Characterization of Bovine Heart Sulfotransferase Catalyzing the Sulfation of Tyrosine-Containing Peptides.

Suiko, Masahito; Fernando, P. H. Prasantha; Sakakibara, Yoichi; Kudo, Hisao; Nakamura, Toyohiko; Liu, Ming‐Cheh

doi:10.3177/jnsv.43.485

Cited by 4 publications

(2 citation statements)

References 17 publications

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“…Previous kinetic studies on tyrosylprotein sulfotransferases involved the use of lysates from cultured cells or tissues as the enzyme source that almost certainly contained a mixture of the two isozymes [20; 32; 44–50]. Individual kinetic analysis of the two TPST isozymes became possible after the purification and cloning of TPST-1 and TPST-2 10 years ago.…”

Section: Discussionmentioning

confidence: 99%

Mass spectrometric kinetic analysis of human tyrosylprotein sulfotransferase-1 and -2

Danan

Hoffhines

et al. 2008

J. Am. Soc. Mass Spectrom.

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Protein tyrosine O-sulfation, a widespread post-translational modification, is mediated by two Golgi enzymes, tyrosylprotein sulfotransferase-1 and Ϫ2. These enzymes catalyze the transfer of sulfate from the universal sulfate donor 3=-phosphoadenosine-5=-phosphosulfate (PAPS) to the hydroxyl group of tyrosine residues to form tyrosine O-sulfate ester and PAP. More than 60 proteins have been identified to be tyrosine sulfated including several G protein-coupled receptors, such as CC-chemokine receptor 8 (CCR8) that is implicated in allergic inflammation, asthma, and atherogenesis. However, the kinetic properties of purified tyrosylprotein sulfotransferase (TPST)-1 and Ϫ2 have not been previously reported. Moreover, currently there is no available quantitative TPST assay that can directly monitor individual sulfation of a series of tyrosine residues, which is present in most known substrates. We chose an MS-approach to address this limitation. In this study, a liquid chromatography electrospray ionisation mass spectrometry (LC/ESI-MS)-based TPST assay was developed to determine the kinetic parameters of individual TPSTs and a mixture of both isozymes using CCR8 peptides as substrates that have three tyrosine residues in series. Our method can differentiate between mono-and disulfated products, and our results show that the K m,app for the monosulfated substrate was 5-fold less than the nonsulfated substrate. The development of this method is the initial step in the investigation of kinetic parameters of the sequential tyrosine sulfation of chemokine receptors by TPSTs and in determining its catalytic mechanism. (J

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Section: Discussionmentioning

confidence: 99%

Mass spectrometric kinetic analysis of human tyrosylprotein sulfotransferase-1 and -2

Danan

Hoffhines

et al. 2008

J. Am. Soc. Mass Spectrom.

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“…PTS was initially demonstrated in cell lysate from rat pheochromocytoma PC12 cells [ 19 ]. After that, TPST activities have been characterized in numerous cell lines and tissues, including mammalian tissues such as bovine adrenal medulla [ 20 ] and heart [ 21 ], rat brain [ 22 ], liver [ 23 , 24 , 25 ], gastric mucosa [ 26 ], and submandibular salivary glands [ 27 , 28 ], human liver [ 29 , 30 ], gastric mucosa [ 31 ], saliva [ 32 ], and platelets [ 33 ]. Human TPST mRNA expression level was analyzed in various human tissues (adrenal gland, bone marrow, brain, colon, heart, kidney, liver, lung, pancreas, peripheral leukocytes, placenta, prostate, salivary gland, skeletal muscle, small intestine, spinal cord, spleen, stomach, testis, thymus, thyroid gland, trachea, and uterus) by real-time reverse transcription PCR [ 34 ].…”

Section: Tpst Sources and Its Preparation: Enzyme Preparations Sementioning

confidence: 99%

Tyrosine Sulfation as a Protein Post-Translational Modification

et al. 2015

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Integration of inorganic sulfate into biological molecules plays an important role in biological systems and is directly involved in the instigation of diseases. Protein tyrosine sulfation (PTS) is a common post-translational modification that was first reported in the literature fifty years ago. However, the significance of PTS under physiological conditions and its link to diseases have just begun to be appreciated in recent years. PTS is catalyzed by tyrosylprotein sulfotransferase (TPST) through transfer of an activated sulfate from 3'-phosphoadenosine-5'-phosphosulfate to tyrosine in a variety of proteins and peptides. Currently, only a small fraction of sulfated proteins is known and the understanding of the biological sulfation mechanisms is still in progress. In this review, we give an introductory and selective brief review of PTS and then summarize the basic biochemical information including the activity and the preparation of TPST, methods for the determination of PTS, and kinetics and reaction mechanism of TPST. This information is fundamental for the further exploration of the function of PTS that induces protein-protein interactions and the subsequent biochemical and physiological reactions.

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Differential Enzymatic Characteristics and Tissue-Specific Expression of Human TPST-1 and TPST-2

Mishiro

Sakakibara²,

Liu³

et al. 2006

The Journal of Biochemistry

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Protein tyrosine sulfation is emerging as a widespread post-translational modification in multicellular eukaryotes. The responsible enzyme, named tyrosylprotein sulfotransferase (TPST), catalyzes the sulfate transfer from 3'-phosphoadenosine 5'-phosphosulfate to tyrosine residues of proteins. Two distinct TPSTs, designated TPST-1 and TPST-2, had previously been identified. In the present study, we cloned human TPST-1 and TPST-2 expressed and characterized the recombinant enzymes using peptide substrates. These enzymes displayed distinct acidic pH optima and stimulatory effects of Mn(2+). Additionally, the activity of TPST-2, but not TPST-1, was stimulated in the presence of Mg(2+). Compared with TPST-2, TPST-1 displayed considerably lower K(m) and V(max) for the majority of the tested peptide substrates, implying their differential substrate specificity. Quantitative real-time PCR analysis showed that although the two TPSTs were co-expressed in all 20 human tissues examined, the levels of expression of TPST-1 and TPST-2 varied significantly among different tissues. These latter findings may imply distinct physiological functions of TPST-1 and TPST-2.

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Characterization of Bovine Heart Sulfotransferase Catalyzing the Sulfation of Tyrosine-Containing Peptides.

Cited by 4 publications

References 17 publications

Mass spectrometric kinetic analysis of human tyrosylprotein sulfotransferase-1 and -2

Mass spectrometric kinetic analysis of human tyrosylprotein sulfotransferase-1 and -2

Tyrosine Sulfation as a Protein Post-Translational Modification

Differential Enzymatic Characteristics and Tissue-Specific Expression of Human TPST-1 and TPST-2

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