Porcine ligament fibroblasts were cultured from the anterior cruciate (ACL), medial collateral (MCL), and ligamentum teres (LT). There were no apparent differences in confluent cellular morphology among the ligament cell types as evaluated by phase contrast microscopy. The proliferation rate of MCL cells from 24-120 h was significantly higher (p < 05) than that of cells from either the LT or the ACL. MCL cells produced more collagen and less non-collagenous protein than the LT and ACL as determined by [3H]proline incorporation. This resulted in MCL cells producing a higher percentage (37%, p < 05) of collagen relative to total protein than either the ACL (28%) or the LT (32%). The MCL cells produced a significantly higher percentage (34%, p < 05) of type-III collagen relative to total type-I and III collagen than either the ACL (29%) or the LT (29%). The LT and MCL cells had similar and significantly greater coverage of in vitro wounds than the ACL. This study provides the first in vitro study of the LT and demonstrates that fibroblasts from the LT and ACL, two ligaments that heal poorly, have similar in vitro characteristics, with the exception of wound [Zyderm collagen. Clinical efficacy and tolerance].Lysine hydroxylation and cross-linking of collagen.Collagens represent a large family of structurally related extracellular matrix proteins containing unique triple helical structure. One of the characteristics of this structural protein is its extensive post-translational modifications that have major effects on molecular assembly, stability, and metabolism. Hydroxylation of specific lysine residues is one of such unique modifications found in collagen, and the pattern/extent of this modification influences fibrillogenesis, cross-linking, and matrix mineralization. The formation of covalent intermolecular cross-linking is the final modification in collagen biosynthesis and is critical for the stability of collagen. The process of cross-linking is dynamic and the pathways vary depending on the tissues and tissue's physiological state. This tissue specificity of cross-linking pattern may in part be the results of differential expression of various isoforms of lysyl hydroxylases and lysyl oxidases that have been recently identified and partially characterized. This chapter concentrates on recent research progress on these two modifications and the methods for analysis we have developed.Quantitative Characterization of Collagen in the Fibrotic Capsule Surrounding Implanted Polymeric Microparticles through Second Harmonic Generation Imaging.Iowa 50011, United States of America; Department of Chemical & Biological Engineering, Iowa State University, Ames, Iowa 50011, United States of America; Ames National Laboratory, Ames, Iowa 50011, United States of America.The collagenous capsule formed around an implant will ultimately determine the nature of its in vivo fate. To provide a better understanding of how surface modifications can alter the collagen orientation and composition in the fibrotic capsule, we used second harmonic generation (SHG) microscopy to evaluate collagen organization and structure generated in mice subcutaneously injected with chemically functionalized polystyrene particles. SHG is sensitive to the orientation of a molecule, making it a powerful tool for measuring the alignment of collagen fibers. Additionally, SHG arises from the second order susceptibility of the interrogated molecule in response to the electric field. Variation in these tensor components distinguishes different molecular sources of SHG, providing collagen type specificity. Here, we demonstrated the ability of SHG to differentiate collagen type I and type III quantitatively and used this method to examine fibrous capsules of implanted polystyrene particles. Data presented in this work shows a wide range of collagen fiber orientations and collagen compositions in response to surface functionalized polystyrene particles. Dimethylamino functionalized particles were able to form a thin collagenous matrix resembling healthy skin. These findings have the potential to improve the fundamental understanding of how material properties influence collagen organization and composition quantitatively.Conflict of interest statement: Competing Interests: The authors have declared Demonstrating collagen tendon fibril segments involvement in intrinsic tendon University, College of Medicine, Hershey, PA 17033, United States.Severed tendons can undergo regenerative healing, intrinsic tendon repair. Fibrillogenesis of chick tendon involves collagen fibril segments (CFS), which are the building blocks of collagen fibers that make up tendon fascicles. benefits of collagen are 10 micron in length, composed of tropocollagen monomers arranged in parallel arrays. Rather than incorporating Dermatological medications into growing collagen fibers, incorporating large CFS units is the mechanism for generating collagen fibers. Is intrinsic tendon repair through the reestablishment of tendon embryogenesis? Gentamicin treated 10-day-old chick embryo tendons released CFS were fluorescently tagged with Rhodamine (Rh). Organ cultured severed 14-day-old embryo tendon explants received Rh tagged CFS.
benefits of collagen|Dermatological medications
