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R M Wright

Publications and source records attributed to R M Wright.

At least 37 records · Page 2Linked to original sources

Analysis of aldehyde oxidase and xanthine dehydrogenase/oxidase as possible candidate genes for autosomal recessive familial amyotrophic lateral sclerosis.

Recently, point mutations in superoxide dismutase 1 (SOD1) have been shown to lead to a subset of autosomal dominantly inherited familial amyotrophic lateral sclerosis (ALS). These findings have led to the hypothesis that defects in oxygen radical metabolism may be involved in the pathogenesis of ALS. Therefore, we decided to analyze other enzymes involved in oxygen radical metabolism for possible involvement in other forms of ALS. We report here analysis of two genes encoding the molybdenum hydroxylases aldehyde oxidase (AO) and xanthine dehydrogenase/oxidase (XDH) for involvement in ALS. Of particular interest, one gene identified as encoding aldehyde oxidase is shown to map to 2q33, a region recently shown to contain a gene responsible for a familial form of ALS with autosomal recessive inheritance (FALS-AR). The AO gene appears to be located within 280,000 bp of simple sequence repeat marker D2S116, which shows no recombination with the FALS-AR locus. The AO gene is highly expressed in glial cells of human spinal cord. In addition, we mapped a gene for XDH to 2p22, a region previously shown to contain a highly homologous but different form of XDH. Neither of these XDH genes appears to be highly expressed in human spinal cord. This evidence suggests that AO may be a candidate gene for FALS-AR.

Aldehyde Oxidase↗

Binding epitope of somatostatin defined by phage-displayed peptide libraries.

We have developed a versatile phagemid system to display peptides on the surface of M13 bacteriophage at a copy number which approaches monovalency. In this system, a phagemid encodes a peptide fused to the amino-terminus of the second domain (dII) of the minor coat protein pIII under control of the inducible lac promoter. The fusion protein is displayed in combination with several copies of wild-type pIII on the surface of phage. Two diverse random octapeptide libraries, one linear and one which contained flanking cysteines capable of forming disulfide bridges, were were generated using an in vitro mutagenesis approach and affinity selected on an anti-somatostatin mAb. Peptides with high affinity for the mAb were enriched only from the cyclic library and the tetrapeptide, FWKT, was identified by consensus as the binding epitope. The selected peptides exhibited not only the primary amino acid sequence but also shared structural features with somatostatin. One peptide, CRFWKTWC, also exhibited nanomolar affinities for the five known somatostatin receptor subtypes. This system can easily be adapted to display individual peptides or a wide range of custom peptide libraries.

Amino Acid Sequence↗

Mitochondrial respiration scavenges extramitochondrial superoxide anion via a nonenzymatic mechanism.

We determined that mitochondrial respiration reduced cytosolic oxidant stress in vivo and scavenged extramitochondrial superoxide anion (O2-.) in vitro. First, Saccharomyces cerevisiae deficient in both the cytosolic antioxidant cupro-zinc superoxide dismutase (Cu,Zn-SOD) and electron transport (Rho0 state) grew poorly (P < 0.05) in 21% O2 compared with parent yeast and yeast deficient only in electron transport or Cu,Zn-SOD, whereas anaerobic growth was the same (P > 0.05) in all yeast. Second, isolated yeast and mammalian mitochondria scavenged extramitochondrial O2-. generated by xanthine/xanthine oxidase. Yeast mitochondria scavenged 42% more (P < 0.05) extramitochondrial O2-. during pyruvate/malate-induced respiration than in the resting state. Addition of either antimycin (respiratory chain inhibitor) or FCCP (respiratory chain uncoupler) prevented increased O2-. scavenging. Mitochondria isolated from yeast deficient in the mitochondrial manganous superoxide dismutase (Mn-SOD) increased (P < 0.05) O2-. scavenging 56% during respiration. This apparent SOD activity, expressed in units of SOD activity per milligram of mitochondrial protein, was the same (9 +/- 0.6 vs. 10 +/- 1.0; P = 0.43) as the O2-. scavenging of mitochondria with Mn-SOD, suggesting that respiration-dependent mitochondrial O2-. scavenging was nonenzymatic. Finally, isolated rat liver and lung mitochondria also increased (P < 0.05) O2-. scavenging during respiration. We speculate that respiring mitochondria, via the protonmotive pump, present a polarized, proton-rich surface that enhances nonenzymatic dismutation of extramitochondrial O2-. and that this is a previously unrecognized function of mitochondrial respiration with potential physiological ramifications.

Animals↗

Tissue specificity of the acrosomal protein SP-10: a contraceptive vaccine candidate molecule.

The tissue specificity of the intra-acrosomal protein SP-10 was examined by Northern blot and polymerase chain reaction (PCR) analysis. Messenger RNA from 36 tissues in the female baboon (Papio papio) was isolated, separated on agarose gels, transferred to nylon, and probed with either SP-10, beta-actin, or cyclophilin cDNA. Northern blots, which were processed at both low and high stringency, showed SP-10 to be expressed exclusively in the testis. The mRNA from each tissue was also reverse transcribed, and both SP-10 and beta-actin were amplified by PCR from the resulting cDNA. Ethidium bromide-stained agarose gels of the SP-10 PCR products showed three clear bands from the testis but no co-migrating bands from the other tissues. Southern blots of the PCR products showed that only the three bands in the testis were related to SP-10. The data demonstrate that the SP-10 gene products are testis specific, a characteristic essential for a contraceptive vaccine candidate molecule.

Acrosome↗

Human SP-10: acrosomal distribution, processing, and fate after the acrosome reaction.

SP-10 is a testis-specific acrosomal protein that has been detected in several species including humans. Extracts from whole human testis and epididymal, ejaculated, and capacitated sperm were analyzed by Western blot for SP-10 polypeptides. The testis extracts contained a full-length SP-10 protein at approximately 45 kDa as well as other immunoreactive SP-10 peptides at 32, 30, 28, and 26 kDa. Extracts from epididymal, ejaculated, and capacitated sperm contained several immunoreactive SP-10 peptides that co-migrated with the 32-26-kDa SP-10 peptides in the testis extracts. Epididymal, ejaculated, and capacitated sperm extracts did not contain the 45-kDa SP-10 peptide observed in testis extracts, but did contain immunoreactive SP-10 peptides from 25 to 18 kDa that were not detected in testis extracts. These results indicate that a full-length 45-kDa SP-10 precursor protein is present in the testis and that SP-10 peptides of 32, 30, 28, and 26 kDa result from proteolytic processing of the SP-10 precursor protein in the testis and/or alternative splicing. In addition, SP-10 peptides of 25-18 kDa were first detected in extracts of caput epididymal sperm and probably resulted from the proteolytic processing of the 45- and 32-26-kDa SP-10 peptides in the initial segment or caput epididymidis. Also, no additional SP-10 bands were detected in extracts of cauda epididymal, ejaculated, or capacitated sperm, suggesting that no further processing of the 32-18-kDa SP-10 peptides occurred during epididymal transit, ejaculation, and capacitation. Electron microscopic immunocytochemical observations of epididymal, ejaculated, and capacitated sperm revealed that colloidal gold labeling of SP-10 was most abundant within the principal segment and posterior bulb of the equatorial segment of the acrosome, while the colloidal gold labeling of SP-10 was sparse in the anterior equatorial segment of the acrosome. After a follicular fluid-induced acrosome reaction, SP-10 was detected on the inner acrosomal membrane in the equatorial segment and was associated with hybrid vesicles. This localization after the acrosome reaction is consistent with the hypothesis that SP-10 may be involved in sperm-zona binding or penetration.

Acrosome↗

Absence of electron transport (Rho 0 state) restores growth of a manganese-superoxide dismutase-deficient Saccharomyces cerevisiae in hyperoxia. Evidence for electron transport as a major source of superoxide generation in vivo.

To address the possibility that electron transport is a biologically significant source of superoxide anion (O2-.) during exposure to hyperoxia in vivo, we constructed Saccharomyces cerevisiae strains with selective disruptions in the gene encoding the mitochondrial manganese-containing superoxide dismutase (Mn-SOD) and/or genes encoding proteins critical for complexes in electron transport. We hypothesized that complete absence of electron transport would restore growth in hyperoxia to a Mn-SOD-deficient yeast. We found that yeast deficient in Mn-SOD activity failed to grow normally in hyperoxia (95% O2, 5% CO2). In contrast, Mn-SOD-deficient yeast with complete absence of electron transport (the Rho 0 state) grew normally in hyperoxia. By comparison, Mn-SOD-deficient yeast which were deficient only in cytochrome-c-oxidase, the terminal step in electron transport, had only partially restored growth in hyperoxia. Our results indicate that electron transport is a major source of O2-. in vivo, and that the principal site of this O2-. production is proximal to the cytochrome-c-oxidase complex.

Electron Transport↗

cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase.

We isolated cDNAs encoding xanthine dehydrogenase (XD; xanthine:NAD+ oxidoreductase, EC 1.1.1.204) from a human liver cDNA library. The complete nucleotide sequence of human XD was determined; the deduced amino acid sequence encoded a protein of 1336 amino acid residues of M(r) 147,782. Human XD possessed many of the signature sequences typical of XDs from flies and rodents, including an unusual cysteine distribution, a potential 2Fe/2S binding site, and a putative molybdopterin cofactor binding domain. Analysis of potential NAD binding sites suggested a simple hypothesis for the conversion of human XD into the oxygen metabolite forming xanthine oxidase (XO; xanthine:oxygen oxidoreductase, EC 1.1.3.22). Using a human XD complementary RNA hybridization probe, we found a 5100-base RNA in human liver by RNA blot-hybridization analysis. This RNA exhibited tissue-specific distribution that may be pertinent to XD- and XO-mediated oxygen radical injury in ischemia/reperfusion and inflammation. A second 4500-base RNA was detected in some tissues and may arise through differential transcription termination.

Amino Acid Sequence↗

Stage-specific detection of mRNA for the sperm antigen SP-10 in human testes.

SP-10 is a sperm-specific, intra-acrosomal protein that is considered to be a vaccine candidate for immunocontraception. In the present study, in situ hybridization with biotin and 35S labeled riboprobes was used to determine the pattern of SP-10 mRNA expression in human testes. Both methods demonstrated SP-10 mRNA primarily in round spermatids found in stages I, II, and III of the seminiferous cycle. Morphometric analysis of silver grains with the 35S-labeled probe showed less SP-10 mRNA in spermatids at stages IV, V, and VI than in previous stages, and rarely was label found in spermatogonia or spermatocytes. The expression of SP-10 mRNA first appeared at stage I coincident with the appearance of the protein, which was shown previously to persist in the acrosomal matrix throughout spermiogenesis. The decrease in SP-10 mRNA occurred when spermatids underwent polarization, nuclear condensation, and elongation. The appearance of SP-10 mRNA in round spermatids suggests that increases in SP-10 transcription or SP-10 mRNA stability or both occur as spermatids develop from the Golgi phase to the cap phase. The subsequent decline of SP-10 mRNA, despite the persistence of the SP-10 protein in all spermatids, suggests that a decrease in SP-10 transcription or an increase in mRNA degradation occurs when spermatids elongate.

Acrosome↗

Cloning and sequencing of baboon and cynomolgus monkey intra-acrosomal protein SP-10: homology with human SP-10 and a mouse sperm antigen (MSA-63).

In this study, cDNAs encoding the intraacrosomal protein SP-10 were cloned and sequenced from baboon (Papio papio) and macaque (Macaca fascicularis) testis libraries and the sequence compared to that of human SP-10. Two alternatively spliced SP-10 cDNAs were obtained from both baboon and macaque testis libraries. The two cDNAs in each species contained open reading frames encoding proteins of exactly 285 and 251 amino acids. A 98% homology between baboon and macaque SP-10 was found at the protein and DNA levels. An 85% and 89% homology between baboon and macaque SP-10 and human SP-10 was present at the protein and DNA level, respectively. A mouse intraacrosomal protein, MSA-63, considered to be an SP-10 homologue, exhibited an overall 53% homology to nonhuman primate SP-10 and a 60% homology to human SP-10 at the protein level. Polymerase chain reaction analysis of testis mRNA confirmed the existence of two alternatively spliced SP-10 mRNAs in both nonhuman primates. Primer extension analysis indicated a common major transcriptional start site in baboon, macaque, and human SP-10 67 nucleotides 5' to the ATG codon. The amino acid sequence data for nonhuman primate SP-10s suggest that antibodies generated by vaccinating baboons and macaques with human SP-10 will likely recognize nonhuman primate SP-10, supporting the testing of an SP-10 contraceptive vaccine based on human SP-10 in these nonhuman primate models.

Acrosome↗

Refinement of the localization of the gene for human intraacrosomal protein SP-10 (ACRV1) to the junction of bands q23-->q24 of chromosome 11 by nonisotopic in situ hybridization.

The human sperm antigen SP-10 is a testis-specific protein associated with the matrix of the acrosomal vesicle in developing spermatids and the acrosomal matrix and membranes of ejaculated sperm. A previous study, utilizing somatic cell hybrids, localized the gene for SP-10 to chromosome 11 and assigned the gene symbol ACRV1 (acrosomal vesicle protein-1). Although previous analysis of several somatic cell hybrids containing portions of chromosome 11 indicated that ACRV1 was in the p12-->q13 region, the present fluorescence in situ hybridization studies using cDNA, ribo, and genomic versions of probes for SP-10 coupled to analysis of an expanded series of somatic cell hybrids demonstrated the refined localization of ACRV1 to the junction of bands q23 and q24 of chromosome 11. A comparison of the three types of probes used for the in situ study demonstrated that while the genomic probe hybridized most efficiently, the riboprobe hybridized to the same location and was superior to the cDNA probe in mapping this single-copy gene. This report emphasizes the utility of riboprobes for chromosome localization of single-copy genes.

Acrosome↗

Arachidonic acid stimulates interleukin-6 release from rat peritoneal macrophages in vitro: evidence for a prostacyclin-dependent mechanism.

Interleukin-6 (IL-6) is a cytokine involved in the differentiation of B-cells to antibody secreting plasma cells, the activation of T-cells, and the stimulation of hepatocyte production of acute phase proteins. Because of the pro-inflammatory effects of this cytokine, we investigated the ability of the fatty acid arachidonic acid (AA) to regulate the release of IL-6 from rat resident peritoneal macrophages (M phi) in vitro. AA (0.5-16 microM) stimulated IL-6 release during a 4 h incubation period in a biphasic manner, with 4 microM AA generating a peak of IL-6 release (3-5-fold). AA (0.5-16 microM) also induced an increasing release of the AA metabolite thromboxane B2 (TXB2). The AA-induced release of IL-6 occurred within 1-2 h of incubation, whereas TXB2 concentrations were elevated within 5 min of AA treatment. The TX synthetase inhibitor CGS 12970 (4.0 microM and 40.0 microM) effectively blocked the generation of TXB2, but increased prostacyclin (PGI2) generation and potentiated the release of IL-6. In addition, PGI2, as well as the PGI2 agonists iloprost and cicaprost, stimulated IL-6 release from M phi by greater than 5-fold over vehicle-treated basal levels. These data suggest that PGI2 (but not TXA2) is involved in AA-induced IL-6 release from peritoneal M phi.

Animals↗

Cloning and characterization of the gene coding for the human acrosomal protein SP-10.

SP-10 is a human intra-acrosomal protein that is first detected in the developing acrosome of round spermatids and is observed associated with the acrosomal membranes and matrix of mature sperm. Recombinant SP-10 is currently being tested as a contraceptive vaccine immunogen on the basis of its tissue specificity as well as functional assays indicating that anti-SP-10 antisera inhibit sperm-egg interactions. In the present study, structural characterization of the human SP-10 gene was undertaken to investigate the expression of the gene and to identify possible functions of the SP-10 protein within the acrosome. Genomic blots indicate that SP-10 is encoded by a single-copy gene. Mapping and sequencing of the 8-kb SP-10 gene show that the SP-10 mRNA consists of exons of 119, 487, 113, and 390 bp with each exon coding for a distinct structural domain within the SP-10 protein. An in-frame alternatively spliced form of the SP-10 mRNA, identified during SP-10 cDNA characterization, employs the same 3' splice site as the 487-bp exon and a unique 5' splice site within the 487-bp exon. Previous comparisons of human, baboon, and macaque SP-10 cDNA sequences indicated that the baboon and macaque cDNAs contained 60 bp (20 aa) not present in the human SP-10 cDNA. Analysis of the human SP-10 genomic sequence suggests that a 60-bp deletion may have occurred during the evolution of the human SP-10 gene by homologous recombination.(ABSTRACT TRUNCATED AT 250 WORDS)

Acrosome↗

Assay for recombinant and native human intraacrosomal antigen SP-10.

PROBLEM: To develop a method to measure a recombinant sperm protein, SP-10, during scale up and purification for a contraceptive vaccine formulation. METHOD: A quantitative assay method for the human intraacrosomal protein SP-10 was developed utilizing the format of indirect capture enzyme-linked immunosorbent assay (ELISA). A SP-10 specific monoclonal antibody mAb, MHS-10, was used as the capture antibody. Two recognition reagents, a rabbit polyclonal anti-SP-10 antisera (pAb) and a biotin-labeled mAb, MHS-10, were used as the recognition antibodies, respectively. A SP-10 recombinant fusion protein consisting of 125 SP-10 amino acids linked to glutathione transferase was used as a working SP-10 standard. The coefficient of variance for the assay system using the rabbit pAb was in the range of 0.099 to 0.157, and for the assay system using the biotinylated mAb MHS-10 was in the range of 0.081 to 0.084. RESULTS: Employing biotinylated MHS-10 as the recognition antibody, it was found that the native SP-10 molecule had more than one MHS-10 epitope. The concentration of SP-10 in a pool of human sperm extracts was found to be approximately 1% of the total proteins, assayed by both of the recognition antibody systems. CONCLUSIONS: The assay system described is useful to monitor the yield of recombinant SP-10 during scale-up production of the SP-10 vaccine.

Acrosome↗

Pressure-independent baroreflex resetting produced by chronic infusion of angiotensin II in rabbits.

The purpose of this study was to test the hypothesis that chronic infusion of angiotensin II (ANG II) in rabbits shifts or resets baroreflex control of heart rate to a higher pressure level via a mechanism that is independent of the hypertension that is produced. The baroreflex relationship between arterial pressure and heart rate was assessed by first infusing progressively increasing doses of nitroprusside (3, 6, 12, 24, and 48 micrograms.kg-1 x min-1) to lower pressure and then increasing doses of phenylephrine (0.5, 1, 2, 4, and 8 micrograms.kg-1 x min-1) to raise pressure. Two weeks of intravenous ANG II infusion (20 ng.kg-1 x min-1) increased plasma ANG II levels from 9 +/- 1 to 146 +/- 24 pg/ml (P < 0.05), increased arterial pressure from 62 +/- 2 to 95 +/- 2 mmHg (P < 0.05), and transiently increased heart rate. The baroreflex was shifted to a higher pressure level after 30 min and 1, 3, 7, 9, and 14 days of ANG II infusion. Thirty minutes after the ANG II infusion on days 1, 7, and 14 was stopped, arterial pressure decreased, and the baroreflex shifted back to control, indicating that ANG II was required for the resetting that was produced. However, when the ANG II infusion was continued and arterial pressure was instead reduced for 30 min by infusing nitroprusside on days 3 and 9, the baroreflex relationship between arterial pressure and heart rate remained positioned at a higher pressure level.(ABSTRACT TRUNCATED AT 250 WORDS)

Angiotensin II↗

Lipopolysaccharide induces interleukin-6 release from rat peritoneal macrophages in vitro: evidence for a novel mechanism.

Interleukin-6 (IL-6) is a cytokine involved in the terminal differentiation of B-cells, T-cell activation, and secretion of hepatic acute phase proteins. The production of IL-6 is regulated by many factors, including IL-1 and lipopolysaccharide (LPS). Because IL-6 may be an important contributor to the effects of LPS in inflammation and septic shock, we investigated the ability of LPS to induce IL-6 release from peritoneal macrophages (m phi) in vitro. M phi were isolated from male Long-Evans rats, and cultured in 96-well tissue culture plates at 1 x 10(5) cells/well in serum-free RPMI-1640 medium. Following a 2-hr attachment period, the cells were rinsed twice to remove the nonadherent cells. LPS (0.006-100 ng/ml) stimulated IL-6 release by six- to 12-fold during a 4 hr incubation. In contrast, IL-1 beta (0.006-100 ng/ml) had no effect. Because cyclooxygenase metabolites of arachidonic acid are increased by LPS, we determined the effects of indomethacin (a cyclooxygenase inhibitor) and CGS8515 (a 5-lipoxygenase inhibitor) on LPS-induced IL-6 release. Neither indomethacin (10 microM) nor CGS8515 (2.5 microM) had any effect on basal or LPS-induced IL-6 release. Very low concentrations of LPS (0.01-1,000 pg/ml) stimulated IL-6 by two- to threefold. Pertussis toxin (10 ng/ml), which inactivates Gi protein, had no effect on LPS-induced IL-6 release from mø. Thromboxane B2 (TXB2) concentrations were also elevated with as little as 0.1 pg/ml LPS; however, pertussis toxin inhibited LPS-stimulated TXB2 release.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

Purification and microsequencing of the intra-acrosomal protein SP-10. Evidence that SP-10 heterogeneity results from endoproteolytic processes.

The human sperm antigen SP-10 has been shown to be a testis-specific, intra-acrosomal protein that is associated with the membranes and matrix of the acrosomal vesicle. Sperm extracts, analyzed on Western blots with a monoclonal antibody to SP-10, have shown heterogeneity of SP-10 peptides ranging from 17.5-34 kDa. Although the entire SP-10 amino acid sequence of 265 amino acids (28.3 kDa) has been deduced from sequencing SP-10 cDNAs, the nature of multiple SP-10 peptide bands is incompletely understood. In this study, we developed a three-step purification method for SP-10 peptides using monoclonal antibody affinity chromatography, reverse-phase HPLC, and preparative gel electrophoresis. Eight SP-10 peptides separated by this protocol and sequenced using Edman degradation showed amino termini that corresponded to regions on the deduced SP-10 amino acid sequence. Peptides with progressively lower apparent mass aligned further toward the carboxy terminus. On the basis of putative cleavage sites on the SP-10 sequence, endoproteases that act at five different peptide bonds are predicted to cleave SP-10: these hydrolyze following arginine (a trypsin-like protease, possibly acrosin), and following serine, proline, glycine, and glutamic acid (previously undescribed intra-acrosomal protease specificities). The present studies 1) provide a purification method for SP-10 peptides; 2) confirm that the SP-10 cDNAs previously sequenced encode authentic SP-10; and 3) yield indirect evidence that endoproteases act to contribute to SP-10 heterogeneity.

Acrosome↗

Cloning, characterization, and nucleotide sequence of a gene encoding Microbispora bispora BglB, a thermostable beta-glucosidase expressed in Escherichia coli.

Genomic DNA fragments encoding beta-glucosidase activities of the thermophilic actinomycete Microbispora bispora were cloned into Escherichia coli. Transformants expressing beta-glucosidase activity were selected by their ability to hydrolyze the fluorogenic substrate 4-methylumbelliferyl-beta-D-glucoside. Two genes encoding beta-glucosidase activity were isolated and distinguished by restriction analysis, Southern hybridization, and the substrate specificities of the encoded enzymes. One gene, bglB, encoded a beta-glucosidase that was expressed intracellularly in E. coli. It exhibited a molecular mass of approximately 52,000 Da by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (PAGE) and 51,280 Da by nondenaturing gradient PAGE, a pI of 4.6, and temperature and pH optima of 60 degrees C and 6.2, respectively. Cloned BglB showed greater activity against cellobiose than against aryl-beta-D-glucosides and was thermostable, retaining about 70% of its activity after 48 h at 60 degrees C. BglB activity is activated two- to threefold in the presence of 2 to 5% (0.1 to 0.3 M) glucose. The DNA sequence of the 2.2-kb insert carrying bglB has been determined. An open reading frame which codes for a protein of 473 amino acids with a predicted molecular mass of 52,227 Da showed significant homology (40 to 47% identity) with beta-glucosidases from glycosal hydrolase family 1.

Actinomycetales↗

Children with cerebral venous thrombosis diagnosed with magnetic resonance imaging and magnetic resonance angiography.

From 1985 to 1991, 13 children were diagnosed at the University of Illinois College of Medicine at Peoria, Saint Francis Medical Center, with cerebral venous thrombosis (CVT) by magnetic resonance imaging scan. Ages ranged from newborn to 5 years. Six children were premature neonates, five were term neonates and two were 5 years old. In the premature neonates, thrombosis was usually associated with other problems. All the term neonates had seizures. In all neonates, thrombosis resolved without any specific treatment. In the two older children, one presented with pseudotumor cerebri and one with coma. These children required neurosurgical intervention. Follow-up magnetic resonance imaging scans were obtained in 9 of 13 children and showed thrombus resolution in each case. Three children were studied in the acute and convalescent stages by magnetic resonance angiography using time-of-flight techniques. Each follow-up magnetic resonance angiogram showed improvement in venous flow consistent with their clinical course and other imaging studies. We conclude that 1) CVT in children encompasses a range of clinical conditions which may or may not require neurosurgical intervention; 2) magnetic resonance imaging is superior to other modalities for the diagnosis of CVT; and 3) magnetic resonance angiography is an alternative means to monitor the evolution of CVT and efficacy of therapeutic intervention.

Cerebral Angiography↗