Glomus tumor of the cheek: an immunohistochemical demonstration of actin and myosin. 1985

T Saku, and H Okabe, and K Matsutani, and M Sasaki

A rare case of a buccal glomus tumor was examined by light and electron microscopy. Histologically, the tumor consisted of various vascular spaces surrounded by masses of epithelioid glomus cells, coexisting with a hemangiomatous proliferation of the vessels. Immunohistochemical stainings revealed that the tumor cells were positive for smooth-muscle actin and myosin, with various intensities of the stainings. The electron microscope invariably showed microfilaments in the tumor cells. The results suggest that the glomus tumor cells have characteristics of the smooth-muscle cell and the tumor has a hamartomatous nature.

UI MeSH Term Description Entries
D008297 Male Males
D008875 Middle Aged An adult aged 45 - 64 years. Middle Age
D009130 Muscle, Smooth Unstriated and unstriped muscle, one of the muscles of the internal organs, blood vessels, hair follicles, etc. Contractile elements are elongated, usually spindle-shaped cells with centrally located nuclei. Smooth muscle fibers are bound together into sheets or bundles by reticular fibers and frequently elastic nets are also abundant. (From Stedman, 25th ed) Muscle, Involuntary,Smooth Muscle,Involuntary Muscle,Involuntary Muscles,Muscles, Involuntary,Muscles, Smooth,Smooth Muscles
D009218 Myosins A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain. Myosin ATPase,ATPase, Actin-Activated,ATPase, Actomyosin,ATPase, Myosin,Actin-Activated ATPase,Actomyosin ATPase,Actomyosin Adenosinetriphosphatase,Adenosine Triphosphatase, Myosin,Adenosinetriphosphatase, Actomyosin,Adenosinetriphosphatase, Myosin,Myosin,Myosin Adenosinetriphosphatase,ATPase, Actin Activated,Actin Activated ATPase,Myosin Adenosine Triphosphatase
D002610 Cheek The part of the face that is below the eye and to the side of the nose and mouth. Bucca,Buccas,Cheeks
D005153 Facial Neoplasms New abnormal growth of tissue in the FACE. Facial Neoplasm,Neoplasm, Facial,Neoplasms, Facial
D005918 Glomus Tumor A blue-red, extremely painful vascular neoplasm involving a glomeriform arteriovenous anastomosis (glomus body), which may be found anywhere in the skin, most often in the distal portion of the fingers and toes, especially beneath the nail. It is composed of specialized pericytes (sometimes termed glomus cells), usually in single encapsulated nodular masses which may be several millimeters in diameter (From Stedman, 27th ed). CHEMODECTOMA, a tumor of NEURAL CREST origin, is also sometimes called a glomus tumor. Glomangioma,Glomangiomas,Glomus Tumors,Tumor, Glomus,Tumors, Glomus
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000199 Actins Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle. F-Actin,G-Actin,Actin,Isoactin,N-Actin,alpha-Actin,alpha-Isoactin,beta-Actin,gamma-Actin,F Actin,G Actin,N Actin,alpha Actin,alpha Isoactin,beta Actin,gamma Actin

Related Publications

T Saku, and H Okabe, and K Matsutani, and M Sasaki
January 1978, Advances in neurology,
T Saku, and H Okabe, and K Matsutani, and M Sasaki
January 1977, Acta physiologica Scandinavica. Supplementum,
T Saku, and H Okabe, and K Matsutani, and M Sasaki
January 1977, Acta neurologica Scandinavica. Supplementum,
T Saku, and H Okabe, and K Matsutani, and M Sasaki
January 1978, Verhandlungen der Anatomischen Gesellschaft,
T Saku, and H Okabe, and K Matsutani, and M Sasaki
January 2012, Case reports in medicine,
T Saku, and H Okabe, and K Matsutani, and M Sasaki
January 1971, Radiologia diagnostica,
T Saku, and H Okabe, and K Matsutani, and M Sasaki
April 2013, The Journal of bone and joint surgery. American volume,
T Saku, and H Okabe, and K Matsutani, and M Sasaki
April 1988, Cancer,
T Saku, and H Okabe, and K Matsutani, and M Sasaki
January 1985, Taiwan yi xue hui za zhi. Journal of the Formosan Medical Association,
T Saku, and H Okabe, and K Matsutani, and M Sasaki
January 1983, American journal of clinical pathology,
Copied contents to your clipboard!