Identification of the gene encoding the human mitochondrial RNA polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence Tags database

A gene cloning strategy based on the screening of the Expressed Sequence Tags database (dbEST) using sequences of mitochondrial housekeeping proteins of yeast was employed to identify the cDNA encoding the precursor of the human mitochondrial RNA polymerase (h- mtRPOL). The 3831 bp h-mtRPOL cDNA is located on chromosome 19p13.3 and encodes a protein of 1230 amino acid residues. The protein sequence shows significant homologies with sequences corresponding to mitochondrial RNA polymerases from lower eukaryotes, and to RNA polymerases from several bacteriophages. The mitochondrial RNA polymerase carries out the central activity of mitochondrial gene expression and, by providing the RNA primers for replication- initiation, is also implicated in the maintenance and propagation of the mitochondrial genome. Genes involved in the control of mtDNA replication and gene expression are attractive candidates for human disorders due to abnormalities of nucleo-mitochondrial intergenomic signalling. The availability of the h-mtRPOL cDNA will allow us to test its role in mitochondrial pathology. In addition, we propose the 'cyberscreening' of dbEST, based on yeast/human cross-species comparison, as a powerful, simple, rapid and inexpensive method, that may accelerate several-fold the molecular dissection of the human mitochondrial proteome.      

Bullous eosinophilic cellulitis (Wells'' syndrome) associated with Churg–Strauss syndrome

We report a patient with Churg-Strauss syndrome (CSS) with asthma, eosinophilia, nasal polyposis and ANCA-associated multisystem vasculitis, who's skin eruption started with erythematous urticarial-plaques followed by haemorrhagic bullae. Histology of the plaques revealed 'flame figures' in the dermis with no granulomatous or vasculitic process, consistent with the diagnosis of eosinophilic cellulitis or Wells' syndrome. The association of CSS and Wells' syndrome observed in this patient may have a common pathogenesis. CSS may induce Wells' syndrome by an unknown factor.     

Acute otomastoiditis and its complications: role of CT

Acute bacterial (suppurative) otomastoiditis responds to antibiotic treatment; radiologic study is required only when there is clinical suggestion of coalescent mastoiditis, intracranial complications, or an underlying chronic disease. Computed tomography (CT) is the method of choice for evaluating otogenic intra- or extra-cranial complications. CT scans can show stages of disease progression when infection has spread by way of soft tissue, blood, and bone pathways into the dural venous sinuses, meninges, labyrinth, facial nerves, epidural and other intracranial spaces. When there is clinical suggestion of acute coalescent mastoiditis, a CT scan of the temporal bone can confirm the presence of rarefying osteitis, coalescence of the air cells, and subperiosteal abscess.     

Fc-independent cross-linking of a novel platelet membrane protein by a monoclonal antibody causes platelet activation

A monoclonal antiplatelet antibody (MA-13G8E1) is described that dose- dependently induces platelet aggregation and serotonin release in an Fc- independent fashion. Whereas platelets were equally aggregated by F(ab')2 fragments of this monoclonal antibody (MoAb), its Fab fragments, on the other hand, were inactive, indicating that divalent interaction is an essential requirement to induce platelet activation by MA-13G8E1. In addition, we could show that platelet epitope cross- linking by MA-13G8E1 occurred on the same platelet. MA-13G8E1 stimulated platelet phospholipase C (PLC) and induced activation of protein kinase C (PKC), both of which were almost unaffected by aspirin pretreatment. Furthermore, PLC activation appeared to be a direct antibody-mediated effect, since intracellular Ca2+ rises were not inhibited by EGTA, cytochalasin B, or aggregation-blocking MA-16N7C2 (antiglycoprotein [anti-GP]IIb/IIa). The MA-13G8E1 antigen is constitutively expressed on resting platelets of different species (7,100 +/- 800 molecules per human platelet), but not on other cell types tested. Both immunoprecipitation and affinity isolation by MA- 13G8E1 showed two low-molecular weight proteins (45 and 36 kD), having slightly acidic isoelectric pH levels (4.5 to 5.5) and forming multimolecular complexes. In conclusion, we found an MoAb that is able to induce platelet activation in an Fc-independent fashion. The mechanism involves cross-linking of a hitherto undescribed platelet membrane protein, leading to PLC and PKC stimulation.     

Compression of the left brachiocephalic vein by the innominate artery resulting in massive arm edema in a hemodialysis patient.

We report case of extrinsic compression of the left brachiocephalic vein by the innominate resulting in massive edema of the arm in a patient with hemodialysis Gore-Tex graft. To our knowledge, such phenomenon has not been previously reported.     

Low seminal zinc bound to high molecular weight proteins in asthenozoospermic patients: evidence of increased sperm zinc content in oligoasthenozoospermic patients [published erratum appears in Hum Reprod 1998 Jun;13(6):1750]

Total seminal zinc concentration, seminal zinc fraction bound to high molecular weight proteins (HMW-Zn%) and zinc content in spermatozoa were assayed in the ejaculates of 90 asthenozoospermic patients subdivided into two study groups: normoasthenozoospermics (group I: n = 50) and oligoasthenozoospermics (group II: n = 40). The zinc concentrations of patients were compared with those of a control group of donors showing normal semen parameters. All samples were also investigated for their sperm membrane functional integrity by the hypo- osmotic swelling test (HOS). The results showed normal total zinc concentrations but very low HMW-Zn% values (P < 0.001) in seminal plasma of the two groups of asthenozoospermic patients compared to the controls. Furthermore higher zinc amounts (P < 0.001) were measured in spermatozoa of oligoasthenozoospermic patients compared to group I and to the control group. Oligoasthenozoospermics also displayed a lower HOS score (P < 0.001) compared to the other two groups. These data suggest that the increased unbound seminal zinc could contribute to the decrease of sperm motility in normoasthenozoospermic and oligoasthenozoospermic patients. A further impairment in sperm motility could occur in the oligoasthenozoospermic patients where the increase of seminal free zinc was followed by a major zinc uptake by spermatozoa. The higher intrasperm zinc content in these patients could be a reflection of their low sperm membrane functionality.