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Brian J. Morris - One of the best experts on this subject based on the ideXlab platform.

  • similarity of blood pressure for each genotype of the insertion deletion polymorphism of the Dipeptidyl Carboxypeptidase 1 gene in different age groups of patients with severe familial essential hypertension
    Clinical and Experimental Pharmacology and Physiology, 1994
    Co-Authors: Brian J. Morris, Robert Y L Zee
    Abstract:

    1. The association of alleles of an insertion/deletion polymorphism (I/D) of the Dipeptidyl Carboxypeptidase-1 gene with hypertension is controversial. If a particular allele makes a major contribution to blood pressure, then hypertensives homozygous for this allele could be expected to have higher high blood pressure than those homozygous for the alternate allele. 2. The present study examined this hypothesis by comparing pretreatment blood pressures of hypertensives who had been genotypes for the I/D polymorphism. Blood pressures for different age groups ( or = 60 years) were also examined for each genotype. In addition, several other parameters were examined. 3. Systolic blood pressures were found to be 167 +/- 3, 167 +/- 3 and 170 +/- 6 mmHg (mean +/- s.e.) for the genotypes II, ID and DD, respectively. Diastolic blood pressures were 113 +/- 4, 111 +/- 2 and 111 +/- 4, for the respective genotypes. One-way ANOVA showed that the respective blood pressure values did not differ significantly across genotypes. Blood pressures for different age groups of hypertensives were also similar. 4. In addition, body mass index, mean age and sex did not differ between genotypes, either for the group as a whole or for the different age groups. 5. In conclusion, the present study could find no evidence to support a genetic association between the I/D polymorphism of DCP1 and blood pressure in a group with severe, familial hypertension living in Sydney.

  • genotypic influence on plasma Dipeptidyl Carboxypeptidase 1 activity in hypertensives
    Clinical and Experimental Pharmacology and Physiology, 1994
    Co-Authors: Brian J. Morris, J. C. Monaghan, Rose Perich, G. S. Stokes, Bruce Jackson, Andrew P. Schrader
    Abstract:

    SUMMARY 1. Plasma Dipeptidyl Carboxypeptidase-1 (DCP1; angiotensin I-converting enzyme, kininase II; EC 3.4.15.1) tracks with the deletion allele in genotypes of a 287 bp insertion/deletion (I/D) polymorphism of its gene, DCP1, in healthy Caucasian populations. The aim of the present study was to see whether genotype has a similar influence on plasma DCP1 in hypertensives. 2. The study involved 35 Caucasian patients with severe, familial essential hypertension, who were not being treated with DCP1 inhibitors, and 94 normotensives. Genotyping for the I/D polymorphism was performed by polymerase chain reaction and plasma DCP1 activity was measured by rate of hydrolysis of both [3H]-Hip-Gly-Gly and Hip-His-Leu. 3. Plasma DCP1 activity (nmol Gly-Gly/min per mL; mean ± s.e.m.) was 67 ± 2, 82 ± 4 and 91 ± 6 in II, ID and DD hypertensives, respectively, which was similar to values of 68 ± 4, 82 ± 3 and 94 ± 3 in normotensives (P= 0.0001 by one-way analysis of variance). Results for the His-Leu assay indicated similar tracking with genotype. 4. The Michaelis constant (μmol Hip-Gly-Gly/mL; mean ± s.e.m., n= 10) for DD subjects was the same as for II subjects (10.6 ± 1.6 vs 11.1 ± 2.3; P = 0.86). 5. In conclusion, in severely hypertensive Caucasian subjects, plasma DCP1 activity is subject to a similar genotypic influence in hypertensives as has been reported previously in normotensives. Furthermore, the plasma DCP1 enzyme itself appears to be functionally similar for each genotype.

  • GENOTYPIC INFLUENCE ON PLASMA Dipeptidyl Carboxypeptidase‐1 ACTIVITY IN HYPERTENSIVES
    Clinical and experimental pharmacology & physiology, 1994
    Co-Authors: Brian J. Morris, J. C. Monaghan, Rose Perich, G. S. Stokes, Bruce Jackson, Andrew P. Schrader
    Abstract:

    SUMMARY 1. Plasma Dipeptidyl Carboxypeptidase-1 (DCP1; angiotensin I-converting enzyme, kininase II; EC 3.4.15.1) tracks with the deletion allele in genotypes of a 287 bp insertion/deletion (I/D) polymorphism of its gene, DCP1, in healthy Caucasian populations. The aim of the present study was to see whether genotype has a similar influence on plasma DCP1 in hypertensives. 2. The study involved 35 Caucasian patients with severe, familial essential hypertension, who were not being treated with DCP1 inhibitors, and 94 normotensives. Genotyping for the I/D polymorphism was performed by polymerase chain reaction and plasma DCP1 activity was measured by rate of hydrolysis of both [3H]-Hip-Gly-Gly and Hip-His-Leu. 3. Plasma DCP1 activity (nmol Gly-Gly/min per mL; mean ± s.e.m.) was 67 ± 2, 82 ± 4 and 91 ± 6 in II, ID and DD hypertensives, respectively, which was similar to values of 68 ± 4, 82 ± 3 and 94 ± 3 in normotensives (P= 0.0001 by one-way analysis of variance). Results for the His-Leu assay indicated similar tracking with genotype. 4. The Michaelis constant (μmol Hip-Gly-Gly/mL; mean ± s.e.m., n= 10) for DD subjects was the same as for II subjects (10.6 ± 1.6 vs 11.1 ± 2.3; P = 0.86). 5. In conclusion, in severely hypertensive Caucasian subjects, plasma DCP1 activity is subject to a similar genotypic influence in hypertensives as has been reported previously in normotensives. Furthermore, the plasma DCP1 enzyme itself appears to be functionally similar for each genotype.

  • Similarity of blood pressure for each genotype of the insertion/deletion polymorphism of the Dipeptidyl Carboxypeptidase-1 gene in different age groups of patients with severe, familial essential hypertension.
    Clinical and experimental pharmacology & physiology, 1994
    Co-Authors: Brian J. Morris, Robert Y L Zee
    Abstract:

    1. The association of alleles of an insertion/deletion polymorphism (I/D) of the Dipeptidyl Carboxypeptidase-1 gene with hypertension is controversial. If a particular allele makes a major contribution to blood pressure, then hypertensives homozygous for this allele could be expected to have higher high blood pressure than those homozygous for the alternate allele. 2. The present study examined this hypothesis by comparing pretreatment blood pressures of hypertensives who had been genotypes for the I/D polymorphism. Blood pressures for different age groups ( or = 60 years) were also examined for each genotype. In addition, several other parameters were examined. 3. Systolic blood pressures were found to be 167 +/- 3, 167 +/- 3 and 170 +/- 6 mmHg (mean +/- s.e.) for the genotypes II, ID and DD, respectively. Diastolic blood pressures were 113 +/- 4, 111 +/- 2 and 111 +/- 4, for the respective genotypes. One-way ANOVA showed that the respective blood pressure values did not differ significantly across genotypes. Blood pressures for different age groups of hypertensives were also similar. 4. In addition, body mass index, mean age and sex did not differ between genotypes, either for the group as a whole or for the different age groups. 5. In conclusion, the present study could find no evidence to support a genetic association between the I/D polymorphism of DCP1 and blood pressure in a group with severe, familial hypertension living in Sydney.

  • independent marked associations of alleles of the insulin receptor and Dipeptidyl Carboxypeptidase i genes with essential hypertension
    Clinical Science, 1993
    Co-Authors: Brian J. Morris, Robert Y L Zee, Lihua Ying, Lyn R Griffiths
    Abstract:

    1. There is evidence to suggest that essential hypertension is a polygenic disorder and that it arises from yet-to-be-identified predisposing variants of certain genes that influence blood pressure. The cloning of various hormone, enzyme, adrenoceptor and hormone receptor genes whose products are involved in blood pressure control and the identification of polymorphisms of these has permitted us to test their genetic association with hypertension. 2. Cross-sectional analyses of a number of candidate gene markers were performed in hypertensive and normotensive subjects who were selected on the basis of both parents being either hypertensive or normotensive, respectively, and the difference in total alleles on all chromosomes for each polymorphism between the hypertensive and normotensive groups was test by χ analysis with one degree of freedom. 3. A marked association was observed between hypertension and insertion alleles of polymorphisms of the insulin receptor gene (INSR) (P<0.0040) and the Dipeptidyl Carboxypeptidase-1 (angiotensin I-converting enzyme; kininase II) gene (DCP1) (P<0.0018). No association with hypertension was evident, however, for polymorphisms of the growth hormone, low-density lipoprotein receptor, renal kallikrein, α2- and β1-adrenoreceptor, atrial natriuretic factor and insulin genes. 4. All but one of the hypertensive subjects had at least one of the hypertension-associated alleles, and although subjects homozygous for both were three times more frequent in the hypertensive group, examination of the nine possible genotypes suggested that the INSR and DCP1 alleles are independent markers for hypertension. 5. The present results suggest that genetic variant(s) in close linkage disequilibrium with polymorphisms at INSR and DCP1 may be involved in part in the aetiology of essential hypertension.

A. Yaron - One of the best experts on this subject based on the ideXlab platform.

  • [50] Dipeptidyl Carboxypeptidase from Escherichia coli
    Methods in Enzymology, 2004
    Co-Authors: A. Yaron
    Abstract:

    Publisher Summary Dipeptidyl earboxypeptidase (DCP) from Escherichia coli (E.coli) is an intracellular enzyme, which hydrolytically removes dipeptides from the carboxyl end of low- and high-molecular-weight peptides. This chapter discusses the two methods used to monitor the enzyme purification. In the first method the assay used for monitoring the enzyme purification is based on the release of glycylproline from the carboxyl end of the sequential polypeptide Dnp(Pro-Gly-Pro), using the colorimetric ninhydrin method for quantitative determination of the dipeptide. The second method uses the following basis: the absence of interfering peptidases benzyloxycarbonyltetraalanine can be used as the substrate and the hydrolysis by DCP may be followed either by the colorimetric ninhydrin method or by the potentiometric method, using a recording pH stat. The chapter also elaborates on the Potentiometric Assay, the purification process of E.coli, purity and properties and kinetic parameters.

Andrew P. Schrader - One of the best experts on this subject based on the ideXlab platform.

  • genotypic influence on plasma Dipeptidyl Carboxypeptidase 1 activity in hypertensives
    Clinical and Experimental Pharmacology and Physiology, 1994
    Co-Authors: Brian J. Morris, J. C. Monaghan, Rose Perich, G. S. Stokes, Bruce Jackson, Andrew P. Schrader
    Abstract:

    SUMMARY 1. Plasma Dipeptidyl Carboxypeptidase-1 (DCP1; angiotensin I-converting enzyme, kininase II; EC 3.4.15.1) tracks with the deletion allele in genotypes of a 287 bp insertion/deletion (I/D) polymorphism of its gene, DCP1, in healthy Caucasian populations. The aim of the present study was to see whether genotype has a similar influence on plasma DCP1 in hypertensives. 2. The study involved 35 Caucasian patients with severe, familial essential hypertension, who were not being treated with DCP1 inhibitors, and 94 normotensives. Genotyping for the I/D polymorphism was performed by polymerase chain reaction and plasma DCP1 activity was measured by rate of hydrolysis of both [3H]-Hip-Gly-Gly and Hip-His-Leu. 3. Plasma DCP1 activity (nmol Gly-Gly/min per mL; mean ± s.e.m.) was 67 ± 2, 82 ± 4 and 91 ± 6 in II, ID and DD hypertensives, respectively, which was similar to values of 68 ± 4, 82 ± 3 and 94 ± 3 in normotensives (P= 0.0001 by one-way analysis of variance). Results for the His-Leu assay indicated similar tracking with genotype. 4. The Michaelis constant (μmol Hip-Gly-Gly/mL; mean ± s.e.m., n= 10) for DD subjects was the same as for II subjects (10.6 ± 1.6 vs 11.1 ± 2.3; P = 0.86). 5. In conclusion, in severely hypertensive Caucasian subjects, plasma DCP1 activity is subject to a similar genotypic influence in hypertensives as has been reported previously in normotensives. Furthermore, the plasma DCP1 enzyme itself appears to be functionally similar for each genotype.

  • GENOTYPIC INFLUENCE ON PLASMA Dipeptidyl Carboxypeptidase‐1 ACTIVITY IN HYPERTENSIVES
    Clinical and experimental pharmacology & physiology, 1994
    Co-Authors: Brian J. Morris, J. C. Monaghan, Rose Perich, G. S. Stokes, Bruce Jackson, Andrew P. Schrader
    Abstract:

    SUMMARY 1. Plasma Dipeptidyl Carboxypeptidase-1 (DCP1; angiotensin I-converting enzyme, kininase II; EC 3.4.15.1) tracks with the deletion allele in genotypes of a 287 bp insertion/deletion (I/D) polymorphism of its gene, DCP1, in healthy Caucasian populations. The aim of the present study was to see whether genotype has a similar influence on plasma DCP1 in hypertensives. 2. The study involved 35 Caucasian patients with severe, familial essential hypertension, who were not being treated with DCP1 inhibitors, and 94 normotensives. Genotyping for the I/D polymorphism was performed by polymerase chain reaction and plasma DCP1 activity was measured by rate of hydrolysis of both [3H]-Hip-Gly-Gly and Hip-His-Leu. 3. Plasma DCP1 activity (nmol Gly-Gly/min per mL; mean ± s.e.m.) was 67 ± 2, 82 ± 4 and 91 ± 6 in II, ID and DD hypertensives, respectively, which was similar to values of 68 ± 4, 82 ± 3 and 94 ± 3 in normotensives (P= 0.0001 by one-way analysis of variance). Results for the His-Leu assay indicated similar tracking with genotype. 4. The Michaelis constant (μmol Hip-Gly-Gly/mL; mean ± s.e.m., n= 10) for DD subjects was the same as for II subjects (10.6 ± 1.6 vs 11.1 ± 2.3; P = 0.86). 5. In conclusion, in severely hypertensive Caucasian subjects, plasma DCP1 activity is subject to a similar genotypic influence in hypertensives as has been reported previously in normotensives. Furthermore, the plasma DCP1 enzyme itself appears to be functionally similar for each genotype.

C G Miller - One of the best experts on this subject based on the ideXlab platform.

  • Cloning and nucleotide sequence of the Salmonella typhimurium dcp gene encoding Dipeptidyl Carboxypeptidase.
    Journal of bacteriology, 1992
    Co-Authors: S Hamilton, C G Miller
    Abstract:

    Plasmids carrying the Salmonella typhimurium dcp gene were isolated from a pBR328 library of Salmonella chromosomal DNA by screening for complementation of a peptide utilization defect conferred by a dcp mutation. Strains carrying these plasmids overproduced Dipeptidyl Carboxypeptidase approximately 50-fold. The nucleotide sequence of a 2.8-kb region of one of these plasmids contained an open reading frame coding for a protein of 77,269 Da, in agreement with the 80-kDa size for Dipeptidyl Carboxypeptidase (determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration). The N-terminal amino acid sequence of Dipeptidyl Carboxypeptidase purified from an overproducer strain agreed with that predicted by the nucleotide sequence. Northern (RNA) blot data indicated that dcp is not cotranscribed with other genes, and primer extension analysis showed the start of transcription to be 22 bases upstream of the translational start. The amino acid sequence of dcp was not similar to that of a mammalian Dipeptidyl Carboxypeptidase, angiotensin I-converting enzyme, but showed striking similarities to the amino acid sequence of another S. typhimurium peptidase encoded by the opdA (formerly optA) gene.

Domenico Amici - One of the best experts on this subject based on the ideXlab platform.

  • Purification and characterisation of swine serum proteinase which hydrolyses epidermal inhibitory pentapeptide.
    Biochimica et biophysica acta, 1996
    Co-Authors: Massimo Bramucci, Antonino Miano, Luana Quassinti, Ennio Maccari, Silvia Canofeni, Domenico Amici
    Abstract:

    In this paper we describe the purification to molecular homogeneity of the enzyme that cleaves the synthetic epidermal mitosis-inhibiting pentapeptide (pyroGlu-Glu-Asp-Ser-Gly; EPP) from swine serum. Biochemical characterisation of the enzyme shows a glycoprotein with apparent molecular mass of 200 kDa. The Km and Kcat values for EPP hydrolysis are 0.624 mM and 694 s-1, respectively. Use of proteinase inhibitors shows the enzyme's metalloendopeptidase character. Moreover, captopril and lisinopril prevent the cleavage of EPP. The N-terminal amino-acid sequence of the purified protein corresponds to the N-terminal amino-acid sequence of swine kidney angiotensin-converting enzyme, a Dipeptidyl Carboxypeptidase (EC 3.4.15.1).