrane CENTRAL (Cochrane Library), and the databases included in the Web of Science for studies published between 1940 and 2023 on HIMTs, including its reported synonyms. Case series or cohort studies that reported on the management and outcomes of at least four patients with histologically confirmed HIMTs were included in the analysis. RESULTS: After screening 4553 publications, 22 articles including a total of 440 patients with confirmed HIMTs were eligible for inclusion. The average age was 53.4 years (range 42.0-65.0) with a male to female ratio of 1.7:1. Abdominal pain, discomfort, fever, and loss of weight were the most common presenting symptoms. Surgical resection is the standard of care for HIMTs and is associated with low mortality of 3.4% and low disease recurrence. CONCLUSION: HIMT is a disease more often affecting middle-aged males. The lesions are typically solitary with low recurrence after treatment. The relative roles of surgical versus medical treatment remain unclear. Differences in clinical presentation, histopathology, and treatment of HIMTs compared to inflammatory myofibroblastic tumour (IMT) at extrahepatic sites could challenge the current view of IMT as a single pathological entity.

Energy distributions at the high-spin ferric sites in myoglobin crystals.

The orientation and temperature dependence (4.2-2.5 K) of electron paramagnetic resonance (EPR) power saturation and spin-lattice relaxation rate, and the orientation dependence of signal linewidth, were measured in single crystals of the aquo complex of ferric sperm whale skeletal muscle myoglobin. The spin-packet linewidth was found to be temperature independent and to vary by a factor of seven within the heme plane. An analysis is presented which enables one to arrive at (a) hyperfine component line-widths and, from the in-plane angular variation of the latter, at (b) the widths of distributions in energy differences between low-lying electronic levels and (c) the angular spread in the in-plane principal g-directions. The values of the energy level distributions in crystals obtained from the measurements and analysis reported here are compared with those obtained by a different method for the same protein complex in frozen solution. The spread in the rhombic energy splitting is significantly greater in solution than in the crystal.

EPR characterization of alcohol complexes of ferric myoglobin and hemoglobin.

Frozen solution electron paramagnetic resonance spectra of the aquo, methanol, and ethanol complexes of ferric myoglobin and hemoglobin are quantitatively analyzed in terms of the rhombic to tetragonal symmetry ratio and the admixture of quartet states, both with regard to central values of these parameters and the widths of their distributions. In both the methanol and ethanol complexes of ferric myoglobin the main change from the aquo complex is a narrowing of the spread in the rhombic to tetragonal symmetry ratio (reduction in structural variation). The alcohol complexes of both the alpha- and beta-chains within the tetramer of ferric hemoglobin are characterized by a lowering of symmetry (as compared with the aquo complex). Qualitative differences in distribution widths among the complexes are consistent with an origin in molecular structure and dynamics rather than in ice matrix-induced strain.

Crystalline state disorder and hyperfine component line widths in ferric hemoglobin chains.

In X-band electron paramagnetic resonance spectra from single crystals of horse ferric hemoglobin, observed line widths at the low- and high-field extrema are 30 and 24 g, and as much as 400 G in the intermediate region. This behavior is similar to that of ferric myoglobin. Due to large anisotropy in the g-tensors, the line width variation can be accounted for on the basis of heme orientation disorder. This disorder is characterized by an angle, determined here by two independent methods. In these computations Gaussian disorder on a sphere is assumed. The disorder angle is found to be constant on the sphere and about 4 degrees for both alpha- and beta- chains. Treatment of crystals with heavy water (buffer) increases the disorder. Since ligand nitrogen hyperfine couplings are available from hemoglobin electron nuclear double resonance, single crystal electron paramagnetic resonance spectra can be simulated by superimposing hyperfine bands, where the line width of the component bands is a variable and the disorder model above is employed. Comparison with observed resonances fixes the hyperfine component line widths. These component line widths from ferric hemoglobin in the crystalline state are found to be smaller than those in frozen solution.

Quantitative evaluation of contributions to electron paramagnetic resonance line widths in ferric hemoglobin single crystals.

The contributions to the dipolar broadening of ferric magnetic resonances, from crystals of hemoglobin for which the atomic coordinates are known, have been calculated. The total second moment of the g = 2 resonance so determined is about 50 (MHz)2 or 5.0 G (peak-to-trough), figures consistent with the range of values found from analysis of experimental data. Two-thirds of this second moment comes from the two protons of the H2O molecule coordinated to the iron. Treatment with D2O is predicted to reduce the total second moment at g = 2 to about 25 (MHz)2, whereas the experimental measurements on single crystals show no decrease. If the structure of the tetramer is assumed to be the same when in solution as in the crystal, the total second moment is readily redetermined for hemoglobin in solution; the value so obtained is found to be significantly smaller than that from analysis of the g = 2 resonance measured in frozen solution. These two unexpected observations can be explained in terms of distributions in spin Hamiltonian parameters, the spread depending upon the nature of the sample--crystal or solution, ordinary or heavy water-treated. This distribution in H2O and D2O solutions appears to be about the same, since the measured differences in component line width agree with the calculated difference in dipolar contributions.