scholarly journals Plasma Porphyrins in the Porphyrias

1999 ◽  
Vol 45 (7) ◽  
pp. 1070-1076 ◽  
Author(s):  
J Thomas Hindmarsh ◽  
Linda Oliveras ◽  
Donald C Greenway
Keyword(s):  
Renal Failure ◽  
Healthy Subjects ◽  
Porphyria Cutanea Tarda ◽  
Plasma Concentrations ◽  
Acute Intermittent Porphyria ◽  
Fluorometric Detection ◽  
Erythropoietic Protoporphyria ◽  
Clinical Sensitivity ◽  
Hereditary Coproporphyria ◽  
Coproporphyrin I

Abstract Background: As an aid in the diagnosis and management of porphyria we have developed a method to fractionate and quantify plasma porphyrins and have evaluated its use in various porphyrias. Methods: We used HPLC with fluorometric detection to measure plasma concentrations of uroporphyrin I and III, heptacarboxyl III, hexacarboxyl III, pentacarboxyl III, and coproporphyrin I and III. We studied 245 healthy subjects, 32 patients with classical porphyria cutanea tarda (PCT), 12 patients with PCT of renal failure, 13 patients with renal failure, 8 patients with pseudoporphyria of renal failure, 3 patients with acute intermittent porphyria, 5 patients with variegate porphyria, 5 patients with hereditary coproporphyria, and 4 patients with erythropoietic protoporphyria. Results: Between-run CVs were 5.4–13%. The recoveries of porphyrins added to plasma were 71–114% except for protoporphyrin, which could not be reliably measured with this technique. Plasma porphyrin patterns clearly identified PCT, and its clinical sensitivity equaled that of urine porphyrin fractionation. The patterns also allowed differentiation of PCT of renal failure from pseudoporphyria of renal failure. Conclusions: The assay of plasma porphyrins identifies patients with PCT and appears particularly useful for differentiating PCT of renal failure from pseudoporphyria of renal failure.

Amounts of Faecal Porphyrin-Peptide Conjugates in the Porphyrias

1972 ◽  
Vol 43 (2) ◽  
pp. 299-302 ◽  
Author(s):  
M. R. Moore ◽  
G. G. Thompson ◽  
A. Goldberg
Keyword(s):  
Porphyria Cutanea Tarda ◽  
Acute Intermittent Porphyria ◽  
Normal Subjects ◽  
Erythropoietic Protoporphyria ◽  
Peptide Conjugates ◽  
Peptide Complex ◽  
Variegate Porphyria ◽  
Hereditary Coproporphyria ◽  
Different Types

1. The levels of ‘X-porphyrin’, a porphyrin-peptide complex, have been studied in the faeces of patients with different types of porphyria, as well as in fifty normal subjects. 2. These levels have been shown to be significantly elevated in untreated porphyria cutanea tarda and in variegate porphyria. 3. Lesser elevations were seen in acute intermittent porphyria and hereditary coproporphyria. There was no elevation in erythropoietic protoporphyria.

Metabolic Disease

2017 ◽  
Author(s):  
Virginia P. Sybert
Keyword(s):  
Metabolic Disorders ◽  
Porphyria Cutanea Tarda ◽  
Hunter Syndrome ◽  
Acrodermatitis Enteropathica ◽  
Erythropoietic Protoporphyria ◽  
Prolidase Deficiency ◽  
Treatment Mode ◽  
Congenital Erythropoietic Porphyria ◽  
Hereditary Coproporphyria

Chapter 11 covers Porphyrias (Congenital Erythropoietic Porphyria, Erythropoietic Protoporphyria, Hereditary Coproporphyria, Porphyria Cutanea Tarda, and Variegate Porphyria), Mucopolysaccharidoses (Hunter Syndrome), and Other Metabolic Disorders (Acrodermatitis Enteropathica, Alkaptonuria, Biotinidase Deficiency, Familial Cutaneous Amyloidosis, and Prolidase Deficiency). Each condition is discussed in detail, including dermatologic features, associated anomalies, histopathology, basic defect, treatment, mode of inheritance, prenatal diagnosis, and differential diagnosis.

Metabolic Disease

2012 ◽  
Author(s):  
Virginia P. Sybert
Keyword(s):  
Metabolic Disease ◽  
Metabolic Disorders ◽  
Porphyria Cutanea Tarda ◽  
Hunter Syndrome ◽  
Biotinidase Deficiency ◽  
Acrodermatitis Enteropathica ◽  
Erythropoietic Protoporphyria ◽  
Prolidase Deficiency ◽  
Congenital Erythropoietic Porphyria ◽  
Hereditary Coproporphyria

Porphyrias – Congenital Erythropoietic Porphyria – Erythropoietic Protoporphyria – Hereditary Coproporphyria – Porphyria Cutanea Tarda – Variegate Porphyria – Mucopolysaccharidoses – Hunter Syndrome – Other Metabolic Disorders – Acrodermatitis Enteropathica – Alkaptonuria – Biotinidase Deficiency – Familial Cutaneous Amyloidosis – Prolidase Deficiency

The Porphyrias

2016 ◽  
Author(s):  
Karl E Anderson ◽  
Attallah Kappas
Keyword(s):  
Biosynthetic Pathway ◽  
Aminolevulinic Acid ◽  
Clinical Symptoms ◽  
Porphyria Cutanea Tarda ◽  
Acute Intermittent Porphyria ◽  
Genetic Traits ◽  
Molecular Defects ◽  
Clinical Presentations ◽  
Congenital Erythropoietic Porphyria ◽  
Hereditary Coproporphyria

The porphyrias are uncommon disorders caused by deficiencies in the activities of enzymes of the heme biosynthetic pathway. The enzymatic defects that cause porphyrias are inherited, with the exception of porphyria cutanea tarda, which is primarily acquired. In all porphyrias, there is significant interplay between genetic traits and acquired or environmental factors in the expression of clinical symptoms. This review discusses the classification, pathophysiology, and clinical presentations of the porphyrias. These include those associated with neurovisceral attacks (acute intermittent porphyria, variegate porphyria, hereditary coproporphyria, and δ-aminolevulinic acid dehydratase [alad] deficiency porphyria) and the porphyrias associated with cutaneous photosensitivity (porphyria cutanea tarda, hepatoerythropoietic porphyria, erythropoietic protoporphyria, and congenital erythropoietic porphyria). Specific emphasis on the epidemiology, molecular defects and pathophysiology, clinical features, diagnosis, and treatment are discussed for each of these disorders. A table lists the safe and unsafe drugs for patients with porphyrias. Figures illustrate the genetic pathways of the disorders and the activities of enzymes of the heme biosynthetic pathway. This review contains 2 highly rendered figures, 1 table, and 96 references.

scholarly journals ABCB6 Polymorphisms are not Overly Represented in Patients with Porphyria

2021 ◽  
Author(s):  
Colin P Farrell ◽  
Gaël Nicolas ◽  
Robert J. Desnick ◽  
Charles J. Parker ◽  
Jerome Lamoril ◽  
...  
Keyword(s):  
Biosynthetic Pathway ◽  
Genetic Factors ◽  
Autosomal Dominant ◽  
Clinical Phenotype ◽  
Acute Intermittent Porphyria ◽  
Mendelian Inheritance ◽  
Erythropoietic Protoporphyria ◽  
Transporter Protein ◽  
Hereditary Coproporphyria ◽  
Knockout Animals

The Mendelian inheritance pattern of acute intermittent porphyria, hereditary coproporphyria, and variegate porphyria is autosomal dominant, but the clinical phenotype is heterogeneous. Within the general population, penetrance is low, but among first-degree relatives of a symptomatic proband, penetrance is higher. These observations suggest that genetic factors, in addition to mutation of the specific enzyme of the biosynthetic pathway of heme, contribute to the clinical phenotype. Recent studies by others suggested that the genotype of the transporter protein ABCB6 contribute to the porphyria phenotype. Identifying the molecule(s) that are transported by ABCB6 has been problematic and has led to uncertainty with respect to how or if variants/mutants contribute to phenotypic heterogeneity. Knockout mouse models of Abcb6 have not provided a direction for investigation as homozygous knockout animals do not have a discrete phenotype. To address the proposed link between ABC6 genotype and porphyria phenotype, a large cohort of patients with acute hepatic porphyria and erythropoietic protoporphyria was analyzed. Our studies showed that ABCB6 genotype did not correlate with disease severity. Therefore, genotyping of ABCB6 in patients with acute hepatic porphyria and erythropoietic protoporphyria is not warranted.

Plasma D Dimer: A Useful Marker of Fibrin Breakdown in Renal Failure

1989 ◽  
Vol 61 (03) ◽  
pp. 522-525 ◽  
Author(s):  
M P Gordge ◽  
R W Faint ◽  
P B Rylance ◽  
H Ireland ◽  
D A Lane ◽  
...  
Keyword(s):  
Renal Failure ◽  
Renal Function ◽  
Acute Renal Failure ◽  
Monoclonal Antibodies ◽  
Diabetic Nephropathy ◽  
Renal Disease ◽  
Plasma Concentrations ◽  
Significant Negative Correlation ◽  
Healthy Controls ◽  
D Dimer

SummaryD dimer and other large fragments produced during the breakdown of crosslinked fibrin may be measured by enzyme immunoassay using monoclonal antibodies. In 91 patients with renal disease and varying degrees of renal dysfunction, plasma D dimer showed no correlation with renal function, whereas FgE antigen, a fibrinogen derivative which is known to be cleared in part by the kidney, showed a significant negative correlation with creatinine clearance. Plasma concentrations of D dimer were, however, increased in patients with chronic renal failure (244 ± 3l ng/ml) (mean ± SEM) and diabetic nephropathy (308 ± 74 ng/ml), when compared with healthy controls (96 ± 13 ng/ml), and grossly elevated in patients with acute renal failure (2,451 ± 1,007 ng/ml). The results indicate an increase in fibrin formation and lysis, and not simply reduced elimination of D dimer by the kidneys, and are further evidence of activated coagulation in renal disease. D dimer appears to be a useful marker of fibrin breakdown in renal failure.

scholarly journals The Effect of Bilateral Nephrectomy on Renalase and Catecholamines in Hemodialysis Patients

2021 ◽  
Vol 18 (12) ◽  
pp. 6282
Author(s):  
Magda Wiśniewska ◽  
Natalia Serwin ◽  
Violetta Dziedziejko ◽  
Małgorzata Marchelek-Myśliwiec ◽  
Barbara Dołęgowska ◽  
...  
Keyword(s):  
Healthy Subjects ◽  
Plasma Concentrations ◽  
Serum Levels ◽  
Hemodialysis Patients ◽  
Pressure Regulation ◽  
Serum Concentrations ◽  
Monoamine Oxidase Activity ◽  
Normal Kidney ◽  
Bilateral Nephrectomy ◽  
Arterial Blood

Background/Aims: Renalase is an enzyme with monoamine oxidase activity that metabolizes catecholamines; therefore, it has a significant influence on arterial blood pressure regulation and the development of cardiovascular diseases. Renalase is mainly produced in the kidneys. Nephrectomy and hemodialysis (HD) may alter the production and metabolism of renalase. The aim of this study was to examine the effect of bilateral nephrectomy on renalase levels in the serum and erythrocytes of hemodialysis patients. Methods: This study included 27 hemodialysis patients post-bilateral nephrectomy, 46 hemodialysis patients without nephrectomy but with chronic kidney disease and anuria and 30 healthy subjects with normal kidney function. Renalase levels in the serum and erythrocytes were measured using an ELISA kit. Results: Serum concentrations of renalase were significantly higher in post-bilateral nephrectomy patients when compared with those of control subjects (101.1 ± 65.5 vs. 19.6 ± 5.0; p < 0.01). Additionally, renalase concentrations, calculated per gram of hemoglobin, were significantly higher in patients after bilateral nephrectomy in comparison with those of healthy subjects (994.9 ± 345.5 vs. 697.6 ± 273.4, p = 0.015). There were no statistically significant differences in plasma concentrations of noradrenaline or adrenaline. In contrast, the concentration of dopamine was significantly lower in post-nephrectomy patients when compared with those of healthy subjects (116.8 ± 147.7 vs. 440.9 ± 343.2, p < 0.01). Conclusions: Increased serum levels of renalase in post-bilateral nephrectomy hemodialysis patients are likely related to production in extra-renal organs as a result of changes in the cardiovascular system and hypertension.

Dyslipidemia of chronic renal failure: the nature, mechanisms, and potential consequences

2006 ◽  
Vol 290 (2) ◽  
pp. F262-F272 ◽  
Author(s):  
N. D. Vaziri
Keyword(s):  
Renal Failure ◽  
Chronic Renal Failure ◽  
Hepatic Lipase ◽  
Low Density Lipoprotein ◽  
Plasma Concentrations ◽  
Cholesterol Acyltransferase ◽  
Lipoprotein Metabolism ◽  
Density Lipoprotein ◽  
Triglyceride Rich Lipoprotein ◽  
Density Lipoprotein Receptor

Chronic renal failure (CRF) results in profound lipid disorders, which stem largely from dysregulation of high-density lipoprotein (HDL) and triglyceride-rich lipoprotein metabolism. Specifically, maturation of HDL is impaired and its composition is altered in CRF. In addition, clearance of triglyceride-rich lipoproteins and their atherogenic remnants is impaired, their composition is altered, and their plasma concentrations are elevated in CRF. Impaired maturation of HDL in CRF is primarily due to downregulation of lecithin-cholesterol acyltransferase (LCAT) and, to a lesser extent, increased plasma cholesteryl ester transfer protein (CETP). Triglyceride enrichment of HDL in CRF is primarily due to hepatic lipase deficiency and elevated CETP activity. The CRF-induced hypertriglyceridemia, abnormal composition, and impaired clearance of triglyceride-rich lipoproteins and their remnants are primarily due to downregulation of lipoprotein lipase, hepatic lipase, and the very-low-density lipoprotein receptor, as well as, upregulation of hepatic acyl-CoA cholesterol acyltransferase (ACAT). In addition, impaired HDL metabolism contributes to the disturbances of triglyceride-rich lipoprotein metabolism. These abnormalities are compounded by downregulation of apolipoproteins apoA-I, apoA-II, and apoC-II in CRF. Together, these abnormalities may contribute to the risk of arteriosclerotic cardiovascular disease and may adversely affect progression of renal disease and energy metabolism in CRF.

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