Open AccessUbiquitin-Like Protein from Human Placental Extract Exhibits Collagenase Activity
Author(s) -
Debashree De,
Piyali Datta Chakraborty,
Jyotirmoy Mitra,
Kusum Sharma,
Somnath Mandal,
Aneesha Das,
Saikat Chakrabarti,
Debasish Bhattacharyya
Publication year - 2013
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0059585
Subject(s) - collagenase , zymography , ubiquitin , biochemistry , chemistry , interstitial collagenase , gelatinase , metalloproteinase , placenta , microbiology and biotechnology , matrix metalloproteinase , enzyme , biology , pregnancy , fetus , genetics , gene
An aqueous extract of human placenta exhibits strong gelatinase/collagenase activity in zymography. 2-D gel electrophoresis of the extract with gelatin zymography in the second dimension displayed a single spot, identified as ubiquitin-like component upon MALDI/TOF MS/MS analysis. Immunoblot indicated presence of ubiquitin and absence of collagenase in the extract. Collagenase activity of the ubiquitin-like component was confirmed from the change in solubility of collagen in aqueous buffer, degradation of collagen by size-exclusion HPLC and atomic force microscopy. Quantification with DQ-gelatin showed that the extract contains 0.04 U/ml of collagenase activity that was inhibited up to 95% by ubiquitin antibody. Ubiquitin from bovine erythrocytes demonstrated mild collagenase activity. Bioinformatics studies suggest that placental ubiquitin and collagenase follow structurally divergent evolution. This thermostable intrinsic collagenase activity of placental extract might have wide physiological relevance in degrading and remodeling collagen as it is used as a drug for wound healing and pelvic inflammatory diseases.