title: Effects of a bioscaffold on collagen fibrillogenesis in healing medial collateral ligament in rabbits.
abstract: Bioscaffolds have been successfully used to improve the healing of ligaments and tendons. In a rabbit model, the application of porcine small intestine submucosa (SIS) to the healing medial collateral ligament (MCL) resulted in improved mechanical properties with the formation of larger collagen fibrils. Thus, the objective of the study was to find out whether the SIS bioscaffold could improve the gene expressions of fibrillogenesis-related molecules, specifically, collagen types I, III, V, and small leucine-rich proteoglycans including decorin, biglycan, lumican, and fibromodulin, as well as collagen fibril morphology and organization, in the healing rabbit MCL at an early time point (6 weeks postinjury). Twenty skeletally mature rabbits were equally divided into two groups. In the SIS-treated group, a 6-mm gap was surgically created and a layer of SIS was sutured to cover the gap, whereas the gap was left open in the nontreated group. At 6 weeks postinjury, Masson's trichrome staining showed that the SIS-treated group had more regularly aligned collagen fibers and cells. Transmission electron microscopy revealed that the SIS-treated group had larger collagen fibrils with a diameter distribution from 24 to 120 nm, whereas the nontreated group had only small collagen fibrils (ranging from 26 to 87 nm, p < 0.05). Finally, the quantitative real-time PCR showed that the mRNAs of collagen type V, decorin, biglycan, and lumican in the SIS-treated group were 41, 58, 51, and 43% lower than those in the nontreated group, respectively (p < 0.05). Such significant reduction in the gene expressions are closely related to the improved morphological characteristics, which are known to be coupled with better mechanical properties, as previously reported in longer term studies.
authors.affiliation: Musculoskeletal Research Center, Department of Bioengineering, University of Pittsburgh, 300 Technology Drive, Pittsburgh, Pennsylvania 15219, USA.
authors.forename: Rui
authors.initials: R
authors.lastname: Liang
authors.forename: Savio L-Y
authors.initials: SL
authors.lastname: Woo
authors.forename: Tan D
authors.initials: TD
authors.lastname: Nguyen
authors.forename: Ping-Cheng
authors.initials: PC
authors.lastname: Liu
authors.forename: Alejandro
authors.initials: A
authors.lastname: Almarza
mesh_terms: D000818:Animals; D011508:Chondroitin Sulfate Proteoglycans / Q000235:genetics / Q000378:metabolism; D003094:Collagen / Q000235:genetics* / Q000378:metabolism; D024042:Collagen Type I / Q000235:genetics / Q000378:metabolism; D024061:Collagen Type III / Q000235:genetics / Q000378:metabolism; D024062:Collagen Type V / Q000235:genetics / Q000378:metabolism; D058575:Decorin; D004195:Disease Models, Animal; D016326:Extracellular Matrix Proteins / Q000235:genetics / Q000378:metabolism; D005260:Female; D000071235:Fibromodulin; D007413:Intestinal Mucosa / Q000502:physiology / Q000637:transplantation; D007632:Keratan Sulfate / Q000235:genetics / Q000378:metabolism; D000071234:Lumican; D017888:Medial Collateral Ligament, Knee / Q000293:injuries* / Q000502:physiology* / Q000648:ultrastructure; D046529:Microscopy, Electron, Transmission; D011509:Proteoglycans / Q000235:genetics / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism; D011817:Rabbits; D013552:Swine; D023822:Tissue Engineering; D014945:Wound Healing / Q000502:physiology*
chemical_list: D011508:Chondroitin Sulfate Proteoglycans; D024042:Collagen Type I; D024061:Collagen Type III; D024062:Collagen Type V; D058575:Decorin; D016326:Extracellular Matrix Proteins; D000071234:Lumican; D011509:Proteoglycans; D012333:RNA, Messenger; D000071235:Fibromodulin; D003094:Collagen; D007632:Keratan Sulfate