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Anat Rec. 2000 Dec 1;260(4):392-401.
Compressive force promotes chondrogenic differentiation and hypertrophy in midpalatal suture cartilage in growing rats.
Saitoh S, Takahashi I, Mizoguchi I, Sasano Y, Kagayama M, Mitani H.
Clinics for Maxillo-Oral Disorders, Tohoku University Dental Hospital, Aoba-ku, Sendai, Japan. ssaitrthod.dent.tohoku.ac.jp
Midpalatal suture cartilage (MSC) is secondary cartilage located between the bilateral maxillary bones and has been utilized in the analysis of the biomechanical characteristics of secondary cartilage. The present study was designed to investigate the effects of compressive force on the differentiation of cartilage in midpalatal suture cartilage in rats. Forces of various magnitudes were applied to the midpalatal suture cartilage in 4-week-old male Wistar rats for 1, 2, 4, 7, or 14 days, mediated through the bilateral 1st molars using orthodontic wires. The differentiation pathways in the MSC cells were examined by immunohistochemistry for the differentiation markers type I, type II and type X collagen, and glycosaminoglycans (GAGs), chondroitin-4-sulfate, chondroitin-6-sulfate and keratan sulfate. Histologically and immunohistochemically, the midpalatal suture cartilage in control rats had the characteristic appearance of secondary cartilage. In the experimental groups, the center of the midpalatal suture cartilage that contained osteo-chondro progenitor cells seemed to become mature cartilage and its immuno-reaction to type II and X collagen and GAGs increased as the experiment progressed. This differentiation was dependent upon the magnitude and duration of the force applied to the midpalatal suture cartilage; i.e., cartilaginous differentiation progressed more rapidly as the applied force increased. The present results suggest that the differentiation of osteo-chondro progenitor cells into mature and hypertrophic chondrocytes in the precartilaginous cell layer is promoted by compressive force. 2000 Wiley-Liss, Inc.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11074405&dopt=Abstract
Anat Rec. 2000 Dec 1;260(4):402-9.
27 kDa extracellular matrix protein revealed by a monoclonal antibody raised against rat testis.
Yazama F, Sawada H.
Department of Anatomy, Yokohama City University, School of Medicine, Yokohama, Kanagawa 236-0004, Japan. fyzmed.yokohama-cu.ac.jp
In search of unique components of the seminiferous tubule extracellular matrix, monoclonal antibodies were raised against an isolated seminiferous tubule extracellular matrix, and the monoclonal antibody 12G11 was cloned. By immunofluorescence microscopy in eight kinds of rat tissues (testis, lung, liver, small intestine, cardiac muscle, skeletal muscle, kidney, and brain), 12G11 antigen existed only in the testis. Immunoelectron microscopy revealed that the antigen is localized in the basement membrane of the seminiferous tubule and in the basement membranes of myoid cells. For a biochemical analysis, eight kinds of rat extracellular matrices were isolated and solubilized with 8 M urea and 2% beta-mercaptoethanol. Immunoblot analysis of these samples in 0.8% agarose gel also showed that the antigen was specific for the testis, and in a two high-molecular weight aggregates. These aggregates seemed to contain type IV collagen and laminin chains. The antigen of 12G11 antibody was shown to be 27 kDa by 10% SDS-PAGE followed by immunoblotting. From these data, the existence of a testis specific 27 kDa basement membrane protein, which associate with type IV collagen and laminin, was suggested. 2000 Wiley-Liss, Inc.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11074406&dopt=Abstract
Biol Chem. 2002 Sep;383(9):1407-13.
Degradation of extracellular matrix protein tenascin-C by cathepsin B: an interaction involved in the progression of gliomas.
Mai J, Sameni M, Mikkelsen T, Sloane BF.
Department of Pharmacology, Wayne State University, School of Medicine, Detroit, MI 48201, USA.
Degradation of extracellular matrix proteins by proteases such as the cysteine protease cathepsin B is critical to malignant progression. We have established that procathepsin B presents on the surface of tumor cells through its interaction with the annexin II tetramer [Mai et al., J. Biol. Chem. 275 (2000),12806-12812]. Cathepsin B activity can also be detected on the tumor cell surface and in their culture medium. Interestingly, the annexin II tetramer also interacts with extracellular matrix proteins, such as collagen I, fibrin and tenascin-C. Both cathepsin B and tenascin-C are expressed at high levels in malignant tumors, especially at the invasive edges of tumors, and are implicated in tumor angiogenesis. In this study, we report that tenascin-C can be degraded by cathepsin B in vitro. We demonstrate by immunohistochemistry that both cathepsin B and tenascin-C are expressed highly in malignant anaplastic astrocytomas and glioblastomas as compared to normal brain tissues. Interestingly, cathepsin B and tenascin-C were also detected in association with tumor neovessels. We suggest that interactions between cathepsin B and tenascin-C are involved in the progression of gliomas including the angiogenesis that is a hallmark of anaplastic astrocytomas.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12437133&dopt=Abstract
Lasers Surg Med. 2000;27(4):305-18.
Histologic signatures of thermal injury: applications in transmyocardial laser revascularization and radiofrequency ablation.
Whittaker P, Zheng S, Patterson MJ, Kloner RA, Daly KE, Hartman RA.
Heart Institute, Good Samaritan Hospital, & Department of Medicine, University of Southern California, Los Angeles, California 90017, USA. pwhittakenamail.com
BACKGROUND AND OBJECTIVE: Cardiac treatments such as transmyocardial laser revascularization and radiofrequency ablation cause thermal injury. We sought to provide quantitative histologic methods of assessing such injury by using the inherent birefringence of cardiac muscle and collagen; specifically, to exploit the connection between thermal injury and the loss of birefringence. STUDY DESIGN/MATERIALS AND METHODS: We quantified tissue birefringence changes in vitro for temperatures up to 130 degrees C. This information was used to assess thermal injury associated with myocardial channels made in vitro. We then measured in vivo cardiac injury 30 minutes and 3 days after radiofrequency exposure. RESULTS: Birefringence decreased above 60 degrees C for muscle and above 70 degrees C for collagen. Temperatures above 80 degrees C were associated with collagen fiber straightening and above 95 degrees C with little muscle birefringence. Injury adjacent to laser channels was greatest parallel to cell orientation. In vivo, muscle with reduced birefringence was surrounded by cells exhibiting focal birefringence increases (contraction bands). Early injury assessment marked by birefringence changes corresponded to lesion size at 3 days. CONCLUSION: Polarized light revealed histologic temperature signatures corresponding to irreversible muscle injury and collagen denaturation. 2000 Wiley-Liss, Inc.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11074507&dopt=Abstract
llnl.gov
BACKGROUND AND OBJECTIVE: Helical macromolecules such as collagen and DNA are characterized by nonlinear optical properties, including nonlinear susceptibility. Because collagen is the predominant component of most biological tissues, as well as the major source of second harmonic generation (SHG), it is reasonable to assume that changes in harmonic signal can be attributed to structural changes in collagen. The purpose of this study is to determine whether various modifications of collagen structure affect second harmonic intensity. STUDY DESIGN/MATERIALS AND METHODS: SHG was measured in tissues from cows, humans, and chickens. The effects of beam polarization, thermal denaturation, glyco-oxidative damage, and enzymatic cleavage of tissues on second harmonic intensity was studied. RESULTS: The second harmonic intensity differed considerably among different tissues, as did the effect of the incident beam polarization. In structurally modified collagen, SHG was significantly degraded from SHG in intact collagen. CONCLUSION: These structural modifications are representative of changes that occur in pathophysiologic conditions such as thermal injury, diabetes, tumor invasion, and abnormal wound healing. The ability to assess these changes rapidly and noninvasively has considerable clinical applicability. SHG analysis might provide a unique tool for monitoring these structural changes of collagen.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11074509&dopt=Abstract
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