Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0001511 (Adhesion)
 5,955 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Adhesion molecule upregulation occurs in inflammatory myopathies, and is one of the myriad functions of tumor necrosis factor-alpha (TNF-alpha). TNF-alpha acts via two different receptors of 55 (TNF-R55) and 75 kD (TNF-R75). We immunolocalized TNF-alpha and its receptors in polymyositis, inclusion body myositis and dermatomyositis. In each myopathy, TNF-alpha was detected in macrophages, in myonuclei in regenerating muscle fibers, and freely dispersed in endomysial or perimysial connective tissue. Many endothelial cells in dermatomyositis expressed TNF-alpha. TNF-R55 was strongly expressed on myonuclei of regenerating muscle fibers. TNF-R75 was increased on endothelial cells in the midst of inflammatory infiltrates in each myopathy, and on perifascicular and perimysial endothelia, remote from inflammatory foci in dermatomyositis. Possible TNF-alpha-mediated effects include: increased transendothelial cell trafficking, activation of T/B cells and macrophages, induction of MHC-I gene products, and focal muscle fiber atrophy. In dermatomyositis, the upregulated TNF-R75, via its consensus elements for transcription factors, may be involved in endothelial cell degeneration. Strong TNF-R55 expression on regenerating myonuclei is consistent with a role of TNF-alpha and TNF-R55 in muscle regeneration.
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PMID:Immunolocalization of tumor necrosis factor-alpha and its receptors in inflammatory myopathies. 1039 51

To assess the differential expression of adhesion molecules ICAM-1 and VCAM-1 in vessels and muscle fibers in acquired inflammatory myopathy, a series comprising thirty-seven muscle biopsy specimens from patients with JDM, fifteen with DM, fifteen with PM and seven with IBM was studied. Histochemical and immunohistochemical tests (StreptABCcomplex/HRP) for ICAM-1 and VCAM-1 (Dakopatts) were performed in serial frozen sections. ICAM-1 expression in vessels was significantly (p<0.0001) more present in JDM than PM, DM or IBM. However, in muscle fibers, ICAM-1 expression was absent in both JDM and IBM, but present in 33.4% and 40% in PM and DM respectively (p<0.0001). VCAM-1 expression in vessels was significantly more present in PM and DM than JDM and IBM (p<0.0001) while VCAM-1 expression in muscle fibers was almost absent in the four groups (p=0.2632). These findings emphasize the importance of adhesion molecules in the pathophysiology of the inflammatory myopathies, mainly the marked ICAM-1 expression in vessels in JDM, corroborating the microvascular involvement in this disease. In contrast, VCAM-1 seems not to play a major role in JDM, as previously described in PM, DM and IBM. Adhesion molecule expression in JDM presents a differential characteristic when compared to PM, DM and IBM.
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PMID:Difference in adhesion molecule expression (ICAM-1 and VCAM-1) in juvenile and adult dermatomyositis, polymyositis and inclusion body myositis. 1643 35

Myoblast fusion contributes to muscle growth in development and during regeneration of mature muscle. Myoblasts fuse to each other as well as to multinucleate myotubes to enlarge the myofiber. The molecular mechanisms of myoblast fusion are incompletely understood. Adhesion, apposition, and membrane fusion are accompanied by cytoskeletal rearrangements. The ferlin family of proteins is implicated in human muscle disease and has been implicated in fusion events in muscle, including myoblast fusion, vesicle trafficking and membrane repair. Dysferlin was the first mammalian ferlin identified and it is now known that there are six different ferlins. Loss-of-function mutations in the dysferlin gene lead to limb girdle muscular dystrophy and the milder disorder Miyoshi Myopathy. Dysferlin is a membrane-associated protein that has been implicated in resealing disruptions in the muscle plasma membrane. Newer data supports a broader role for dysferlin in intracellular vesicular movement, a process also important for resealing. Myoferlin is highly expressed in myoblasts that undergoing fusion, and the absence of myoferlin leads to impaired myoblast fusion. Myoferlin also regulates intracellular trafficking events, including endocytic recycling, a process where internalized vesicles are returned to the plasma membrane. The trafficking role of ferlin proteins is reviewed herein with a specific focus as to how this machinery alters myogenesis and muscle growth.
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PMID:Ferlin proteins in myoblast fusion and muscle growth. 2162 Oct 72