Ubiquitin-like protein from human placental extract exhibits collagenase activity

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 indicat...

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Bibliographic Details
Published in:PloS one 2013-03, Vol.8 (3), p.e59585-e59585
Main Authors: De, Debashree, Datta Chakraborty, Piyali, Mitra, Jyotirmoy, Sharma, Kanika, Mandal, Somnath, Das, Aneesha, Chakrabarti, Saikat, Bhattacharyya, Debasish
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Angiogenesis
Animals
Atomic force microscopy
Bioinformatics
Biology
Breast cancer
Cattle
Cell adhesion & migration
Cell cycle
Collagen
Collagenase
Collagenases - chemistry
Collagenases - metabolism
Collagens
Councils
Crystallography
Deoxyribonucleic acid
Divergence
DNA
Erythrocytes
Extracellular matrix
Female
Fourier transforms
Gel electrophoresis
Gelatin
Gelatinase
Gelatinases - chemistry
Gelatinases - metabolism
Growth factors
High-performance liquid chromatography
Humans
Industrial research
Inflammatory diseases
Liquid chromatography
Medicine
Microscopy
Molecular Sequence Data
Peptide Fragments - chemistry
Peptide Fragments - metabolism
Peptides
Placenta
Placenta - enzymology
Pregnancy
Proteins
R&D
Red blood cells
Research & development
Solubility
Species Specificity
Ubiquitin
Ubiquitins - chemistry
Ubiquitins - metabolism
Wound Healing
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Summary: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.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0059585