Heparan sulfate biosynthesis: methods for investigation of the heparanosome

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Heparan sulfate biosynthesis : methods for investigation of the heparanosome. / Multhaupt, Hinke A B; Couchman, John R.

In: Journal of Histochemistry and Cytochemistry, Vol. 60, No. 12, 12.2012, p. 908-15.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Multhaupt, HAB & Couchman, JR 2012, 'Heparan sulfate biosynthesis: methods for investigation of the heparanosome', Journal of Histochemistry and Cytochemistry, vol. 60, no. 12, pp. 908-15. https://doi.org/10.1369/0022155412460056

APA

Multhaupt, H. A. B., & Couchman, J. R. (2012). Heparan sulfate biosynthesis: methods for investigation of the heparanosome. Journal of Histochemistry and Cytochemistry, 60(12), 908-15. https://doi.org/10.1369/0022155412460056

Vancouver

Multhaupt HAB, Couchman JR. Heparan sulfate biosynthesis: methods for investigation of the heparanosome. Journal of Histochemistry and Cytochemistry. 2012 Dec;60(12):908-15. https://doi.org/10.1369/0022155412460056

Author

Multhaupt, Hinke A B ; Couchman, John R. / Heparan sulfate biosynthesis : methods for investigation of the heparanosome. In: Journal of Histochemistry and Cytochemistry. 2012 ; Vol. 60, No. 12. pp. 908-15.

Bibtex

@article{477020277e994ac7abcf3fa056277bb9,
title = "Heparan sulfate biosynthesis: methods for investigation of the heparanosome",
abstract = "Heparan sulfate is perhaps the most complex polysaccharide known from animals. The basic repeating disaccharide is extensively modified by sulfation and uronic acid epimerization. Despite this, the fine structure of heparan sulfate is remarkably consistent with a particular cell type. This suggests that the synthesis of heparan sulfate is tightly controlled. Although genomics has identified the enzymes involved in glycosaminoglycan synthesis in a number of vertebrates and invertebrates, the regulation of the process is not understood. Moreover, the localization of the various enzymes in the Golgi apparatus has not been carried out in a detailed way using high-resolution microscopy. We have begun this process, using well-known markers for the various Golgi compartments, coupled with the use of characterized antibodies and cDNA expression. Laser scanning confocal microscopy coupled with line scanning provides high-quality resolution of the distribution of enzymes. The EXT2 protein, which when combined as heterodimers with EXT1 comprises the major polymerase in heparan sulfate synthesis, has been studied in depth. All the data are consistent with a cis-Golgi distribution and provide a starting point to establish whether all the enzymes are clustered in a multimolecular complex or are distributed through the various compartments of the Golgi apparatus.",
keywords = "Animals, Endoplasmic Reticulum, Golgi Apparatus, Heparitin Sulfate, Humans, Immunohistochemistry, Microscopy, Confocal, Multienzyme Complexes",
author = "Multhaupt, {Hinke A B} and Couchman, {John R}",
year = "2012",
month = dec,
doi = "10.1369/0022155412460056",
language = "English",
volume = "60",
pages = "908--15",
journal = "Journal of Histochemistry and Cytochemistry",
issn = "0022-1554",
publisher = "SAGE Publications",
number = "12",

}

RIS

TY - JOUR

T1 - Heparan sulfate biosynthesis

T2 - methods for investigation of the heparanosome

AU - Multhaupt, Hinke A B

AU - Couchman, John R

PY - 2012/12

Y1 - 2012/12

N2 - Heparan sulfate is perhaps the most complex polysaccharide known from animals. The basic repeating disaccharide is extensively modified by sulfation and uronic acid epimerization. Despite this, the fine structure of heparan sulfate is remarkably consistent with a particular cell type. This suggests that the synthesis of heparan sulfate is tightly controlled. Although genomics has identified the enzymes involved in glycosaminoglycan synthesis in a number of vertebrates and invertebrates, the regulation of the process is not understood. Moreover, the localization of the various enzymes in the Golgi apparatus has not been carried out in a detailed way using high-resolution microscopy. We have begun this process, using well-known markers for the various Golgi compartments, coupled with the use of characterized antibodies and cDNA expression. Laser scanning confocal microscopy coupled with line scanning provides high-quality resolution of the distribution of enzymes. The EXT2 protein, which when combined as heterodimers with EXT1 comprises the major polymerase in heparan sulfate synthesis, has been studied in depth. All the data are consistent with a cis-Golgi distribution and provide a starting point to establish whether all the enzymes are clustered in a multimolecular complex or are distributed through the various compartments of the Golgi apparatus.

AB - Heparan sulfate is perhaps the most complex polysaccharide known from animals. The basic repeating disaccharide is extensively modified by sulfation and uronic acid epimerization. Despite this, the fine structure of heparan sulfate is remarkably consistent with a particular cell type. This suggests that the synthesis of heparan sulfate is tightly controlled. Although genomics has identified the enzymes involved in glycosaminoglycan synthesis in a number of vertebrates and invertebrates, the regulation of the process is not understood. Moreover, the localization of the various enzymes in the Golgi apparatus has not been carried out in a detailed way using high-resolution microscopy. We have begun this process, using well-known markers for the various Golgi compartments, coupled with the use of characterized antibodies and cDNA expression. Laser scanning confocal microscopy coupled with line scanning provides high-quality resolution of the distribution of enzymes. The EXT2 protein, which when combined as heterodimers with EXT1 comprises the major polymerase in heparan sulfate synthesis, has been studied in depth. All the data are consistent with a cis-Golgi distribution and provide a starting point to establish whether all the enzymes are clustered in a multimolecular complex or are distributed through the various compartments of the Golgi apparatus.

KW - Animals

KW - Endoplasmic Reticulum

KW - Golgi Apparatus

KW - Heparitin Sulfate

KW - Humans

KW - Immunohistochemistry

KW - Microscopy, Confocal

KW - Multienzyme Complexes

U2 - 10.1369/0022155412460056

DO - 10.1369/0022155412460056

M3 - Journal article

C2 - 22899865

VL - 60

SP - 908

EP - 915

JO - Journal of Histochemistry and Cytochemistry

JF - Journal of Histochemistry and Cytochemistry

SN - 0022-1554

IS - 12

ER -

ID: 49106613