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Biomedical subjects

J J Rydel

Publications and source records attributed to J J Rydel.

6 recordsLinked to original sources
PubMed1998

An 18-year-old man with Goodpasture's syndrome and ANCA-negative central nervous system vasculitis.

An 18-year-old man with Goodpasture's syndrome developed a recurrent seizure disorder refractory to anticonvulsant therapy spanning a full course of plasmapheresis and cytotoxic therapy. Status epilepticus developed during a taper of cytotoxic agents, with magnetic resonance imaging (MRI) findings consistent with multiple lacunar infarcts. Although the diagnosis of vasculitis was considered, anti-neutrophilic cytoplasmic antibody serology was consistently negative. A meningeal biopsy showed vasculitis, which was successfully treated with the reintroduction of high-dose steroids and cytotoxic agents in conjunction with anticonvulsants. Nearly 1 year later, with Goodpasture's disease in remission, he received a living-related renal transplant from his mother. He is currently leading a normal lifestyle. From an extensive review of the literature, this is the first case of anti-neutrophil cytoplasmic antibody-negative central nervous system (CNS) vasculitis in a patient with Goodpasture's syndrome.

Adolescent↗
PubMed1995

Focal segmental glomerular sclerosis in adults: presentation, course, and response to treatment.

The authors performed a retrospective clinicopathologic study in 81 patients with primary focal segmental glomerular sclerosis (FSGS) to determine whether they could identify clinical or histologic features at presentation that could be predictive of outcome and response to therapy. Males constituted 58% of patients, and 53% were black. At biopsy the patients were 40 +/- 17 years old; 74% were nephrotic, and renal insufficiency was present in 62%. The average time from presentation to biopsy was 16 months, and the average total follow-up was 62 months. Nephrotic patients had a significantly poorer prognosis as compared with nonnephrotic patients (5- and 10-year survivals of 76% and 57% v 92% and 92%; P < 0.05). A multivariate analysis was done on histologic and clinical features at biopsy, assessing for risk factors leading to end-stage renal disease, showing only the serum creatinine and the degree of interstitial fibrosis to have a significant correlation. Thirty nephrotic patients received prednisone, with a treatment time of 5.5 +/- 4 months and a total dose of 5.9 +/- 2.9 g per course of treatment. Fifteen of these patients (50%) achieved a remission by 3.7 +/- 2 months (10 complete remission and 5 partial remissions), with all patients responding within 9 months. Only two patients had spontaneous remissions (both partial). The 5- and 10-year survival for patients in remission were both 100% as compared with 66% and 41% (P < 0.01), respectively, for nephrotic patients not in remission. No clinical feature at presentation of biopsy was predictive of response to therapy when a multivariate analysis was performed.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗
PubMed1995

Renal vasculitis associated with ciprofloxacin.

We report two patients treated with ciprofloxacin who presented with acute renal failure. On renal biopsy, a necrotizing vasculitis was identified in addition to acute interstitial nephritis. Improvement in renal function resulted with the discontinuation of the antibiotic and the institution of immunosuppressive therapy.

Aged↗
PubMed1989

Sequential localization of antibody to multiple regions of the glomerular capillary wall in passive Heymann nephritis.

Passive Heymann nephritis was produced in rats by injection of the multispecific anti-Fx1A antibody. At time points 1 hour, 1 day, 2 days, 3 days, and 4 days groups of rats were sacrificed and their kidneys fixed by retrograde perfusion with paraformaldehyde lysine periodate. The antibody was visualized by direct immunofluorescence and by 125I-Protein-A electron microscopic autoradiography. Localization of the antibody in the lamina rara interna, lamina densa, lamina rara externa and the glomerular epithelial cell was determined by electron microscopic autoradiography according to the method of Saltpeter, Fertuck, and Saltpeter (Saltpeter MM, Fertuck MC, Saltpeter EE: J Cell Biol 72:161, 1977). At least 100 grains/kidney were analyzed. At one hour the antibody was localized in a linear, discontinuous pattern by immunofluorescent microscopy. Ultrastructurally, the antibody was present in all regions of the capillary wall although predominantly in the lamina rara interna. At later time points the immunofluorescence staining changed to the typical granular pattern with majority of the grains localizing to the lamina rara externa and the cell body of the glomerular epithelial cell. The importance of these observations is several-fold. (a) It suggests the involvement of multiple antigens in the pathogenesis of Heymann nephritis. (b) The initial reaction to the lamina rara interna may be potentiating the eventual formation of deposits in the lamina rara externa by locally permeabilizing the capillary wall and allowing passage to other antibodies. (c) The immune complexes formed at the various sites in the capillary may be getting shed and trapped in the lamina rara externa resulting in coalescence and genesis of the nephritogenic electron-dense deposits.

Animals↗
PubMed1984

Overexpression and sequence of the Escherichia coli cheY gene and biochemical activities of the CheY protein.

We overexpressed the CheY protein by fusing the cheY gene to the tryptophan promoter from Serratia marcescens. Expression of the trp promoter-cheY fusion and subsequent purification of the protein resulted in the isolation of up to 20 mg of homogeneously pure CheY protein from 100 mg of the cytoplasmic supernatant fraction. Purification of the CheY protein was accomplished by exploiting the affinity of CheY protein to cibacron blue dye and molecular sieve chromatography. Preliminary biochemical characterization of the pure CheY protein revealed specific interactions with S-adenosylmethionine and cibacron blue dye. Additional kinetic analysis showed that CheY protein inhibits EcoRI methyltransferase. The amino acid composition of the CheY protein predicted by the DNA sequence of the cheY gene and the amino acid analysis of the CheY protein were in agreement, confirming the authenticity of the purified CheY protein.

Amino Acid Sequence↗