Literature DB >> 3663708

Amino acid sulfur as a source of sulfate for sulfated proteoglycans produced by Swiss mouse 3T3 cells.

J M Keller1, K M Keller.   

Abstract

The uptake of sulfate by Swiss mouse 3T3 cells is blocked in the presence of 1 mM 4-isothiocyano-4'-acetamido-stilbene-2,2-disulfonic acid (SITS). In the absence of an exogenous source of sulfate, glycosaminoglycans produced by cells in the presence of the inhibitor are sulfated to the same extent as those produced by cells grown in its absence. The sulfate utilized in the absence of medium sulfate has been identified as that produced by the oxidation of the sulfur present in the amino acids cysteine and methionine. This finding indicates that, under conditions of restricted exogenous sulfate, caution is needed in the interpretation of data obtained with the use of [35S]methionine and/or [35S]cysteine as a general protein label, since both tyrosine and a variety of types of protein-linked carbohydrate chains may be modified by sulfation.

Entities:  

Mesh:

Substances:

Year:  1987        PMID: 3663708     DOI: 10.1016/0304-4165(87)90230-3

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  Heparin-binding EGF-like growth factor stimulation of smooth muscle cell migration: dependence on interactions with cell surface heparan sulfate.

Authors:  S Higashiyama; J A Abraham; M Klagsbrun
Journal:  J Cell Biol       Date:  1993-08       Impact factor: 10.539

2.  In vivo contribution of amino acid sulfur to cartilage proteoglycan sulfation.

Authors:  Fabio Pecora; Benedetta Gualeni; Antonella Forlino; Andrea Superti-Furga; Ruggero Tenni; Giuseppe Cetta; Antonio Rossi
Journal:  Biochem J       Date:  2006-09-15       Impact factor: 3.857

3.  Repression of myogenic differentiation by aFGF, bFGF, and K-FGF is dependent on cellular heparan sulfate.

Authors:  B B Olwin; A Rapraeger
Journal:  J Cell Biol       Date:  1992-08       Impact factor: 10.539

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.