{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Colville MJ"],"funding":["NIGMS NIH HHS","NIH HHS"],"pubmed_abstract":["Lubricin, a lubricating glycoprotein abundant in synovial fluid, forms a low-friction brush polymer interface in tissues exposed to sliding motion including joints, tendon sheaths, and the surface of the eye. Despite its therapeutic potential in diseases such as osteoarthritis and dry eye disease, there are few sources available. Through rational design, we developed a series of recombinant lubricin analogs that utilize the species-specific tissue-binding domains at the N- and C-termini to increase biocompatibility while replacing the central mucin domain with an engineered variant that retains the lubricating properties of native lubricin. In this study, we demonstrate the tissue binding capacity of our engineered lubricin product and its retention in the joint space of rats. Next, we pre"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2024.05.05.592580"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11092771"],"repository":["biostudies-literature"],"pubmed_title":["Recombinant manufacturing of multispecies biolubricants."],"pmcid":["PMC11092771"],"funding_grant_id":["DP2 GM119133","S10 OD025049"],"pubmed_authors":["Bonassar LJ","Schmidt S","Chen K","Vishwanath K","Williams RM","Huang LT","Reesink HL","Su J","Colville MJ","Paszek MJ"],"additional_accession":[]},"is_claimable":false,"name":"Recombinant manufacturing of multispecies biolubricants.","description":"Lubricin, a lubricating glycoprotein abundant in synovial fluid, forms a low-friction brush polymer interface in tissues exposed to sliding motion including joints, tendon sheaths, and the surface of the eye. Despite its therapeutic potential in diseases such as osteoarthritis and dry eye disease, there are few sources available. Through rational design, we developed a series of recombinant lubricin analogs that utilize the species-specific tissue-binding domains at the N- and C-termini to increase biocompatibility while replacing the central mucin domain with an engineered variant that retains the lubricating properties of native lubricin. In this study, we demonstrate the tissue binding capacity of our engineered lubricin product and its retention in the joint space of rats. Next, we pre","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-07-01T03:14:26.794Z","creation":"2026-07-01T03:07:55.588Z"},"accession":"S-EPMC11092771","cross_references":{"pubmed":["38746339"],"doi":["10.1101/2024.05.05.592580"]}}