High impact information on EPYC

• There are 14 potential binding sites for SOX9, a transcription factor present in cartilage, in the promoter, and in the first intron of DSPG3 [1].
• In this study, we have determined that the human DSPG3 gene is composed of seven exons: Exon 2 of DSPG3 includes the start codon, exons 4-7 code for the leucine-rich repeats, exons 3 and 7 contain the potential glycosaminoglycan attachment sites, and exon 7 contains the potential N-glycosylation sites and the stop codon [1].
• In contrast to the tissue distribution of the other SLRPs, DSPG3 is predominantly expressed in cartilage [1].
• Analysis of 1.6 kb of upstream promoter sequence of DSPG3 reveals three TATA boxes, one of which is 20 nucleotides before the transcription start site [1].
• After Sepharose CL-4B chromatography, newly synthesized scleral proteoglycans isolated from normal, form-deprived, and contralateral control eyes, resolved into one major peak that eluted in the position of decorin, a small chondroitin-dermatan sulfate proteoglycan [2].

Biological context of EPYC

• DSPG3 maps to chromosome 12q21 and is composed of 1515 nucleotides of cDNA that code for a 322-amino-acid protein [3].
• We have cloned and sequenced the human homolog to chick PG-Lb from two human chondrocyte cDNA libraries and a human chondrocyte RNA sample [3].

Anatomical context of EPYC

• In the developing limb, chick PG-Lb appears to be exclusively expressed in the zone of flattened chondrocytes [3].
• Thus in these respects they were unlike the small proteochondroitins (PG-Lb or PG-Lt) that have been found in chick-embryo cartilage [4].

Associations of EPYC with chemical compounds

• Characterization of human DSPG3, a small dermatan sulfate proteoglycan [3].

Other interactions of EPYC

• The human homolog has been named DSPG3, as it is the third member of the small dermatan sulfate proteoglycan family to be identified and characterized along with biglycan (PG-I) and decorin (PG-II) [3].
• It shows highest protein sequence identity to epiphycan (37%) and osteoglycin (31%) and belongs to the Class III family of LRR extracellular matrix proteins [5].

References