The use of a 100 IU starting dose of recombinant follicle stimulating hormone (Puregon) in in-vitro fertilization.
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Adult↗
Biomedical subjects
P Hendrix
Publications and source records attributed to P Hendrix.
Daily dietary chromium intake in Belgium, using duplicate portion sampling.
Daily dietary chromium intake in Belgium has been evaluated by sampling duplicate portions of food, heating them at an acidic pH in a microwave oven and then quantifying the chromium by atomic absorption spectrometry. The mean intake value (53 +/- 31 micrograms/day) is similar to levels found for most other countries and is situated at the lower end of the recommended range for a safe and adequate daily dietary intake.
Belgium↗
Daily dietary copper intake in Belgium, using duplicate portion sampling.
Daily dietary copper intake in Belgium has been evaluated by duplicate portion sampling, heating in a microwave oven and atomic absorption spectrometric determination of this element. The mean intake value (1.5 +/- 0.4 mg/day) is similar to levels found for most other countries, but is situated at the lower end of the recommended range for a safe and adequate daily dietary intake.
Adult↗
Measurement of the daily dietary calcium and magnesium intake in Belgium, using duplicate portion sampling.
The daily dietary calcium and magnesium intakes in Belgium were evaluated by sampling duplicate portions of food, destruction in a microwave oven and their calcium and magnesium contents determined by atomic absorption spectroscopy. The mean intake value for calcium (618 +/- 125 mg/day) was found to be less than those values measured in most other countries and was below the recommended daily allowance (RDA). The mean intake value for magnesium (271 +/- 44 mg/day) was similar to levels found in most other countries, but was below the RDA value for healthy adult men (350 mg/day) whilst being adequate for healthy women (280 mg/day).
Adult↗
Daily dietary manganese intake in Belgium, using duplicate portion sampling.
Daily dietary manganese intake in Belgium was evaluated by duplicate portion sampling, destruction by cooking in a microwave oven and subsequent analysis for this element by atomic absorption spectrometry. The mean intake value (3.1 +/- 1.1 mg/day) is similar to levels found for most other countries and is within WHO/RDA and National Research Council, USA recommended intake ranges.
Adult↗
Actual daily dietary intake of selenium in Belgium, using duplicate portion sampling.
The dietary selenium (Se) intake in Belgium has been re-evaluated. Duplicate meal collection, wet acid destruction and flow injection hydride generation atomic absorption spectrometry were used as techniques. The daily intake ranged from 28.4 micrograms (Liège, Walloon part of the country) to 61.1 micrograms (Vilvoorde, central part of the country). Compared with intakes recently published for other countries, the actual Belgian value corresponds to intermediate ranges of Se intake.
Belgium↗
Chronic radiation enteritis.
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Chronic Disease↗
Structure and expression of a 72-kDa regulatory subunit of protein phosphatase 2A. Evidence for different size forms produced by alternative splicing.
The trimeric form of protein phosphatase 2A consisting of 36-, 65-, and 72-kDa subunits (previously termed polycation-stimulated protein phosphatase M) was purified from rabbit skeletal muscle. Amino acid sequence data of the 72-kDa regulatory subunit (termed PR72) were used to isolate cDNAs from human heart and fetal brain libraries and libraries derived from WI-38 and MCF-7 cells. The clones isolated from the heart cDNA library revealed an open reading frame encoding a protein with a predicted molecular mass of 62 kDa. All the peptides sequenced from the protein matched with the sequence predicted from the cDNA. However, in vitro transcription and translation from this cDNA yielded a protein with an apparent molecular mass of 72 kDa on sodium dodecyl sulfate-polyacrylamide gels. From brain we isolated cDNA clones spanning an open reading frame encoding a 130-kDa protein (termed PR130). The apparent molecular mass of the protein produced by in vitro transcription and translation was 130 kDa. This protein has exactly the same deduced C-terminal protein sequence as the PR72 subunit from amino acids 45 to 527 but has an N-terminal extension of 665 amino acids. It is likely, therefore, that these two proteins arise from the same gene by alternative splicing. In human tissues several transcripts were detected by Northern analysis generated probably by the use of different polyadenylation signals and alternative splicing. High levels of the PR72 mRNAs were detected in heart and muscle, while lower levels of PR130 transcripts were found in heart, brain, placenta, lung, muscle, and kidney.
Alternative Splicing↗
Analysis of subunit isoforms in protein phosphatase 2A holoenzymes from rabbit and Xenopus.
A dimeric and two trimeric forms of protein phosphatase 2A (PP2A) were purified from rabbit and Xenopus tissues and analyzed using antisera specific for the catalytic and regulatory subunits. The dimeric holoenzyme consists of a complex between a 36-kDa catalytic subunit associated with a approximately 65-kDa regulatory subunit. The two trimeric holoenzymes consist of the catalytic subunit complexed with 65- and 55-kDa subunits, or 65- and 72-kDa subunits. Antisera were raised against synthetic peptides specific for the alpha- and beta-isoforms of the 65-kDa (PR65 alpha/beta) and 55-kDa (PR55 alpha/beta) subunits identified by molecular cloning. Anti-peptide antisera to the 36-kDa catalytic subunit of PP2A were prepared against two selected regions: one specific for the alpha-isoform and one to a peptide common to both the alpha- and beta-isoforms. Immunochemical analysis of all three mammalian holoenzymes showed that the catalytic, 55- and 65-kDa subunits are both predominantly of the alpha-isoform, which is consistent with the peptide sequence data. The 65-kDa subunit of PP2A holoenzymes isolated from Xenopus skeletal muscle reacted with both anti-alpha and anti-beta PR65-specific antisera whereas the PP2A holoenzymes isolated from Xenopus oocytes reacted preferentially with the beta-specific antisera, indicating developmental changes in the expression of the 65-kDa subunit isoform. Taken together, these results show that the "core" subunits of the PP2A holoenzymes consist of the catalytic complexed with the 65-kDa subunit and that the association of the third subunit does not appear to be influenced by the isoform of these two core subunits.
Amino Acid Sequence↗
Phosphorylation of the phosphatase modulator subunit (inhibitor-2) by casein kinase-1. Identification of the phosphorylation sites.
The isolated modulator subunit of the inactive protein phosphatase-1 is phosphorylated in vitro by casein kinase-1 at two different sites: Ser-86 and Ser-174. The Ser-86 site is a common target for casein kinase-1 and casein kinase-2, but is preferentially phosphorylated by the former enzyme. The Ser-174 site seems to be specific for casein kinase-1, and is phosphorylated at a slower rate. These results give a new insight into the in vitro phosphorylation pattern of the modulator subunit of the phosphatase and provides additional data on the specificity of casein kinase-1.
Amino Acid Sequence↗
Structure of the 55-kDa regulatory subunit of protein phosphatase 2A: evidence for a neuronal-specific isoform.
The trimeric form of protein phosphatase 2A (PP2A1 or polycation-stimulated protein phosphatase H1) was purified to homogeneity from rabbit skeletal muscle. Preparative SDS-polyacrylamide gel electrophoresis was used to purify the individual subunits with relative molecular masses of 36, 55, and 65 kDa. Sequence analysis of five peptides from the 65-kDa regulatory subunit (PR65) suggested that it was identical with the PR65 subunit derived from the dimeric protein phosphatase 2A2. Amino acid sequences derived from the 55-kDa regulatory subunit (PR55) were used to clone human and rabbit cDNAs encoding this protein. The PR55 subunit was found to be encoded by two genes, termed alpha and beta. The open reading frames of the PR55 alpha and beta cDNAs spanned 1341 and 1329 nucleotides, respectively, and predicted proteins with a molecular mass of about 52 kDa that are 86% identical. Comparison of the human PR55 amino acid sequences with the data obtained from the rabbit skeletal muscle protein and a partial rabbit PR55 beta cDNA clone indicated a high degree of conservation. Analysis of the mRNA expression in human cell lines revealed that the PR55 alpha isoform was encoded by two transcripts of about 2.3 and 2.5 kb and a less abundant 4.4-kb mRNA. Whereas a PR55 beta transcript of about 2.3 kb was detected at high levels in the neuroblastoma derived cell line LA-N-1, the level of the mRNA was very low in the other human cell lines analyzed. Interestingly, the PR55 sequence showed limited homology to the catalytic domain (domains VI-IX) of the c-abl protein tyrosine kinase.
Amino Acid Sequence↗
Isolation and characterization of a tyrosyl phosphatase activator from rabbit skeletal muscle and Xenopus laevis oocytes.
PTPA, a specific phosphotyrosyl phosphatase activator of the PCSH2 and PCSL protein phosphatases, was purified up to apparent homogeneity from Xenopus laevis ovaries and rabbit skeletal muscle and highly purified from dog liver. PTPA appears as a 40-kDa protein in gel filtration, as well as in sucrose gradient centrifugation, and as a 37-39-kDa protein doublet in SDS-PAGE. Its estimated cellular concentration of 0.75 microM in oocytes or 0.25 microM in rabbit skeletal muscle is suggestive of an important role in the regulation of the cellular PTPase activity. The PTPase activation reaction of the PCSL phosphatase is time-dependent, ATP and Mg2+ being essential cofactors [A50(ATP) = 0.12 mM in the presence of 5 mM MgCl2]. With RCM lysozyme as substrate, the specific activity of the PTPA-activated PCSL phosphatase is 700 nmol of Pi/(min.mg). The pH optimum of the PTPase shifts from 8.5-9 in basal conditions to a neutral pH (7-7.5), and the A50 for the essential metal ion Mg2+ is decreased (3 mM). The activation is rapidly reversed in the presence of the substrate, and more slowly after removal of ATP.Mg. The PTPA-activated PCSL phosphatase represents a major PTPase activity in the cytosol of X. laevis oocytes (at least 50% of the measurable PTPase with RCM lysozyme phosphorylated on tyrosyl residues). The PTPA activation is specific for the PTPase activity of the PCSL and PCSH2 phosphatases, without affecting their phosphoseryl/threonyl phosphatase activity. However, effectors of the phosphorylase phosphatase activity, such as polycations and okadaic acid, also influence the PTPase activity. Phosphorylase alpha inhibits the activated PTPase activity (I50 = 5 microM). The PTPase activity of the other oligomeric PCS phosphatases (PCSH1 and PCSM) is not influenced, suggesting an inhibitory role for some of their subunits. This activation is compared with the recently described PTPase stimulation of the PCS phosphatases by ATP/PPi [Goris, J., Pallen, C. J., Parker, P. J., Hermann, J., Waterfield, M. D., & Merlevede, W. (1988) Biochem. J. 256, 1029-1034] and by tubulin [Jessus, C., Goris, J., Cayla, X., Hermann, J., Hendrix, P., Ozon, R., & Merlevede, W. (1989) Eur. J. Biochem. 180, 15-22].
4-Nitrophenylphosphatase↗
Phosphotyrosyl phosphatase activity of the polycation-stimulated protein phosphatases and involvement of dephosphorylation in cell cycle regulation.
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Animals↗
Okadaic acid, a specific protein phosphatase inhibitor, induces maturation and MPF formation in Xenopus laevis oocytes.
Micro-injection of, or incubation with okadaic acid (OA), a specific phosphatase inhibitor, can induce formation of maturation-promoting factor (MPF) and germinal vesicle breakdown (GVBD) in Xenopus laevis oocytes. Comparison of the dose-response curves of OA on maturation, isolated enzymes and phosphatase activities in crude oocyte preparations suggests that inhibition of both polycation-stimulated (PCS) and ATP,Mg-dependent (AMD) phosphatases is sufficient but requires that a critical phosphorylation level is attained of one or several of their substrates, resulting in the formation of active MPF and meiotic maturation.
Adenosine Triphosphate↗
Tubulin and MAP2 regulate the PCSL phosphatase activity. A possible new role for microtubular proteins.
Tubulin can stimulate specifically the aryl phosphatase activity of the low-Mr polycation-stimulated (PCSL) phosphatase, measured as p-nitrophenyl phosphatase activity, or using reduced carboxamidomethylated and maleylated (RCM) lysozyme, phosphorylated on tyrosyl residues, as a substrate. This stimulation is independent of the degree of polymerization of tubulin (A50 = 60 nM) and is due to an increase in Vmax. It is mechanistically different from the ATP-induced activation and resistant to heat and trypsin treatment. Chymotrypsin destroys the stimulatory effect of tubulin. The polycation-stimulated phosphorylase phosphatase activity is inhibited by tubulin, probably by a polycation/polyanion interaction. The microtubule-associated protein, MAP2, is inhibitory to the p-nitrophenyl phosphatase activity and tubulin can eliminate this inhibitory effect. MAP2 also inhibits the polycation-stimulated phosphorylase phosphatase activity.
4-Nitrophenylphosphatase↗