XYLT1

XYLT1
Identifiers
Aliases	XYLT1, DBQD2, PXT-I, XT1, XTI, XYLTI, xylT-I, xylosyltransferase 1
External IDs	OMIM: 608124 MGI: 2451073 HomoloGene: 32534 GeneCards: XYLT1
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16p12.3 Start 17,101,769 bp[1] End 17,470,960 bp[1]
Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7|7 F1 Start 116,980,214 bp[2] End 117,272,803 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tibia hair follicle Region I of hippocampus proper synovial joint retinal pigment epithelium entorhinal cortex Brodmann area 23 orbitofrontal cortex palpebral conjunctiva superior frontal gyrus Top expressed in subiculum primary motor cortex retinal pigment epithelium ventromedial nucleus cingulate gyrus paraventricular nucleus of hypothalamus mammillary body lateral hypothalamus medial vestibular nucleus globus pallidus More reference expression data BioGPS n/a
Gene ontology Molecular function protein xylosyltransferase activity transferase activity acetylglucosaminyltransferase activity glycosyltransferase activity metal ion binding Cellular component integral component of membrane extracellular region Golgi apparatus endoplasmic reticulum membrane endoplasmic reticulum membrane Golgi membrane Golgi cis cisterna extracellular space Biological process chondroitin sulfate biosynthetic process heparan sulfate proteoglycan biosynthetic process glycosaminoglycan biosynthetic process glycosaminoglycan metabolic process proteoglycan biosynthetic process ossification involved in bone maturation embryonic skeletal system development chondroitin sulfate proteoglycan biosynthetic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 64131 233781 Ensembl ENSG00000103489 ENSG00000285395 ENSMUSG00000030657 UniProt Q86Y38 Q811B1 RefSeq (mRNA) NM_022166 NM_175645 RefSeq (protein) NP_071449 NP_783576 Location (UCSC) Chr 16: 17.1 – 17.47 Mb Chr 7: 116.98 – 117.27 Mb PubMed search [3] [4]
Wikidata
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Xylosyltransferase 1 is an enzyme that in humans is encoded by the XYLT1 gene.^[5][6]

Xylosyltransferase (XT; EC 2.4.2.26) catalyzes the transfer of UDP-xylose to serine residues within XT recognition sequences of target proteins. Addition of this xylose to the core protein is required for the biosynthesis of the glycosaminoglycan chains characteristic of proteoglycans.[supplied by OMIM]^[6]

Clinical relevance

Baratela-Scott syndrome

In 2012 Baratela-Scott syndrome was identified in humans.^[7] A GGC repeat expansion, and methylation of exon 1 of XYLT1 is a common pathogenic variant in Baratela-Scott syndrome.^[8]

Patients with Bartarlla-Scott syndrome exhibit abnormal development of the skeleton, characteristic facial features, and cognitive developmental delay. Skeletal problems include knee cap in the wrong position, short long bones with mild changes to the narrow portion, short palm bones with stub thumbs, short thigh necks, shallow hip sockets, and malformations of the spine. Characteristic facial features include a flattened midface with a broad nasal bridge, cleft palate, and unibrow. The syndrome also cause pre-school onset of a cognitive developmental delay, with a shortened attention span. Some of the cognitive delay is masked by a warm and engaging personality.

Axon extension

Neurons use the presence of extracellular matrix molecules as clues whether to promote or suppress extension of axons. Chondroitin sulfate proteoglycans suppress the extension of axons over the glial scar, a barrier which develops after lesioning the spinal cord. Proteoglycans consist of one relatively small protein core and attached large glycosaminoglycan side chains. To block the very formation of these side chains xylosyltransferase (XYLT1) which attaches xylose to a serine of the protein core as initiation for glycosaminoglycan chain extension, was targeted by a class of designed DNA molecules. These molecules are called DNA-enzymes which were designed to specifically cleave XYLT1 mRNA within cells. DNA-enzymes are readily taken up by mammalian cells, but are more stable and require much lower concentrations then siRNA. XTYL1 DNA-enzyme in co-cultures of neurons with neurocan secreting cells displayed a marked increase of axon outgrowth. Rats with defined spinal cord lesions, i.a. the clinically relevant contusion injury, treated with XTYL1 DNA-enzyme administered by micro-infusion pumps or systemically achieved improvements in the horizontal ladder task, enhanced axonal plasticity, growth of the corticospinal tract, no effect on neuropathic pain when using mechanical and thermal allodynia tests and no toxicological or pathological side effects compared to control animals.{{Oudega M, Chao OY, Avison DL, Bronson RT, Buchser WJ, Hurtado A, Grimpe B. (2012) Systemic administration of a deoxyribozyme to xylosyltransferase-1 mRNA promotes recovery after a spinal cord injury Exp Neurol. Sep;237(1):170-9. doi: 10.1016/j.expneurol.2012.06.006. PMID: 22721770}}

References

Further reading