GGDB:

CHST8 encodes carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 8. This enzyme has the activity to transfer sulfate to the 4-position of GalNAc at the non-reducing end of N-linked and O-linked glycans. Sulfated GalNAc is a characteristic structure present in glycoprotein hormones such as LH and TSH secreted from the pituitary gland, and functions in the clearance of the hormone from the blood. The CHST8 gene is expressed in the pituitary gland, and mice lacking the gene have increased levels of LH in their blood, resulting in premature aging. In humans, there are two isoenzymes （CHST8 and CHST9）.

Keyword: LacdiNAc , glycoprotein hormone , sulfotransferase

Sulfotransferases

GGDB Symbol

CHST8 Alias

Designation

N-acetylgalactosamine-4-O-sulfotransferase

Organism

Homo sapiens

GeneID

64377

HGNC

CHST8 (15993)

mRNA

NM_022467

map

19q13.1

Protein

NP_071912

EC#

2.8.2.7

CAZy

GlyCosmos Glycogenes

CHST8

OMIM

610190

Disease name

GDGDB

Human Protein Atlas

ENSG00000124302

Mus musculus

mRNA	NM_175140
Protein	NP_780349
MGI	52927

Rattus norvegicus

mRNA	XM_218506
Protein	XP_218506

J. Biol. Chem. 2000-12-01 ;275(49):38402-9.

Molecular cloning and expression of the pituitary glycoprotein hormone N-acetylgalactosamine-4-O-sulfotransferase.

Xia G. et al. PMID:10988300 Refer to: TABLE I

DONOR : PAPS

Glc	Man	Gal	GlcNAc	GalNAc	Fuc	Xyl	Neu5Ac	Neu5Gc	GlcA	IdoA	GlcN

Substrate Transferred

	JCGG-STR029199 GlyTouCan: G71793UG GlyCosmos Glycans: G71793UG	PAPS	JCGG-STR029465 GlyTouCan: G00547ZN GlyCosmos Glycans: G00547ZN

table 1
Glycoprotein	Enzyme activity
Chondroitin	30

J. Biol. Chem. 2001-04-01 ;276(14):10861-9.

Molecular cloning and expression of an N-acetylgalactosamine-4-O-sulfotransferase that transfers sulfate to terminal and non-terminal beta 1,4-linked N-acetylgalactosamine.

Kang HG. et al. PMID:11139592

DONOR : PAPS

Glc	Man	Gal	GlcNAc	GalNAc	Fuc	Xyl	Neu5Ac	Neu5Gc	GlcA	IdoA	GlcN

Substrate Transferred

	JCGG-STR029533 GlyTouCan: G00057MO GlyCosmos Glycans: G00057MO	PAPS	JCGG-STR007477 GlyTouCan: G33129LQ GlyCosmos Glycans: G33129LQ

table 1
Glycoprotein	Enzyme activity
[IdUA(a1-3)GalNAc(b1-4)]n	0
GlcA(b1-3)Gal(b1-4)	0

J. Biol. Chem. 2001-06-01 ;11(6):495-504.

Molecular cloning and expression of two distinct human N-acetylgalactosamine 4-O-sulfotransferases that transfer sulfate to GalNAc beta 1-->4GlcNAc beta 1-->R in both N- and O-glycans.

Hiraoka N. et al. PMID:11445554

J. Biol. Chem. 2002-09-01 ;277(38):34766-72.

Molecular cloning and characterization of chondroitin-4-O-sulfotransferase-3. A novel member of the HNK-1 family of sulfotransferases.

Kang HG. et al. PMID:12080076 Refer to: TABLE I

DONOR : PAPS

Glc	Man	Gal	GlcNAc	GalNAc	Fuc	Xyl	Neu5Ac	Neu5Gc	GlcA	IdoA	GlcN

Substrate Transferred

	JCGG-STR029199 GlyTouCan: G71793UG GlyCosmos Glycans: G71793UG	PAPS	JCGG-STR029465 GlyTouCan: G00547ZN GlyCosmos Glycans: G00547ZN

table 1
Glycoprotein	Enzyme activity
Chondroitin	73
Dermatan	52

J. Biol. Chem. 2005-12-01 ;15(12):1349-58.

Differential expression and enzymatic properties of GalNAc-4-sulfotransferase-1 and GalNAc-4-sulfotransferase-2.

Boregowda RK. et al. PMID:16079414

RNA Expression from Human Protein Atlas

This RNA expression data uses "HPA data" from the Human Protein Atlas. Tissue RNA Expression

data available from v22.proteinatlas.org

J. Biol. Chem. 2000-12-01 ;275(49):38402-9.

Molecular cloning and expression of the pituitary glycoprotein hormone N-acetylgalactosamine-4-O-sulfotransferase.

Xia G. et al. PMID:10988300

Glycobiology 2000-12-01 ;275(51):40605-13.

Molecular cloning and characterization of GalNAc 4-sulfotransferase expressed in human pituitary gland.

Okuda T. et al. PMID:11001942

J. Biol. Chem. 2001-06-01 ;11(6):495-504.

Molecular cloning and expression of two distinct human N-acetylgalactosamine 4-O-sulfotransferases that transfer sulfate to GalNAc beta 1-->4GlcNAc beta 1-->R in both N- and O-glycans.

Hiraoka N. et al. PMID:11445554

J. Biol. Chem. 2005-12-01 ;15(12):1349-58.

Differential expression and enzymatic properties of GalNAc-4-sulfotransferase-1 and GalNAc-4-sulfotransferase-2.

Boregowda RK. et al. PMID:16079414

adrenal glandsatriumbrainfetal brainheartliverlunglymph nodemammary glandpancreasprostatespleentestistrachea

Provided by GOA

Function
N-acetylgalactosamine 4-O-sulfotransferase activity

Process
carbohydrate biosynthetic process
central nervous system development
hormone biosynthetic process
proteoglycan biosynthetic process
sulfur compound metabolic process

Component
Golgi membrane
integral component of membrane

CHST8

Sulfotransferases

Orthologous Gene

Mus musculus

Rattus norvegicus

Acceptor Substrates (Reference)

Molecular cloning and expression of the pituitary glycoprotein hormone N-acetylgalactosamine-4-O-sulfotransferase.

DONOR : PAPS

Substrate Transferred

Molecular cloning and expression of an N-acetylgalactosamine-4-O-sulfotransferase that transfers sulfate to terminal and non-terminal beta 1,4-linked N-acetylgalactosamine.

DONOR : PAPS

Substrate Transferred

Molecular cloning and expression of two distinct human N-acetylgalactosamine 4-O-sulfotransferases that transfer sulfate to GalNAc beta 1-->4GlcNAc beta 1-->R in both N- and O-glycans.

Molecular cloning and characterization of chondroitin-4-O-sulfotransferase-3. A novel member of the HNK-1 family of sulfotransferases.

DONOR : PAPS

Substrate Transferred

Differential expression and enzymatic properties of GalNAc-4-sulfotransferase-1 and GalNAc-4-sulfotransferase-2.

Acceptor Substrates (KEM-C)

Expression

Expression (Reference)

Molecular cloning and expression of the pituitary glycoprotein hormone N-acetylgalactosamine-4-O-sulfotransferase.

Molecular cloning and characterization of GalNAc 4-sulfotransferase expressed in human pituitary gland.

Molecular cloning and expression of two distinct human N-acetylgalactosamine 4-O-sulfotransferases that transfer sulfate to GalNAc beta 1-->4GlcNAc beta 1-->R in both N- and O-glycans.

Differential expression and enzymatic properties of GalNAc-4-sulfotransferase-1 and GalNAc-4-sulfotransferase-2.

Gene Ontology