[Severe carotid stenosis: cerebral autoregulation in the ipsilateral region]. / Kriticheskie stenozy vnutrennikh sonnykh arterii: tserebral'naia autoreguliatsiia v ipsilateral'nom basseine.

AIM: To study cerebral autoregulation (CA) in region of the stenotic carotid artery. MATERIAL AND METHODS: The study involved 35 patients with critical stenosis of the carotid arteries, including 24 patients were asymptomatic and 11 patients with symptomatic course. Blood flow velocity in middle cerebral arteries was monitored using Multi Dop X (DWL, Germany) with simultaneous noninvasive systemic blood pressure registration (CNAP, Austria). CA was assessed by calculating the phase shift (PS) between spontaneous oscillations of blood flow velocity and blood pressure within the range of systemic Mayer waves (80-120 mHz). RESULTS: In 18 patients, the CA indicators were in the normal range (PS 1.2±0.3 rad). Seventeen patients, including asymptomatic as well as symptomatic types, had impaired CA (PS 0.2±0.2 rad and 0.3±0.2 rad, respectively). Reconstructive surgery, irrespective of clinical manifestations, led to the significant increase in PS (p<0.001) in the early postoperative period (0.9±0.5 and 0.9±0.3 rad, respectively). CONCLUSION: A significant variability in the cerebrovascular reserve capacity in symptomatic and asymptomatic types of carotid artery stenosis was found. CA can be used in determining the indications for surgical treatment and evaluation of its effectiveness in patients with stenosis of carotid arteries.

Purification of a soluble cytochrome P450 from Trichosporon montevideense.

The yeast Trichosporon montevideense CBS 6721 expressed large amounts of cytochrome P450 after cultivation in a glucose-peptone medium. The P450, which could be detected in the cytosolic fraction after cell breakage and ultracentrifugation, was purified to electrophoretic homogeneity and migrated in SDS-PAGE with a M(r) of 43,000. As indicated by IEF, the preparation consisted of two different P450 isoforms with pI-values of 5.9 and 6.2, which were named P450MS1 and P450MS2 respectively. Both isoforms had a characteristic maximum at 446 nm in the reduced carbon monoxide difference spectra. Partial N-terminal sequencing of P450MS1 and P450MS2 demonstrated a high degree of sequence homology between the soluble P450 enzymes of T. montevideense CBS 6721 and their close relationship to the soluble P450 forms of Trichosporon spec. SBUG 752, T. cutaneum ATCC 58094 and to the P450s of the CYP55 family of Fusarium oxysporum and Cylindrocarpon tonkinense.

Identification, mapping, and genomic structure of a novel X-chromosomal human gene (SMPX) encoding a small muscular protein.

Reciprocal probing has been used to identify a cDNA clone (xh8H11) representing a gene preferentially expressed in striated muscle. The gene maps close to DXS7101 31.9 cM from the short arm telomere of the X-chromosome at Xp22.1. On searching expressed and genomic databases, 21 expressed sequence tags were found that allowed the assignment of a human extended consensus sequence of 887 bp, suggesting a completely expressed gene symbolized as SMPX. By using the human consensus sequence, the orthologous mouse Smpx and rat SMPX genes could be aligned and confirmed by complete sequencing of additional SMPX-related clones obtained by library screening. An open reading frame was identified encoding a peptide of 88-86 and 85 amino acids in human and rodents, respectively. The predicted peptide had no significant homologies to known structural elements. The human consensus cDNA sequence was used to define the genomic structure of the human SMPX that had been missed by a previous large scale sequencing approach. The gene consists of five exons (> or =172, 57, 84, 148, > or =422 bp) and four introns (3639, 10410, 6052, 31134 bp) comprising together 52.1 kb and is preferentially and abundantly expressed in heart and skeletal muscle. Thus, a novel human gene encoding a small muscular protein that maps to Xp22.1 (SMPX) has been identified and structurally characterized as a basis for further functional analysis.