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At least 19 recordsLinked to original sources
PubMed1983

Light-induced release of protoporphyrin, but not of zinc protoporphyrin, from erythrocytes in a patient with greatly elevated erythrocyte protoporphyrin.

A patient with greatly increased erythrocyte protoporphyrin, but normal porphyrins in urine and feces, is described. The patient later developed a malignant lymphoma, and the reason why she accumulated protoporphyrin in her erythrocytes is not known. The protoporphyrin in the erythrocytes consisted of two types of protoporphyrin, free protoporphyrin (30%) and zinc protoporphyrin (70%). Upon irradiation of erythrocytes in the absence of albumin, protoporphyrin and zinc protoporphyrin, which were both bound to hemoglobin, were released. In contrast, when the irradiation was carried out in the presence of albumin, the photohemolysis was negligible, and there was release of free protoporphyrin, but not of zinc protoporphyrin, from the erythrocytes. In vivo albumin is present in the plasma and the results may help to explain why patients with erythropoietic protoporphyria (erythrocytes containing free protoporphyrin) are photosensitive, whereas patients with lead intoxication and iron deficiency (erythrocytes containing zinc protoporphyrin) are not.

Aged↗
PubMed1996

Zinc protoporphyrin, zinc ion, and protoporphyrin reduce focal cerebral ischemia.

BACKGROUND AND PURPOSE: Zinc protoporphyrin pretreatment protects against temporary focal ischemic brain injury in rats. However, it is not known whether the zinc or the protoporphyrin portion of zinc protoporphyrin has effects on focal cerebral ischemia. Hence, all three agents were compared with regard to infarct size and edema in a rat model of middle cerebral artery occlusion. METHODS: Four groups of adult male Sprague-Dawley rats were subjected to 2 hours of temporary middle cerebral artery occlusion followed by 22 hours of reperfusion. Each group was pretreated 30 minutes before middle cerebral artery occlusion with 0.9% NaCl, and then three groups were given equimolar doses of zinc protoporphyrin, zinc chloride, or protoporphyrin, respectively. Regional cerebral blood flow in the ischemic cortex was monitored with a laser Doppler flowmeter. Cerebral infarct size, brain water content, and ion content were measured 24 hours after the onset of occlusion. RESULTS: Regional cerebral blood flow during middle cerebral artery occlusion was approximately 9.2% to 13% of baseline in all four groups. Brain water content in the infarcted zone after temporary focal ischemia in control, zinc protoporphyrin, zinc chloride, and protoporphyrin groups was 85.7%, 80.6%, 85.6%, and 81.4%, respectively. Brain sodium content in the same areas in all four groups paralleled the water content. Infarct size in the controls and groups treated with zinc protoporphyrin, zinc, and protoporphyrin was 25.6%, 7.2%, 7.6%, and 7.2%, respectively. Compared with the control group, the infarct volume in all three treated groups was significantly reduced (P < .05). CONCLUSIONS: The present results indicate that zinc protoporphyrin, but also zinc and protoporphyrin, contribute to brain-protective effects when administered early in a temporary focal ischemia model. Zinc chloride reduced infarct size but not edema formation when compared with zinc protoporphyrin and protoporphyrin. Zinc ion in vivo has brain-protective effects, confirming in vitro studies previously reported by some but contrary to reports of others. Blood versus brain neuropil and cell body concentrations of zinc ion need to be studied in the future to define the precise role of zinc in the complex mechanisms involved in brain ischemia.

Animals↗
PubMed1981

Binding of protoporphyrin to melanin and oxidation-reduction properties of melanin-protoporphyrin complex.

The binding of protoporphyrin to melanin and the effect of the binding of protoporphyrin to melanin on the oxidation-reduction properties of melanin were studied. Various concentrations of protoporphyrin were incubated with melanin suspensions. The amounts of protoporphyrin remaining in the supernatant after sedimentation of the melanin were determined. The amount of bound protoporphyrin was determined by extraction with 3 M HCl. The results showed that when the initial concentration of protoporphyrin was varied, the amounts of protoporphyrin bound were in accordance with Langmuir's isotherm. From these results it was calculated that at infinite concentration of protoporphyrin 7.62 +/- 0.38 microgram protoporphyrin would be bound to 1 mg melanin. The activity to catalyze the coupled oxidation of NADH and reduction of ferricyanide was less in the case of the melanin-protoporphyrin complex than the free melanin. It is suggested that the binding of a naturally occurring photosensitizer such as protoporphyrin to melanin may have significant biological effects viz (i) photosensitivity due to protoporphyrin, (ii) the chemical reactivity of melanin in internal organs, and (iii) protective action of melanin in skin against ultraviolet radiation.

Ferricyanides↗
PubMed1981

Simultaneous quantitation of zinc protoporphyrin and free protoporphyrin in erythrocytes by acetone extraction.

Erythrocyte protoporphyrin content is increased in several human and veterinary disorders in which heme synthesis is disrupted. The nature of the defect determines whether zinc protoporphyrin, unchelated (free) protoporphyrin, or both are present in the erythrocytes. Extraction of the protoporphyrin into acetone/water (80/20 by vol) is a simple, rapid technique by which each protoporphyrin species is delivered into solution without removing zinc from zinc protoporphyrin. The ratio of zinc protoporphyrin to total protoporphyrin concentration correlated significantly with the ratio of fluorescence emission intensities at the zinc protoporphyrin peak and at an isosbestic point. This concentration ratio may be used with a quantitative measure of total erythrocyte protoporphyrin to define the absolute zinc protoporphyrin and free protoporphyrin content of erythrocytes.

Acetone↗
PubMed1979

Chloroplast Biogenesis: XXIV. Intrachloroplastic Localization of the Biosynthesis and Accumulation of Protoporphyrin IX, Magnesium-Protoporphyrin Monoester, and Longer Wavelength Metalloporphyrins during Greening.

The intraplastidic localization of the endogenous metabolic pools from protoporphyrin to protochlorophyll was determined in Cucumis sativus. The endogenous protoporphyrin, Mg-protoporphyrin monoester + longer wavelength metalloporphyrins, protochlorophyllide and protochlorophyllide ester were membrane-bound. Protoporphyrin was synthesized in the stroma and subsequently became associated with the membranes. The membrane-associated protoporphyrin was then converted into Mg-protoporphyrin monoester + longer wavelength metalloporphyrins by membrane-bound enzymes. Although lysed plastids were capable of converting exogenous delta-aminolevulinic acid to protochlorophyllide, the net synthesis of protochlorophyllide from exogenous delta-aminolevulinic acid was lost upon segregating the lysed plastids into stromal and membrane fractions and then recombining the stromal and membrane fraction prior to incubation. The segregated membrane fraction was still capable of converting protoporphyrin into Mg-protoporphyrin monoester + longer wavelength metalloporphyrins in the presence or absence of the stromal fraction. These results indicated that although the reactions from protoporphyrin to Mg-protoporphyrin monoester and longer wavelength metalloporphyrins could survive a considerable degree of plastid disruption, the reactions from Mg-protoporphyrin monoester and longer wavelength metalloporphyrins to protochlorophyllide were more sensitive to structural disorganization.

Journal Article↗
PubMed1998

The ratio of erythrocyte zinc-protoporphyrin to protoporphyrin IX in disease and its significance in the mechanism of lead toxicity on haem synthesis.

Protoporphyrin and zinc-protoporphyrin were measured in the erythrocytes of normal subjects, workers exposed to lead and patients with iron deficiency and erythropoietic protoporphyria (EPP). Results showed significantly higher levels of zinc-protoporphyrin in the lead-exposed workers (P < 0.0001), patients with iron deficiency (P < 0.0001) and EPP patients (P < 0.001) compared with normal subjects. The lead-exposed workers showed the highest levels of zinc-protoporphyrin, which were significantly greater than both the iron-deficient and EPP patients (P < 0.0001). They also showed a higher ratio of zinc-protoporphyrin to free protoporphyrin compared with normal subjects (P < 0.0001) but no significant difference in this ratio was found when compared with iron-deficient patients (P = 0.1). These results are discussed in light of the controversy concerning the mechanism of formation of zinc-protoporphyrin in lead exposure.

Adult↗
PubMed1992

Comparative effects of tin- and zinc-protoporphyrin on steroidogenesis: tin-protoporphyrin is a potent inhibitor of cytochrome P-450-dependent activities in the rat adrenals.

Synthetic metalloporphyins inhibit formation of bilirubin by the heme oxygenase system, an ability that is of considerable experimental and clinical interest for suppression of jaundice in the newborn. The present investigation compares the consequences of treatment with Sn- and Zn-protoporphyrin on hemoprotein-dependent enzymes of the rat adrenals and corticosterone production and defines Sn-protoporphyrin as a potent toxin to adrenal functions. Treatment of rats with Sn-protoporphyrin (two doses of 50 mumols/kg, in 7 d) resulted in a marked reduction of 30-40% in cytochrome P-450-dependent adrenal microsomal 21 alpha-hydroxylase and mitochondrial 11 beta-hydroxylase activities. In the serum, the levels of corticosterone were reduced to about 70% of the control value. In addition, the mitochondrial cytochrome P-450SCC activity was decreased by about 50%. This decrease, however, could not be attributed to a reduced total heme level or an accelerated heme degradatory activity. Disruption by Sn-protoporphyrin of adrenal hemoprotein-dependent functions was not restricted to steroidogenic activities and encompassed drug metabolism activity of the organ; benzo(a)pyrene hydroxylase activity of both the microsomal and the mitochondrial fractions, as well as the microsomal NADPH-cytochrome P-450 reductase activity, were significantly reduced. Zn-protoporphyrin did not cause significant alterations in the above measured parameters although it too was effective in inhibiting the hepatic microsomal heme oxygenase activity. In light of the presently defined adverse effects of Sn-protoporphyrin on adrenal steroidogenesis, we suggest Zn-protoporphyrin is the agent of choice for potential use in treatment of hyperbilirubinemia in humans.

Adrenal Glands↗
PubMed1982

In Vitro Synthesis of the Chlorophyll Isocyclic Ring : Transformation of Magnesium-Protoporphyrin IX and Magnesium-Protoporphyrin IX Monomethyl Ester into Magnesium-2,4-Divinyl Pheoporphyrin A(5).

Developing chloroplasts of Cucumis sativus L., cv Beit Alpha which were incubated with either Mg-protoporphyrin IX or Mg-protoporphyrin IX monomethyl ester in darkness produced a partially phototransformable protochlorophyllide species that was tentatively identified as Mg-2,4-divinyl pheoporphyrin a(5). S-Adenosylmethionine stimulated Mg-2,4-divinyl pheoporphyrin a(5) formation irrespective of the starting material used. In the case of Mg-protoporphyrin IX monomethyl ester, this stimulation was attributed to the need to remethylate substrate that had been hydrolyzed by an endogenous methylesterase which converts part of the added Mg-protoporphyrin IX monomethyl ester to Mg-protoporphyrin IX.NADP and NADPH stimulated the conversion of Mg-protoporphyrin IX to Mg-2,4-divinyl pheoporphyrin a(5). The conversion required oxygen and was half saturated at 50 micromolar dissolved O(2). The conversion was insensitive to inhibitors of iron-sulfur and heme-containing proteins, to Cu chelators, H(2)O(2), and peroxide scavengers. However, the conversion was extremely sensitive to phenazine methosulfate, methylene blue, and methyl viologen.A decrease of the plastids' ability to convert Mg-protoporphyrin IX to Mg-2,4-divinyl pheoporphyrin a(5) after lysis in 0.1 molar NaCl suggested a requirement for plastid integrity.

Journal Article↗
PubMed1982

Evaluation of erythrocyte protoporphyrin and zinc protoporphyrin as micro screening procedures for lead poisoning detection.

Seven hundred and three blood samples from children were analysed for lead by Delves cup atomic absorption, for protoporphyrin by solvent extraction and fluorescence, and for zinc protoporphyrin with two manufacturers' models of automated front-face fluorimeter (haemato-fluorimeter). This power of protoporphyrin analysis for predicting the level of lead in blood was found to be poor. Up to 30% of children with lead concentrations of greater than or equal to 40 g/100 ml (greater than or equal to 1.93 mumol/l) and nearly 60% of children with greater than or equal to 30 microgram/100 ml (greater than or equal to 1.45 mumol/l) would remain undetected if protoporphyrin analysis were used for screening with an action level of 60 microgram/100 ml (1.07 mumol/l) for the porphyrin analysis. The predictive power of protoporphyrin analyses improves with the age of the child, indicating that the less expensive protoporphyrin test may be acceptable for older children, if by this means a large population of children at risk can be screened.

Child↗
PubMed1992

Spectrofluorometric estimation of intermediates of chlorophyll biosynthesis: protoporphyrin IX, Mg-protoporphyrin, and protochlorophyllide.

A highly sensitive spectrofluorometric method for quantitative estimation of certain precursors of chlorophyll biosynthesis from the mixtures of plant tetrapyrroles having overlapping fluorescence emission spectra is developed. At room temperature (293 degrees K) protoporphyrin IX is monitored from its emission maximum, 633 nm, when excited at 400 nm (E400/F633). Protochlorophyllide is estimated at 638 nm, while being excited at 440 nm (E440/F638). Mg-protoporphyrin+Mg-protoporphyrin monoester pool has emission around 589-592 nm. Therefore the integration value of the emission band that extends from 580 to 610 nm is taken to calibrate its concentration. This spectrofluorometric method designed for the determination of protoporphyrin IX, esterified and nonesterified Mg-protoporphyrin pool, and protochlorophyllide is far superior to available spectrophotometric methods and estimates as low as 1 nM concentration of plant pigments. As minute quantities of individual pigments can be quantitatively analyzed from their mixtures, this method eliminates analytical uncertainties due to recovery losses caused by chromatography. However, only dilute samples can be estimated by this spectrofluorometric method as the quantitative relation between fluorescence and concentration deviates from linearity at high, i.e., above 150 nM, concentrations of pigment to be quantified.

Acetone↗
PubMed1980

Hepatic protoporphyrin production in human protoporphyria. Effects of intravenous hematin and analysis of erythrocyte protoporphyrin distribution.

Human protoporphyria with atypical features suggesting increased hepatic protoporphyrin synthesis was investigated in 2 patients. Analysis of the distribution of protoporphyrin among circulating erythrocytes of increasing age indicated that the erythrocyte porphyrin burden derived predominantly from erythroid sources in case 1, and from hepatic sources in case 2. Intravenous hematin was administered to both patients to assess any negative feedback effect on protoporphyrin synthesis. Erythrocyte, fecal and plasma porphyrin levels were measured serially during basal, treatment, and follow-up periods. In case 1, a significant (P less than 0.001) drop in both fecal and plasma levels accompanied hematin, while erythrocyte levels remained unchanged. Hematin produced no appreciable changes in porphyrin concentrations in case 2. Allergic vasculitis followed hematin use in both cases. Based on data of this study and on previous data, a model for protoporphyrin transport and clearance was developed in which the variable clinical and biochemical manifestations of human protoporphyria are related to the relative contributions of erythroid and hepatic sources to the abnormal protoporphyrin pools.

Adult↗
PubMed1981

Accumulation of protoporphyrin IX and Zn protoporphyrin IX in Cyanidium caldarium.

In vivo fluorescence studies of Cyanidium caldarium mutants grown in the dark in dextrose-containing media have shown that these organisms accumulate protoporphyrin IX. In the dark the accumulated protoporphyrin IX is gradually turned into a metalloporphyrin, Zn protoporphyrin. In the light, in the chlorophyll-lacking mutant GGB, both compounds are degraded and phycobiliproteins are formed. These results implicate protoporphyrin IX in situ as the general precursor to tetrapyrrole pigments and Zn protoporphyrin IX as a possible intermediate or regulator in the biosynthesis of phycobilins.

Journal Article↗
PubMed1974

Genetic control of chlorophyll biosynthesis in Chlamydomonas. Analysis of mutants at two loci mediating the conversion of protoporphyrin-IX to magnesium protoporphyrin.

In this report we describe two nonallelic Mendelian protoporphyrin accumulating mutants br(s)-1 and br(c)-1. Results of experiments with these mutants lead us to postulate that porphyrin biosynthesis branches into light and dark steps between protoporphyrin-IX and magnesium protoporphyrin. We hypothesize that the br(c) locus controls a dark step while the br(s) locus either controls a step in the main pathway before the branch or mediates the preparation of the magnesium ion for its insertion into protoporphyrin-IX. The br(s)-1 mutant is thought to be light sensitive because a block prior to the branch point in the porphyrin pathway prevents chlorophyll formation in either the light or the dark. The br(c)-1 mutant, which also accumulates protoporphyrin in the dark, forms chlorophyll and chloroplast lamellae when transferred to the light, showing that function of the porphyrin pathway is normal in the light.

Cell Count↗
PubMed1992

Chloroplast Biogenesis 65 : Enzymic Conversion of Protoporphyrin IX to Mg-Protoporphyrin IX in a Subplastidic Membrane Fraction of Cucumber Etiochloroplasts.

The preparation from Percoll-purified cucumber (Cucumis sativus)etiochloroplasts of a subplastidic membrane fraction that is capable of high rates of Mg insertion into protoporphyrin IX is described. The plastid stroma was inactive when used either alone or in combination with the membrane fraction. Successful preparation of the subplastidic membrane fraction required that Mg-protoporphyrin chelatase was first stabilized by its substrate. This was achieved by lysing Percoll-purified plastids in a fortified hypotonic medium containing protoporphyrin IX prior to ultracentrifugation and separation of the stroma from the plastid membranes. Protoporphyrin IX became membrane bound. Other additives needed for enzyme activity fell into two groups: (a) those needed for enzyme stabilization during membrane preparation and (b) those involved in the primary mechanism of Mg insertion into protoporphyrin IX. Ethylenediaminetetraacetate belonged to the first group, magnesium belonged to the second group, and ATP belonged to both groups.

Journal Article↗
PubMed1984

Free erythrocyte protoporphyrin (FEP) and zinc protoporphyrin (ZnP) as biological parameters for lead poisoning.

Lamola et al. (1974) reported that free erythrocyte protoporphyrin (FEP) is not present as free type protoporphyrin ( FPP ) but rather is chelated with zinc in lead poisoning and iron deficiency anemia. In our fluorometric study of FEP and zinc protoporphyrin ( ZnP ) in erythrocytes of lead-poisoned rabbits and lead workers, the co-existence of ZnP and FPP was observed in the severe stage of acute lead poisoning in rabbits. The ratio of ZnP to FEP in erythrocytes decreased with the progress of lead intoxication, and the amount of FPP was greater than that of ZnP in the severe stage of intoxication. This FPP accumulated in the erythrocytes was easily converted to ZnP by incubation of the hemolysate with zinc. On the other hand, increased protoporphyrin (PP) in bone marrow was present as FPP in lead intoxication. From these results, ZnP in peripheral erythrocytes is considered to be a secondary product, not a primary one. Therefore, the determination of total FEP ( FPP + ZnP ) by the acid solvent extraction method might be more reasonable than using ZnP -determination as the biological parameter of lead poisoning. We propose that erythrocyte porphyrin in lead intoxication should be expressed as FEP, not as ZnP , for the parameter. The present study also suggests that the form of erythrocyte FPP in erythropoietic protoporphyria (EPP) patients is a little different from that in lead-poisoning patients, because of its high chelation reactivity with zinc.

Anemia, Hypochromic↗
PubMed1988

[Automated HPLC method for determining zinc protoporphyrin IX and protoporphyrin IX in erythrocytes of workers exposed to lead].

We developed an automated HPLC method for determining erythrocyte protoporphyrin. After a single extraction with N,N-dimethylformamide (DMF), zinc protoporphyrin IX (ZP) and protoporphyrin IX (PP) were separated by the column packed with a new type of reversed phase silica (capcell type) within 5 min. The column life was markedly extended to facilitate sample injection for about 1,000 times. The concentrations of ZP or TP (total protoporphyrin = 0.9 ZP + PP) determined by the present method correlated well with those determined by the conventional methods, i.e. by hematofluorometer (HF) or acid extraction method (FEP). In 150 workers exposed to lead, the ratio of 0.9 ZP/TP varied between 0.43 and 0.99 with the ratio being less than 0.6 in only 5 workers. The correlation coefficient between Pb-B and ZP was significantly higher than that between Pb-B and PP. Both anticoagulants, heparin and EDTA, could be used in the present method as well as in HF and FEP methods. Reference values for TP by HPLC were between 31.2 and 120.9 micrograms/dl RBC. Samples stored at 37 degrees C for 3 days were also used in the present method and the same results were obtained as in the samples stored at 4 degrees C.

Adult↗
PubMed1992

[Determination of protoporphyrins in blood using HPLC. Standardization of protoporphyrins and interlaboratory comparison of analyses].

1) In order to compare the results of determination of protoporphyrin IX (PP) and zinc protoporphyrin IX (ZP) using HPLC, the preparation procedures for standard solutions of PP and ZP were studied at four laboratories. According to the methods mutually agreeable to the four laboratories, the absorption values using UV-Vis spectrometer from the 4 laboratories were found to be identical. 2) The total of 28 whole blood samples obtained from the same workers whose Pb-B levels ranged from 2.9 to 87.9 micrograms/dl were sent to the 4 laboratories for determination of PP and ZP. The laboratories were allowed to use their own HPLC apparatus, column, mobile phase and fluorometric detectors, although the same procedures were used to prepare the standard solutions of PP and ZP. The results showed that significant biases in ZP and PP levels were found between two out of the 4 laboratories, but the ZP values corrected by the recovery rate showed no statistical difference among the laboratories. 3) Blood levels of ZP, total protoporphyrin (TP, calculated by PP+ZP/1.1), and PP determined by HPLC method correlated well with free erythrocyte protoporphyrin (FEP) determined by the method of extraction into the acidic solvent. The correlation coefficients between Pb-B and log TP, ZP, FEP or PP were 0.82-0.84, 0.80-0.83, 0.786, or 0.70-0.73, respectively. 4) The coincident ratios of PP/TP obtained at 4 laboratories ranged from 12.1 to 19.0%. These values were within a relatively narrow range, although two different kinds of organic solvents (DMF: N',N'-dimethylformamide or Methanol/triton-X 100) were used in the extraction steps.(ABSTRACT TRUNCATED AT 250 WORDS)

Chromatography, High Pressure Liquid↗
PubMed1994

Heme oxygenase: the physiological role of one of its metabolites, carbon monoxide and interactions with zinc protoporphyrin, cobalt protoporphyrin and other metalloporphyrins.

In 1991, we postulated that carbon monoxide, which is formed endogenously from heme catabolism catalyzed by heme oxygenase and shares some of the chemical and biological properties of nitric oxide, may play a role similar to that of nitric oxide as a widespread signal transduction mechanism for the regulation of cell function and communication. We review the experimental evidence that tests this postulate. Carbon monoxide appears to be involved in the neurophysiological phenomenon of long-term potentiation, which appears to play a key role in memory and learning. Zinc protoporphyrin, an inhibitor of heme oxygenase, prevents induction of long-term potentiation. Zinc protoporphyrin is an endogenous substance, the levels of which are increased in iron deficiency states and in lead poisoning, and by inhibiting heme oxygenase may modulate long-term potentiation and memory. It has been shown that, when cobalt protoporphyrin is injected into the medial nuclei of the rat hypothalamus, weight loss occurs. These nuclei contain heme oxygenase, and we postulate that weight loss is due to cobalt protoporphyrin induction of heme oxygenase and increased formation of carbon monoxide, which serves as a signal transduction mechanism in the medial hypothalamus to suppress appetite.

Animals↗