Long-term survival of an infant with diffuse brainstem lesion diagnosed by prenatal MRI: a case report and review of the literature.

BACKGROUND: We describe a unique case of expansive diffuse brainstem lesion diagnosed prenatally by magnetic resonance imaging (MRI) with long-term survival. Findings of fetal and postpartum MRI were highly consistent with the characteristics of diffuse brainstem glioma. METHODS: Diagnosis was based on the features of MRI, and histopathology was not confirmed by biopsy. Although the prognosis of diffuse brainstem tumor is usually poor, this child was asymptomatic at birth and the neurological condition is still normal at 4 years of age without any treatment. RESULTS: During routine imaging follow-up, diameters of the expansion have remained stable, while the size of the lesion compared to the posterior fossa size has diminished. In addition to brainstem tumor, a skin lesion of the back was observed and MRI of the thoracic spine showed a large asymptomatic extradural cystic lesion suggesting an arachnoid cyst. The pontine tumor of this infant, in agreement with a few previously reported cases, suggests a subgroup of beneficial outcome of expansive diffuse brainstem lesions, particularly in the neonatal period. DISCUSSION: In this article, we discuss the prognosis and characteristics of pediatric brainstem tumors and differential diagnosis of neonatal brainstem lesions.

Electronic energy harvesting multi BODIPY-zinc porphyrin dyads accommodating fullerene as photosynthetic composite of antenna-reaction center.

Efficient electronic energy transfer (EET) in the newly synthesized dyads comprised of zinc porphyrin covalently linked to one, two or four numbers of boron dipyrrin (BDP) entities is investigated. Both steady-state and time-resolved emission as well as transient absorption studies revealed occurrence of efficient singlet-singlet energy transfer from BDP to zinc porphyrin with the time scale ranging between 28 and 48 ps. A decrease in time constants for energy transfer with increasing the number of BDP units is observed revealing better antenna effect of dyads bearing higher number of boron dipyrrin entities. Further, supramolecular triads to mimic the 'antenna-reaction center' functionality of photosynthetic reaction center have been successfully constructed by coordinating fulleropyrrolidine appended with an imidazole ligand to the zinc porphyrin. The structural integrity of the supramolecular triads was arrived by optical, computational and electrochemical studies. Free energy calculations revealed possibility of photoinduced electron transfer from singlet excited zinc porphyrin to fullerene, and the preliminary transient absorption studies involving pump-probe technique are supportive of occurrence of electron transfer from (1)ZnP* to fullerene in the supramolecular triads.

Carbonic anhydrase isoenzymes in isolated rat peripheral monocytes, tissue macrophages, and osteoclasts.

The presence of carbonic anhydrase isoenzymes I and II in rat monocytes and macrophagelike cells was studied using monospecific antisera against rat carbonic anhydrase I and II purified from red blood cells. CA II was strongly stained immunohistochemically in osteoclasts and macrophagelike cells in the umbilical cord. Foreign body giant cells, peritoneal macrophages, lung macrophages, and cultured peripheral monocytes, the presumed progenitor cells for osteoclasts, were negative with both antisera. Radioimmunoassay and immunoblotting similarly failed to demonstrate CA II in peripheral monocytes. The lack of CA in monocytes adds a new aspect to the discussion concerning the origin of osteoclasts and monocyte-mediated bone resorption.

Immunohistochemical localization of carbonic anhydrase isoenzyme C in the central and peripheral nervous system of the mouse.

The regional and cellular distribution of the high activity carbonic anhydrase isoenzyme (CA C or CA II) in the mouse nervous system was investigated by an indirect immunoperoxidase (peroxidase-antiperoxidase) method using cross-reactive antibodies prepared against human CA C. In the mature brain an overall strong CA C specific reactivity was revealed in the heavily myelinated nerve tracts, the main immunostaining originating from small, intensively reacting cells interpreted as oligodendrocytes and from the myelin sheaths. An obvious straining was also revealed in the choroid plexus cells, especially in their free borders, and in the erythrocytes of the blood vessels, while the glial cells of the retina similarly exhibited a strong reaction. In the developing brain, CA C was absent shortly after birth, but achieved almost the mature pattern of distribution within about 3 weeks. In the spinal cord most of the positive cells were found in the grey matter, their processes projecting towards the white matter. No reaction was obtained in the sciatic nerve fibers or in the neuronal or satellite cells of the coeliac ganglion.

Carbonic anhydrase in the type I skeletal muscle fibers of the rat. An immunohistochemical study.

The localization of carbonic anhydrase (CA) was studied in rat skeletal muscles with the use of immunohistochemical (peroxidase-antiperoxidase) method. CA was observed in all those fibers that also showed pH 4.3 stable actomyosin adenosine triphosphatase activity (type I fibers), but the reverse did not necessarily hold. More specifically, CA was apparently localized in I-bands, and a weak reaction was also observed in sarcolemma. The function of CA in muscle fibers is possibly connected with the greater demands on CO2 transport and buffer system in muscles adapted to long-lasting contractions.

Immunolabeling of carbonic anhydrase isoenzyme C and glial fibrillary acidic protein in paraffin-embedded tissue sections of human brain and retina.

The specificities of carbonic anhydrase isoenzyme C (CA C) and glial fibrillary acidic (GFA) protein as immunocytochemical markers for different glial cell populations in human brain and retina were studied using indirect immunofluorescence and peroxidase-antiperoxidase complex methods. With antibodies against CA C, only those cerebral cells that were morphologically oligodendrocytes and Müller cells of the retina showed positive immunostaining reaction, whereas antibodies against GFA protein selectively labeled cerebral astrocytes and a part of the glial cells and fibers in the inner layers of the retina. In double labeling, when both glial cell markers were successively localized in the same cerebral tissue sections, GFA protein immunofluorescence was never found in the immunoperoxidase-stained CA C-positive cells, which further supports the oligodendrocyte-specificity of CA C in human brain.

Immunohistochemical localization of carbonic anhydrase isoenzymes VI, II, and I in human parotid and submandibular glands.

Human salivary carbonic anhydrase (HCA VI) was purified by inhibitor affinity chromatography and its location in the human parotid and submandibular glands identified, using a polyclonal antiserum raised against the purified enzyme in rabbits in conjunction with the peroxidase-antiperoxidase complex method. The antibodies raised against the purified enzyme in rabbits did not crossreact with the HCA II or I. However, they slightly recognized human IgA; the antiserum was therefore absorbed with human IgA before immunohistochemical use. HCA VI-specific staining was detected in the cytoplasm and particularly in the secretory granules of the serous acinar cells of both parotid and submandibular glands, the staining of the secretory granules being most distinct in paraformaldehyde-fixed tissues. Some epithelial cells and the luminal content of the striated ducts also gave a specific HCA VI staining. Staining specific for HCA II was also found in the granules of the serous acinar cells, particularly in the submandibular gland when Carnoy fluid fixation was used. Slight HCA II-specific staining was also detected in the striated ductal cells in the Carnoy fluid-fixed specimens. No staining specific for HCA I was detected. The results indicate that the serous acinar cells in human parotid and submandibular glands contain abundant HCA II and HCA VI. Interestingly, only HCA VI is secreted into the saliva, although both enzymes appear to be located in structures resembling the secretory granules in the acinar cells. The enzymes probably form a mutually complementary system regulating the salivary buffer capacity.

Immunohistochemical localization of carbonic anhydrase isoenzyme C in human brain.

Carbonic anhydrase isoenzymes of human brain were examined by the immunoperoxidase method. Only the catalytically highly active isoenzyme C was found in normal cerebral and cerebellar tissues, being located in a limited number of non-neuronal cells interpreted as oligodendrocytes and in myelinated nerve fibres. The enzyme was not evident in the glial cells of astrocytomas.

A single-step solid phase radioimmunoassay for quantifying human carbonic anhydrase I and II in cerebrospinal fluid.

A single-step solid phase radioimmunoassay was developed to detect human carbonic anhydrase (CA) isoenzymes I (CA I) and II (CA II) in cerebrospinal fluid (CSF). The assay is capable of routinely detecting both isoenzymes at ng levels compared to the microgram levels of the traditional catalytic methods, which failed to demonstrate any CA activity in CSF. When the values of immunoreactive CA II in CSF were corrected for blood contamination (the CA I/CA II ratio of blood was about 7.9), the amount of brain tissue originated CA II could be calculated. The CA II values in CSF samples from 13 patients with multiple sclerosis were higher than those in CSF samples from 11 patients with various peripheral neurological disorders. Since CA II has been specifically localized to oligodendrocytes and myelin, our preliminary results suggest the possibility of CA II leakage from oligodendrocytes and myelin into CSF in demyelinating disease.

Immunohistochemical detection of renal carbonic anhydrase of patients with recurrent urolithiasis.

In renal exploratory excisions the isoenzyme C of the carbonic anhydrase was detected in 51 operative treated patients with recurrent urolithiasis and in 6 patients with ren mobilis or stenosis of the ureteral pelvic junction by using the immunohistochemical PAP-method. In the distal tubules and collecting ducts there is an alternating occurrence of cells with small and those with strong reactivity. This correlates with the distribution of mean or principal (P-, small reaction) and intercalated (I-, strong reaction) cells. The number of carbonic anhydrase rich cells and the degree of their cytoplasmic reaction to this enzyme seem to correlate with the ability of the urine to acidify. The patients were divided into four groups according to the mean urine pH estimated for a period of two weeks. The third group with predominantly acid urine (pH less than 5.8) showed a significantly increased number of carbonic anhydrase rich cells (mean = 63% +/- 6, n = 18) as compared to the first group (controls) without urolithiasis and normal urine (pH 5.8-6.8, mean = 46% +/- 8, n = 6) or the second group with urolithiasis and normal urine (pH 5.8-6.8, mean = 46% +/- 8, n = 28). The fourth group with predominant alkaline urine (pH greater than 6.8) showed a significantly decreased number of intercalated cells (mean = 42% +/- 16, n = 5) in comparison to the third group. Indeed, the difference with the control group is not significant but the cytoplasmic reaction of I-cells decreases distinctly in comparison to all other groups.

Endovascular treatment of peripheral aneurysms of the posterior inferior cerebellar artery.

BACKGROUND AND PURPOSE: Peripheral aneurysms of the posterior inferior cerebellar artery (PICA) are rare, and pre-existing literature concerning their endovascular treatment is limited. The purpose of this study was to assess the etiology and clinical characteristics of peripheral PICA aneurysms and to evaluate the angiographic and clinical results of the patients who underwent endovascular treatment for a peripheral PICA aneurysm in a single center. MATERIALS AND METHODS: Twelve consecutive patients with 12 peripheral PICA aneurysms (10 ruptured) included in an internal data base were retrospectively reviewed. Posttreatment and follow-up angiograms were analyzed, and the clinical outcome was recorded. RESULTS: The etiology was dissection in 7 (58%) and unknown in 5 cases (42%). Three dissecting aneurysms reruptured before endovascular treatment, and another 3 demonstrated angiographic progress. Four aneurysms were treated by endosaccular coiling, 6 (all dissecting) by parent artery occlusion, and in 2 cases endovascular treatment failed. Angiographic outcome was complete aneurysm and/or parent artery occlusion in 9 cases and neck remnant in 1 case. One aneurysm needed retreatment at follow-up. One lethal procedural complication occurred, and transient ischemic symptoms appeared in 2 patients. The clinical outcome was good in 7 patients, whereas 3 patients, all poor clinical grade, died (1 for unrelated reasons). No rebleedings have occurred during the follow-up. CONCLUSION: In this series, most peripheral PICA aneurysms were secondary to arterial dissection. They were unstable with a high risk of rebleeding and a high mortality if not treated without delay. Endovascular treatment was effective in preventing rehemorrhage.

Immunohistochemical demonstration of carbonic anhydrase isoenzyme C in the epithelium of the human ciliary processes.

Extravascular location of two main carbonic anhydrase isoenzymes was immunohistochemically investigated in human ciliary processes. The high-activity carbonic anhydrase isoenzyme C was clearly demonstrated in the ciliary epithelium, but was absent from the ciliary stroma. The low-activity isoenzyme B was evident neither in the epithelium nor in the stroma.

Immunohistochemical localization of human carbonic anhydrase isoenzyme C.

Methods for immunohistochemical localization of human carbonic anhydrase isoenzyme C (HCA C) with indirect fluorescent antibody and immunoperoxidase techniques are described. Both methods revealed large amounts of this "high activity" isoenzyme in the mucosae of human stomach and appendix. With the indirect immunofluorescent method the presence of the enzyme in human erythrocyte cytoplasm was also demonstrated. Correlations of present findings with those obtained with the traditional histochemical methods for demonstration of carbonic anhydrase activity are discussed.

Carbonic anhydrase isoenzyme C in the human retina. An immunohistochemical study.

The occurrence of carbonic anhydrase isoenzymes C and B in the retina of the human eye was examined with specific antisera against these enzymes. Immunological analysis were carried out by the double diffusion method of Ouchterlony, and the localization of the enzymes was studied by an application of immunoperoxidase (PAP) technique. A large amount of isoenzyme C was detected in tissue sections from the human retina, whereas the isoenzyme B was totally absent. Isoenzyme C was considered to be located primarily in the glial elements of the retina, correlating with the earlier findings obtained by traditional metal salt methods.

Human carbonic anhydrase isoenzyme C. Effects of some fixatives on the antigenicity and improvements in the method of localization.

The effects of some alcohol and aldehyde containing fixatives on the antigenicity of human carbonic anhydrase isoenzyme C (HCA C) were tested in order to reveal the most suitable method for the immunohistochemical localization of this enzyme. The use of 2% and 4% paraformaldehyde or 2% glutaraldehyde solutions before immunoperoxidase (PAP) staining resulted in the loss of HCA C-specific reactivity in the surface epithelial cells of human appendicular and gastric mucosae, whereas the antigenic reactivity of HCA C was well retained in the parietal cells of gastric glands. In corresponding tissue sections fixed with one of the alcohol containing solutions (abs. methanol, methanol + chloroform 2:1 or Carnoy fluid) both the surface epithelial and parietal cells showed HCA C-specific immunostaining after the PAP procedure. In addition, the antigenicity of HCA C was found to be well preserved in some tubular cells of human kidney fixed in Carnoy fluid. The paraffin infiltration at relatively low temperature did not markedly affect the enzyme antigenicity. Fixation in Carnoy fluid coupled with paraffin embedding at 55-60 degrees C in vacuo was found to give the best preservation of the antigenicity of HCA C with good morphological integrity for light microscopical localization.

Immunohistochemical localization of carbonic anhydrase isoenzymes in the human pancreas.

Carbonic anhydrase exists in two main forms (isoenzymes C and B) which differ from each other immunologically and in their level of activity, for instance. It is important to know the location of the enzyme in order to obtain a better understanding of its physiologic role. Since previous histochemical studies using metal salt methods for the demonstration of carbonic anhydrase activity have produced unsatisfactory results, the immunoperoxidase technique is applied here to investigate the location of the isoenzymes of carbonic anhydrase in the human pancreas. Isoenzyme C was localized specifically in the epithelium of the intra- and interlobular ducts, whereas the isoenzyme B was found only in the erythrocytes of the tissue. No carbonic anhydrase was found in the islets of Langerhans. The immunohistochemical results were confirmed by double immunodiffusion, in which the pancreatic tissue fluid from the thawed frozen sections generated a strong precipitation line with the rabbit antiserum against isoenzyme C and a very weak precipitation with the antiserum against the isoenzyme B.

Immunocytochemical localization of carbonic anhydrase on ultrathin frozen sections with protein A-gold.

The protein A-gold technique was used to localize carbonic anhydrase isozymes on ultrathin frozen sections of kidney collecting duct epithelial cells and erythrocytes. The particulate nature of the gold marker gives a more precise appreciation of the intracellular distribution of this enzyme than has been previously possible, and allows the intensity of the labeling to be quantified. Intercalated cells showed four times more labeling over the cytosol than adjacent principal cells in collecting ducts from the inner stripe of the outer medulla: by double-labeling using protein A-gold particles of different sizes, carbonic anhydrase isozymes B and C were simultaneously localized in erythrocytes.

Management of patients with pain.

Out of an early study of 74 patients treated for pain at our facilities, 14 were selected for dorsal column stimulation (DCS). Compared to a control group on medications, the DCS patients benefited in terms of reduced amounts of pain relievers needed. One patient showed transient loss of somatosensory evoked potentials in association with the use of a high frequency stimulator at the cervical level, as possible evidence of the potential dangers to neural tissue related to the use of bioelectrical devices. However, despite the development of pain centers, new neurosurgical methods including bioelectrical equipment should be devised for treatment of pain patients who are referred from these multidisciplinary centers for neurosurgical treatment.