High impact information on EPYC

• We have isolated cDNA clones encoding the core protein of PG-Lb, proteoglycan which has been shown to be preferentially expressed in the zone of flattened chondrocytes of the developing chick limb cartilage (Shinomura, T., Kimata, K., Oike, Y., Yano, S., and Suzuki, S. (1984) Dev. Biol. 103, 211-220) [1].
• Three different molecular species of proteoglycan (designated PG-H, PG-Lb, and PG-Lt) have been isolated from chick embryo epiphyseal cartilage [2].
• PG-Lb shows no specific binding with hyaluronic acid [2].
• Since the core molecule from pro-PG-Lb is significantly larger in molecular weight than that from PG-Lb, the conversion of pro-PG-Lb to PG-Lb should involve scission of the polypeptide or possibly removal of mannose-containing oligosaccharide chain [2].
• The amino acid composition of PG-Lt is quite different from that of PG-H and PG-Lb and rather resembles that of collagens with respect to high content of glycine and high degrees of hydroxylation of proline and lysine [3].

Biological context of EPYC

• At the onset of cartilage morphogenesis (stage 24), PG-H became recognizable in the cartilage primordia, whereas a parallel section stained for PG-Lb showed no reaction [4].

Anatomical context of EPYC

• The first evidence of PG-Lb appearance was seen in a stage 28 cartilage (e.g., tibia) in which the cells in the middiaphysis became elongated in a direction perpendicular to the long axis of the cartilage [4].

Associations of EPYC with chemical compounds

• The second proteoglycan, PG-Lb, consists of a core protein with Mr congruent to 52,000 dermatan sulfate copolymer chains with glucuronic acid/iduronic acid residues [2].

Analytical, diagnostic and therapeutic context of EPYC

• In the present report, the expression of PG-H and PG-Lb has been studied in developing chick hind limbs (stages 19-33), using antibodies specific for these substances in indirect immunofluorescence [4].

References