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Asian Journal of Surgery Dec 2022
Topics: Humans; Osteochondroma; Ribs; Hemangioma; Bone Neoplasms
PubMed: 35739029
DOI: 10.1016/j.asjsur.2022.06.069 -
Genetics and Molecular Research : GMR Dec 2016Osteosarcoma is a common malignant bone tumor that mainly affects children and adolescents. Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is a member...
Osteosarcoma is a common malignant bone tumor that mainly affects children and adolescents. Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is a member of the tumor necrosis factor superfamily. Caspase-8 appears in the upstream of apoptosis signaling pathway among caspases. We investigated TRAIL and caspase-8 levels in osteosarcoma patients to determine their correlation with cell proliferation and apoptosis. Osteosarcoma and osteochondroma patients receiving surgery in our hospital were selected. TRAIL and caspase-8 expression levels in tissue were determined by immunohistochemistry, and protein levels in cells were evaluated by western blotting. Human osteosarcoma cell viability was determined by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay. The osteosarcoma and osteochondroma cell cycles and apoptosis were investigated by flow cytometry. Correlation analysis was applied to TRAIL and caspase-8 levels during cell apoptosis. Positive TRAIL and caspase-8 expression rates in osteosarcoma tissue were significantly lower than in the controls (P < 0.05). TRAIL (0.114 ± 0.002) and caspase-8 (0.352 ± 0.124) levels in experimental cells were obviously lower than in the controls (P < 0.05). Osteosarcoma cells in the experimental group demonstrated higher proliferation and lower apoptosis at 24, 48, and 72 h (P < 0.05). The experimental cell number increased in the G1 stage and decreased in the S stage (P < 0.05). TRAIL and caspase-8 proteins showed positive correlation with apoptosis in osteosarcoma (P < 0.05). Human osteosarcoma presented reduced TRAIL and caspase-8 levels with enhanced cell proliferation and reduced apoptosis. TRAIL and caspase-8 expression levels were positively correlated with apoptosis in osteosarcoma.
Topics: Adult; Aged; Apoptosis; Bone Neoplasms; Caspase 8; Cell Proliferation; Cell Survival; Female; Gene Expression Regulation, Neoplastic; Humans; Male; Middle Aged; Osteochondroma; Osteosarcoma; TNF-Related Apoptosis-Inducing Ligand; Tumor Cells, Cultured; Young Adult
PubMed: 28002586
DOI: 10.4238/gmr15048876 -
Orthopaedics & Traumatology, Surgery &... Dec 2017Snapping scapula syndrome is a rare condition characterized by crepitus of the scapula on motion of the ipsilateral upper extremity. It may be quite painful and... (Review)
Review
Snapping scapula syndrome is a rare condition characterized by crepitus of the scapula on motion of the ipsilateral upper extremity. It may be quite painful and disabling. The majority of cases are due to bursal and muscular disorders. Snapping scapula syndrome secondary to an underlying osteochondroma is an even more infrequent phenomenon. The case presented highlights the unusual post pubertal growth of an osteochondroma of the scapula that progressed to develop a snapping scapular syndrome. Review of the literature revealed less than fifty reported cases of this phenomenon secondary to an underlying osteochondroma.
Topics: Bone Neoplasms; Humans; Male; Osteochondroma; Scapula; Syndrome; Young Adult
PubMed: 28965995
DOI: 10.1016/j.otsr.2017.01.019 -
Bone Jun 2018Multiple osteochondromas (MO) syndrome is a dominant autosomal bone disorder characterized by the formation of cartilage-capped bony outgrowths that develop at the...
Multiple osteochondromas (MO) syndrome is a dominant autosomal bone disorder characterized by the formation of cartilage-capped bony outgrowths that develop at the juxtaposition of the growth plate of endochondral bones. MO has been linked to mutations in either EXT1 or EXT2, two glycosyltransferases required for the synthesis of heparan sulfate (HS). The establishment of mouse mutants demonstrated that a clonal, homozygous loss of Ext1 in a wild type background leads to the development of osteochondromas. Here we investigate mechanisms that might contribute to the variation in the severity of the disease observed in human patients. Our results show that residual amounts of HS are sufficient to prevent the development of osteochondromas strongly supporting that loss of heterozygosity is required for osteochondroma formation. Furthermore, we demonstrate that different signaling pathways affect size and frequency of the osteochondromas thereby modulating the severity of the disease. Reduced Fgfr3 signaling, which regulates proliferation and differentiation of chondrocytes, increases osteochondroma number, while activated Fgfr3 signaling reduces osteochondroma size. Both, activation and reduction of Wnt/β-catenin signaling decrease osteochondroma size and frequency by interfering with the chondrogenic fate of the mutant cells. Reduced Ihh signaling does not change the development of the osteochondromas, while elevated Ihh signaling increases the cellularity and inhibits chondrocyte differentiation in a subset of osteochondromas and might thus predispose osteochondromas to the transformation into chondrosarcomas.
Topics: Animals; Cell Differentiation; Chondrocytes; Disease Models, Animal; Exostoses, Multiple Hereditary; Growth Plate; Hedgehog Proteins; Heparitin Sulfate; Humans; Loss of Heterozygosity; Mice; N-Acetylglucosaminyltransferases; Receptor, Fibroblast Growth Factor, Type 3; Signal Transduction; Wnt Signaling Pathway; beta Catenin
PubMed: 29545125
DOI: 10.1016/j.bone.2018.03.010 -
BMC Musculoskeletal Disorders Apr 2020Osteochondroma is a benign tumor that occurs mainly at the metaphysis of long bones and seldom arises from carpal bones. We describe an extremely rare case of... (Review)
Review
BACKGROUND
Osteochondroma is a benign tumor that occurs mainly at the metaphysis of long bones and seldom arises from carpal bones. We describe an extremely rare case of osteochondroma of the hamate without a typical cartilaginous cap and with a spiky bony protrusion in an elderly patient.
CASE PRESENTATION
A 78-year-old right-handed female housekeeper had a multilobed osteochondroma of the hamate, which caused carpal tunnel syndrome and irritation of the flexor tendons. Radiological examinations showed a morphological abnormality of the hamate comprising a spiky bony protrusion into the carpal tunnel and a free body proximal to the pisiform. Open carpal tunnel release and resection of the spiky bony protrusion on the hook of the hamate were performed. The flexor digitorum profundus tendons of the ring and little fingers displayed synovitis and partial laceration in the carpal tunnel. Histological examination also showed atypical findings: only a few regions of cartilaginous tissue were seen in the spiky bony protrusion, whereas the free body proximal to the pisiform contained thick cartilaginous tissue such as a cartilaginous cap typical of osteochondroma. We speculated that the bony protrusion to the carpal tunnel had been eroded by mechanical irritation caused by gliding of the flexor tendon and had resulted in the protruding spiky shape with less cartilaginous tissue. The fractured cartilaginous cap had moved into the cavity within the carpal tunnel proximal to the pisiform and had become a large free body.
CONCLUSIONS
Osteochondroma of the carpal bone may take various shapes because the carpal bone is surrounded by neighboring bones and tight ligaments, which can restrict tumor growth. This type of tumor is likely to present with various symptoms because of the close proximity of important structures including nerves, tendons, and joints. The diagnosis of osteochondroma of the carpal bone may be difficult because of its rarity and atypical radiological and histological findings, such as the lack of a round cartilaginous cap. We suggest that surgeons should have a detailed understanding of this condition and should make a definitive diagnosis based on the overall findings.
Topics: Aged; Carpal Tunnel Syndrome; Female; Hamate Bone; Humans; Osteochondroma; Radiography; Tendons; Wrist
PubMed: 32284050
DOI: 10.1186/s12891-020-03272-8 -
Journal of Pediatric Orthopedics 2011Multiple hereditary exostoses, also termed as multiple osteochondromas, is a heritable disorder of connective tissue with primarily orthopaedic clinical manifestations.... (Review)
Review
BACKGROUND
Multiple hereditary exostoses, also termed as multiple osteochondromas, is a heritable disorder of connective tissue with primarily orthopaedic clinical manifestations. Understanding of its biological underpinnings has been advanced on a variety of fronts in recent years.
METHODS
The multifaceted literature regarding osteochondromagenesis and the major clinical challenges in patients with multiple osteochondromas were reviewed.
RESULTS
Consideration of recent advances in molecular biology, biochemistry, and animal modeling of osteochondroma pathogenesis yields a unified model.
CONCLUSIONS
Mechanistic details and therapeutic targets have yet to be elucidated, but the general biology of osteochondroma formation is increasingly clear, as well as its implications in the orthopaedic clinical setting.
Topics: Animals; Exostoses, Multiple Hereditary; Glycomics; Growth Plate; Humans
PubMed: 21654469
DOI: 10.1097/BPO.0b013e31821c7738 -
Connective Tissue Research 2015Heparan sulfate (HS) is a component of cell surface and matrix-associated proteoglycans (HSPGs) that, collectively, play crucial roles in many physiologic processes... (Review)
Review
Heparan sulfate (HS) is a component of cell surface and matrix-associated proteoglycans (HSPGs) that, collectively, play crucial roles in many physiologic processes including cell differentiation, organ morphogenesis and cancer. A key function of HS is to bind and interact with signaling proteins, growth factors, plasma proteins, immune-modulators and other factors. In doing so, the HS chains and HSPGs are able to regulate protein distribution, bio-availability and action on target cells and can also serve as cell surface co-receptors, facilitating ligand-receptor interactions. These proteins contain an HS/heparin-binding domain (HBD) that mediates their association and contacts with HS. HBDs are highly diverse in sequence and predicted structure, contain clusters of basic amino acids (Lys and Arg) and possess an overall net positive charge, most often within a consensus Cardin-Weintraub (CW) motif. Interestingly, other domains and residues are now known to influence protein-HS interactions, as well as interactions with other glycosaminoglycans, such as chondroitin sulfate. In this review, we provide a description and analysis of HBDs in proteins including amphiregulin, fibroblast growth factor family members, heparanase, sclerostin and hedgehog protein family members. We discuss HBD structural and functional features and important roles carried out by other protein domains, and also provide novel conformational insights into the diversity of CW motifs present in Sonic, Indian and Desert hedgehogs. Finally, we review progress in understanding the pathogenesis of a rare pediatric skeletal disorder, Hereditary Multiple Exostoses (HME), characterized by HS deficiency and cartilage tumor formation. Advances in understanding protein-HS interactions will have broad implications for basic biology and translational medicine as well as for the development of HS-based therapeutics.
Topics: Amino Acid Motifs; Animals; Exostoses, Multiple Hereditary; Heparitin Sulfate; Humans; Intercellular Signaling Peptides and Proteins; Protein Structure, Tertiary; Signal Transduction; Translational Research, Biomedical
PubMed: 26076122
DOI: 10.3109/03008207.2015.1045066 -
Acta Reumatologica Portuguesa 2012
Topics: Child, Preschool; Exostoses, Multiple Hereditary; Humans; Male
PubMed: 22781520
DOI: No ID Found -
European Journal of Vascular and... Feb 1996
Topics: Adult; Arterial Occlusive Diseases; Femoral Artery; Femoral Neoplasms; Femoral Vein; Humans; Male; Osteochondroma; Thrombosis
PubMed: 8616664
DOI: 10.1016/s1078-5884(96)80064-5 -
Proceedings of the Royal Society of... Jul 1947
Topics: Enchondromatosis; Exostoses, Multiple Hereditary; Osteochondrodysplasias
PubMed: 19993593
DOI: No ID Found