“Coding” and “Decoding”: hypothesis for the regulatory mechanism involved in heparan sulfate biosynthesis
•Two major steps, “coding” and “decoding”, are involved in the biosynthesis of HS.•“Coding” is based on the distribution of sulfate moieties on the glucosamine.•“Code” is created by N-deacetylase/N-sulfotransferase, which has four isozymes.•C5-epimerase and O-sulfotransferases recognized the “Code”....
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| Vydáno v: | Carbohydrate research Ročník 428; s. 1 - 7 |
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| Hlavní autoři: | , , |
| Médium: | Journal Article |
| Jazyk: | angličtina |
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Elsevier Ltd
16.06.2016
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| ISSN: | 0008-6215, 1873-426X, 1873-426X |
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| Abstract | •Two major steps, “coding” and “decoding”, are involved in the biosynthesis of HS.•“Coding” is based on the distribution of sulfate moieties on the glucosamine.•“Code” is created by N-deacetylase/N-sulfotransferase, which has four isozymes.•C5-epimerase and O-sulfotransferases recognized the “Code”.•This mechanism regulates chemical structure and biological activity of HS.
Heparan sulfate (HS) is widely distributed in mammalian tissues in the form of HS proteoglycans, which play essential roles in various physiological and pathological processes. In contrast to the template-guided processes involved in the synthesis of DNA and proteins, HS biosynthesis is not believed to involve a template. However, it appears that the final structure of HS chains was strictly regulated. Herein, we report research based hypothesis that two major steps, namely “coding” and “decoding” steps, are involved in the biosynthesis of HS, which strictly regulate its chemical structure and biological activity. The “coding” process in this context is based on the distribution of sulfate moieties on the amino groups of the glucosamine residues in the HS chains. The sulfation of these amine groups is catalyzed by N-deacetylase/N-sulfotransferase, which has four isozymes. The composition and distribution of sulfate groups and iduronic acid residues on the glycan chains of HS are determined by several other modification enzymes, which can recognize these coding sequences (i.e., the “decoding” process). The degree and pattern of the sulfation and epimerization in the HS chains determines the extent of their interactions with several different protein factors, which further influences their biological activity. |
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| AbstractList | •Two major steps, “coding” and “decoding”, are involved in the biosynthesis of HS.•“Coding” is based on the distribution of sulfate moieties on the glucosamine.•“Code” is created by N-deacetylase/N-sulfotransferase, which has four isozymes.•C5-epimerase and O-sulfotransferases recognized the “Code”.•This mechanism regulates chemical structure and biological activity of HS.
Heparan sulfate (HS) is widely distributed in mammalian tissues in the form of HS proteoglycans, which play essential roles in various physiological and pathological processes. In contrast to the template-guided processes involved in the synthesis of DNA and proteins, HS biosynthesis is not believed to involve a template. However, it appears that the final structure of HS chains was strictly regulated. Herein, we report research based hypothesis that two major steps, namely “coding” and “decoding” steps, are involved in the biosynthesis of HS, which strictly regulate its chemical structure and biological activity. The “coding” process in this context is based on the distribution of sulfate moieties on the amino groups of the glucosamine residues in the HS chains. The sulfation of these amine groups is catalyzed by N-deacetylase/N-sulfotransferase, which has four isozymes. The composition and distribution of sulfate groups and iduronic acid residues on the glycan chains of HS are determined by several other modification enzymes, which can recognize these coding sequences (i.e., the “decoding” process). The degree and pattern of the sulfation and epimerization in the HS chains determines the extent of their interactions with several different protein factors, which further influences their biological activity. Heparan sulfate (HS) is widely distributed in mammalian tissues in the form of HS proteoglycans, which play essential roles in various physiological and pathological processes. In contrast to the template-guided processes involved in the synthesis of DNA and proteins, HS biosynthesis is not believed to involve a template. However, it appears that the final structure of HS chains was strictly regulated. Herein, we report research based hypothesis that two major steps, namely "coding" and "decoding" steps, are involved in the biosynthesis of HS, which strictly regulate its chemical structure and biological activity. The "coding" process in this context is based on the distribution of sulfate moieties on the amino groups of the glucosamine residues in the HS chains. The sulfation of these amine groups is catalyzed by N-deacetylase/N-sulfotransferase, which has four isozymes. The composition and distribution of sulfate groups and iduronic acid residues on the glycan chains of HS are determined by several other modification enzymes, which can recognize these coding sequences (i.e., the "decoding" process). The degree and pattern of the sulfation and epimerization in the HS chains determines the extent of their interactions with several different protein factors, which further influences their biological activity.Heparan sulfate (HS) is widely distributed in mammalian tissues in the form of HS proteoglycans, which play essential roles in various physiological and pathological processes. In contrast to the template-guided processes involved in the synthesis of DNA and proteins, HS biosynthesis is not believed to involve a template. However, it appears that the final structure of HS chains was strictly regulated. Herein, we report research based hypothesis that two major steps, namely "coding" and "decoding" steps, are involved in the biosynthesis of HS, which strictly regulate its chemical structure and biological activity. The "coding" process in this context is based on the distribution of sulfate moieties on the amino groups of the glucosamine residues in the HS chains. The sulfation of these amine groups is catalyzed by N-deacetylase/N-sulfotransferase, which has four isozymes. The composition and distribution of sulfate groups and iduronic acid residues on the glycan chains of HS are determined by several other modification enzymes, which can recognize these coding sequences (i.e., the "decoding" process). The degree and pattern of the sulfation and epimerization in the HS chains determines the extent of their interactions with several different protein factors, which further influences their biological activity. Heparan sulfate (HS) is widely distributed in mammalian tissues in the form of HS proteoglycans, which play essential roles in various physiological and pathological processes. In contrast to the template-guided processes involved in the synthesis of DNA and proteins, HS biosynthesis is not believed to involve a template. However, it appears that the final structure of HS chains was strictly regulated. Herein, we report research based hypothesis that two major steps, namely “coding” and “decoding” steps, are involved in the biosynthesis of HS, which strictly regulate its chemical structure and biological activity. The “coding” process in this context is based on the distribution of sulfate moieties on the amino groups of the glucosamine residues in the HS chains. The sulfation of these amine groups is catalyzed by N-deacetylase/N-sulfotransferase, which has four isozymes. The composition and distribution of sulfate groups and iduronic acid residues on the glycan chains of HS are determined by several other modification enzymes, which can recognize these coding sequences (i.e., the “decoding” process). The degree and pattern of the sulfation and epimerization in the HS chains determines the extent of their interactions with several different protein factors, which further influences their biological activity. |
| Author | Wang, Fengshan Zhang, Xu Sheng, Juzheng |
| Author_xml | – sequence: 1 givenname: Xu surname: Zhang fullname: Zhang, Xu organization: Key Laboratory of Chemical Biology of Natural Products (Ministry of Education), Institute of Biochemical and Biotechnological Drugs, School of Pharmaceutical Sciences, Shandong University, Jinan 250012, China – sequence: 2 givenname: Fengshan surname: Wang fullname: Wang, Fengshan email: fswang@sdu.edu.cn organization: Key Laboratory of Chemical Biology of Natural Products (Ministry of Education), Institute of Biochemical and Biotechnological Drugs, School of Pharmaceutical Sciences, Shandong University, Jinan 250012, China – sequence: 3 givenname: Juzheng orcidid: 0000-0003-2856-9162 surname: Sheng fullname: Sheng, Juzheng email: shengjuzheng@sdu.edu.cn organization: Key Laboratory of Chemical Biology of Natural Products (Ministry of Education), Institute of Biochemical and Biotechnological Drugs, School of Pharmaceutical Sciences, Shandong University, Jinan 250012, China |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/27088396$$D View this record in MEDLINE/PubMed |
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| Keywords | Heparan sulfate C5-epimerase N-deacetylase/N-sulfotransferase O-sulfotransferase Biosynthesis mechanism |
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| Snippet | •Two major steps, “coding” and “decoding”, are involved in the biosynthesis of HS.•“Coding” is based on the distribution of sulfate moieties on the... Heparan sulfate (HS) is widely distributed in mammalian tissues in the form of HS proteoglycans, which play essential roles in various physiological and... |
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| SubjectTerms | Animals bioactive properties Biocatalysis biosynthesis Biosynthesis mechanism Biosynthetic Pathways C5-epimerase DNA enzymes glucosamine Glucosamine - chemistry Heparan sulfate Heparitin Sulfate - biosynthesis Heparitin Sulfate - chemistry Humans Isoenzymes - metabolism isozymes mammals Molecular Structure N-deacetylase/N-sulfotransferase O-sulfotransferase proteoglycans sulfates Sulfotransferases - metabolism |
| Title | “Coding” and “Decoding”: hypothesis for the regulatory mechanism involved in heparan sulfate biosynthesis |
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