Premium
Characterization of placental proteoglycans
Author(s) -
Engle J. Michael,
Carrino David A.,
Caplan Arnold I.
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a269-c
Subject(s) - decorin , placenta , versican , chemistry , proteoglycan , catabolism , extracellular matrix , biglycan , microbiology and biotechnology , biochemistry , biology , fetus , enzyme , genetics , pregnancy
Proteoglycans were isolated from inner and outer human placenta by chromatography. Toluidine blue staining indicated that DEAE pool 2 contained the presence of glycosaminoglycan (GAG) molecules. Further analysis by immunoblotting of DEAE pool 1 indicated the presence of the full length and a catabolic fragment of versican V1 in both placenta samples. Detectable levels of the V0 splice variant were observed in pool 2 of the outer placenta. DEAE pool 2 of both placenta samples also showed a catabolic fragment of V0 with DPEAAE as it C‐terminus. Intact biglycan was detected in DEAE pool 2 of both placenta samples. Only the inner placenta revealed catabolic fragments. Following DEAE‐Sephacel purification, intact decorin in both placenta samples was detected. The inner placenta sample contained smaller decorin products. Some of the decorin molecules from the inner placenta did not bind to the octyl‐Sepharose and showed an approximate size of 50 kDa. The core decorin protein revealed the typical pattern of two closely migrating bands. We suspect that proteinases contribute to the release of the placenta from the uterine wall in part by degrading extracellular matrix molecules such as proteoglycans. The source and identification of the proteinases await elucidation. Funding from L'Oreal (Paris) and the National Institutes of Health.