Rat Harderian Gland Porphobilinogen Deaminase: Characterization Studies and Regulatory Action of Protoporphyrin IX

Cardalda, Carina; Juknat, Adela Ana; Princ, Fernando G.; Batlle, Alcira

doi:10.1006/abbi.1997.0310

Cited by 12 publications

(3 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition to characterization of a heme metabolism protein complex three points of interest that have significant impact were revealed in the current study. First, data were obtained that suggest the cytosolic protein Hmbs is a functional homodimer, not a monomer as presumed from in vitro studies of the purified protein[ 32 , 62 ]. Second, Ppox was identified as a homodimer in situ as opposed to a monomer as suggested from in vitro studies by others[ 63 ].…”

Section: Discussionmentioning

confidence: 99%

Identification of the Mitochondrial Heme Metabolism Complex

et al. 2015

View full text Add to dashboard Cite

Heme is an essential cofactor for most organisms and all metazoans. While the individual enzymes involved in synthesis and utilization of heme are fairly well known, less is known about the intracellular trafficking of porphyrins and heme, or regulation of heme biosynthesis via protein complexes. To better understand this process we have undertaken a study of macromolecular assemblies associated with heme synthesis. Herein we have utilized mass spectrometry with coimmunoprecipitation of tagged enzymes of the heme biosynthetic pathway in a developing erythroid cell culture model to identify putative protein partners. The validity of these data obtained in the tagged protein system is confirmed by normal porphyrin/heme production by the engineered cells. Data obtained are consistent with the presence of a mitochondrial heme metabolism complex which minimally consists of ferrochelatase, protoporphyrinogen oxidase and aminolevulinic acid synthase-2. Additional proteins involved in iron and intermediary metabolism as well as mitochondrial transporters were identified as potential partners in this complex. The data are consistent with the known location of protein components and support a model of transient protein-protein interactions within a dynamic protein complex.

show abstract

Section: Discussionmentioning

confidence: 99%

Identification of the Mitochondrial Heme Metabolism Complex

et al. 2015

View full text Add to dashboard Cite

show abstract

“…for the activity of the mammalian enzyme porphobilinogen deaminase (PBG-D), 76.1 kJ mol −1 . 26 If we assume that eukaryotic and prokaryotic PBG-D are somewhat similar, then this suggests that PBG-D represents the rate-limiting step for CpIII and UpIII production in P. acnes bacteria when incubated with ALA. In the case of methyl ALA-induced CpIII and UpIII fluorescence in P. acnes, the mean E a was found to be 65.3 kJ mol −1 .…”

Section: Clinical Use Of Pdt For Acnementioning

confidence: 99%

The temperature dependence of porphyrin production in Propionibacterium acnes after incubation with 5-aminolevulinic acid (ALA) and its methyl ester (m-ALA)

Ramstad

Anh-Vu

Johnsson

2006

Photochem Photobiol Sci

View full text Add to dashboard Cite

Topical PDT treatment of the common skin disease acne vulgaris is now in clinical use. Propionibacterium acnes (P. acnes) is known to play an important role in acne. 5-Aminolevulinic acid (ALA) supplementation leads to an enhanced porphyrin production in the bacteria. Subsequent illumination with light of the proper wavelengths can reduce the number of bacteria and this might at least partly explain the PDT effect on acne. We have assessed the effects of temperature on P. acnes washed cell suspensions incubated for 4 h with ALA or ALA methyl ester (m-ALA). The effect on porphyrin production of both the cell suspension incubation temperature as well as the initial growth temperature of the cultivated cells prior to harvesting and use in suspension experiments was investigated. The bacterial porphyrin content was estimated from fluorescence emission spectra. It was found that incubation with ALA or m-ALA at a temperature 42 degrees C resulted in an approx. 100% and 33% increase in the total amount of PDT-relevant porphyrins produced as compared to incubation at 37 degrees C. These results support increasing the skin temperature during incubation with ALA or m-ALA in the clinic. The initial growth temperature, prior to the incubation, had no apparent effect on the ALA or m-ALA induced porphyrins. Activation energy studies indicate slightly higher temperature dependence in the case of ALA produced porphyrins as compared to m-ALA produced porphyrins (77 and 65 kJ mol(-1), respectively).

show abstract

“…The major porphyrin component in rodents was reported to be protoporphyrin, with much smaller amounts of harderoporphyrin and other porphyrins [14,15]. In the rat, the porphyrins present in the adult are in the range of µg\mg of wet weight [16].…”

Section: Introductionmentioning

confidence: 99%

Isolation and characterization of protoporphyrin glycoconjugates from rat Harderian gland by HPLC, capillary electrophoresis and HPLC/electrospray ionization MS

Lim

Razzaque

Luo

et al. 2000

Biochemical Journal

View full text Add to dashboard Cite

It has been widely reported that the Harderian gland, present in most vertebrates, accumulates high levels of porphyrins, particularly protoporphyrin. The present study describes the extraction, identification and characterization of a group of hitherto unreported protoporphyrin glycoconjugates in the rat Harderian gland using HPLC, capillary electrophoresis, on-line HPLC/electrospray ionization MS and tandem MS. The major glycoconjugate was identified as protoporphyrin-1-O-acyl β-xyloside with a smaller amount of protoporphyrin-1-O-acyl β-glucoside also detected. In the Harderian glands studied, 50-70% of the porphyrins present were in the form of protoporphyrin glycoconjugates. This is the first reported occurrence of glycoconjugates of porphyrins in Nature and suggests that previous studies have wrongly identified the major porphyrin in the Harderian gland as the unconjugated protoporphyrin.

show abstract

Rat Harderian Gland Porphobilinogen Deaminase: Characterization Studies and Regulatory Action of Protoporphyrin IX

Cited by 12 publications

References 38 publications

Identification of the Mitochondrial Heme Metabolism Complex

Identification of the Mitochondrial Heme Metabolism Complex

The temperature dependence of porphyrin production in Propionibacterium acnes after incubation with 5-aminolevulinic acid (ALA) and its methyl ester (m-ALA)

Isolation and characterization of protoporphyrin glycoconjugates from rat Harderian gland by HPLC, capillary electrophoresis and HPLC/electrospray ionization MS

Contact Info

Product

Resources

About