Apparent identity of cerebral tyrosylsulfotransferase activities using either a cholecystokinin derivative or an acidic amino acid polymer as substrate

Vargas, Froylan; Schwartz, Jean‐Charles

doi:10.1016/0014-5793(87)81443-6

Cited by 19 publications

(5 citation statements)

References 14 publications

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“…Tyrosylsulphotransferase activities require acidic residues immediately to the N-terminus of the putative sulphation site (Hortin, Folz, Gordon & Strauss, 1986;Vargas & Schwartz, 1987). In proCCK there are two tyrosines in the C-terminal flanking peptide, and in both instances they are in a configuration that is appropriate for sulphation.…”

Section: Biosynthetic Mechanismsmentioning

confidence: 99%

The G. L. Brown Lecture Regulatory Peptides and the Neuroendocrinology of Gut‐brain Relations

Dockray

1988

Exp Physiol

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Section: Biosynthetic Mechanismsmentioning

confidence: 99%

The G. L. Brown Lecture Regulatory Peptides and the Neuroendocrinology of Gut‐brain Relations

Dockray

1988

Exp Physiol

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“…The two enzymes may well be identical (Vargas & Schwartz, 1987), and perhaps this sulphotransferase, or a family of closely related enzymes, is widespread.…”

Section: Prosthetic Modificationsmentioning

confidence: 99%

Post‐translational Modification of Peptide Messengers in the Gut

Dimaline

1988

Exp Physiol

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Classical methods such as precursor isolation, cell-free translation and pulse-chase experiments have been of limited use in studying biosynthesis of gastrointestinal peptides, because cell populations are generally sparse and intermingled with other cell types, rates of peptide turnover are low, and levels of mRNA are generally low. However, with the advent of recombinant DNA technology, and its application in predicting precursor sequences, the opportunity has arisen for an alternative approach to the study of propeptides. The success of this approach has to some extent resulted in the eclipse of studies of post-translational processing, although they are still of considerable physiological importance. Study of gastrointestinal peptides is proving a fruitful source of information about the mechanisms involved, as is now clear from recent work on the precursors for gastrin, cholecystokinin (CCK) and vasoactive intestinal peptide (VIP).This review will focus upon these three precursors to illustrate the important features and the physiological significance of post-translational processing, and to outline the strategies currently used to identify the structural modifications which take place in the synthesis of the peptides. Examples will also be drawn where appropriate from other precursors.

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“…The enzymatic activity mediating the sulfation of proteins in PC12 cell was stimulated by the presence of Mg 2+ and Mn 2+ and inhibited by EDTA 14. Both Mn 2+ and Mg 2+ were equally effective in activating EAY sulfation by bovine adrenal medulla 14 and rat cerebral cortex 16, where as Mn 2+ and Co 2+ stimulated rat liver tyrosylprotein sulfotrasferase 15. In contrast, sulfation of an endogenous membrane protein in A431 cell was not inhibited by EDTA 25.…”

Section: Discussionmentioning

confidence: 97%

“…Tyrosylprotein sulfotransferase has been identified in numerous tissues including bovine adrenal medulla 14 , rat liver 15 , brain 16 , gastric mucosa 17 , submandibular salivary glands 18 and platelets 19 . In this study, we demonstrate for the first time the detection, isolation and characterization of TPST from human saliva.…”

Section: Introductionmentioning

confidence: 99%

Identification and Characterization of Tyrosylprotein Sulfotransferase from Human Saliva

Kasinathan¹,

Ramaprasad²,

Sundaram³

2005

Int. J. Biol. Sci.

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Tyrosylprotein sulfotransferase (TPST), the enzyme responsible for the sulfation of tyrosine residues, has been identified and characterized in submandibular salivary glands previously . Tyrosylprotein sulfotransferase catalyses the sulfation of a variety of secretory and membrane proteins and is believed to be present only in the cell. In the present study, this enzyme was identified for the first time in human saliva. Analysis of human saliva and parotid saliva for the presence of tyrosylprotein sulfotransferase revealed tyrosine sulfating activity displayed by both whole saliva and parotid saliva at pH optimum of 6.8. In contrast to tyrosylprotein sulfotransferase isolated from submandibular salivary glands, salivary enzyme does not require the presence of Triton X-100, NaF and 5'AMP for maximal activity. Similar to the submandibular TPST, the enzyme from saliva also required MnCl 2 for its activity. Maximum TPST activity was observed at 20mM MnCl 2 . The enzyme from saliva was immunoprecipitated and purified by immunoaffinity column using anti-TPST antibody. Affinity purified salivary TPST showed a single band of 50-54 kDa. This study is the first report characterizing a tyrosylprotein sulfotransferase in a secretory fluid.

show abstract

Apparent identity of cerebral tyrosylsulfotransferase activities using either a cholecystokinin derivative or an acidic amino acid polymer as substrate

Cited by 19 publications

References 14 publications

The G. L. Brown Lecture Regulatory Peptides and the Neuroendocrinology of Gut‐brain Relations

The G. L. Brown Lecture Regulatory Peptides and the Neuroendocrinology of Gut‐brain Relations

Post‐translational Modification of Peptide Messengers in the Gut

Identification and Characterization of Tyrosylprotein Sulfotransferase from Human Saliva

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