Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0694563 (eds)
 1,062 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Avian RNA tumor virus envelope glycoprotein protects against sarcoma development by an avian sarcoma virus of the same subgroup. Avian RNA tumor viruses, members of the retrovirus family, induce various malignancies in fowl (Weiss et al. (eds.), 1982, RNA Tumor Viruses, Cold Spring Harbor, N.Y.). These viruses consist of a genomic RNA core surrounded by an envelope with embedded glycoproteins, of 85 and 37 kDa. The 85 kDa glycoprotein is antigenically specific for each subgroup as determined by neutralization. The envelope glycoprotein can be removed from the virion with retention of its antigenicity (Duesberg et al., 1970, Virology 41, 631-646). Two fractions of 4-6S and 8S, separated by sedimentation, were shown to retain antigenicity by interference of neutralization of virus by antibody. Thus, the 4-6S and 8S preparations could possibly serve as immunogens. The objective of this study was to determine if such envelope glycoprotein preparations could function as potential vaccines, and if so, whether the protection afforded would be subgroup specific.
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PMID:Immunization with envelope glycoprotein of an avian RNA tumor virus protects against sarcoma virus tumor induction: role of subgroup. 282 7

The Yoshida sarcoma, a malignant rat tumor, has been reported by Machinami ( Machinami , R. (1972) Acta Pathol. JPN 22, 19-39) to destroy cartilage matrix in vivo. We have characterized an enzyme secreted by Yoshida sarcoma cells in culture which degrades cartilage proteoglycan in solution and also in situ in organ culture ( Mikuni - Takagaki , Y., and Gross, J. (1981) in Proceedings of the 6th International Symposium on Glycoconjugates ( Yamakawa , T., Osawa , T., Handa , S., eds) pp. 491-492, Japan Scientific Societies Press, Tokyo) ( Mikuni - Takagaki , Y., and Gross, J. (1982) in The Extracellular Matrix ( Hawkes , S., and Wang, J.L., eds) pp. 379-385, Academic Press, New York). In this report we characterized the isolated enzyme with the help of a new assay system for measurement of proteoglycan core protein degradation, which utilizes aminopropyl glass beads derivatized with hyaluronic acid. This enzyme, with a neutral pH optimum and apparent molecular weight of about 30,000, is secreted into culture medium in an active form. It is resistant to cartilage-derived inhibitors and to alpha 2-macroglobulin as well as to synthetic and natural inhibitors of serine-, thiol- and carboxylproteinases . It is inhibited by a chelating agent, 1,10-phenanthroline and thiol compounds at relatively high concentrations, and therefore is probably a metalloproteinase. The enzyme degrades type V collagen, types I and II denatured collagen (gelatin), and casein in addition to cartilage proteoglycan, but not bovine serum albumin, myoglobin, fibrinogen, elastin or native collagen types I, II, III, and IV. These findings suggest that the Yoshida sarcoma may degrade cartilage matrix in vivo by means of a secreted, active, inhibitor-resistant enzyme.
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PMID:Cartilage-degrading neutral proteinase secreted by Yoshida sarcoma cells. Purification and properties. 637 64

A tailgut cyst is a rare congenital lesion that can develop in the presacral space from the remnants of an embryonic hindgut. It is unusual for malignant change to occur in a tailgut cyst. We report a case of a large long-standing tailgut cyst, which was removed during a laparotomy. Histopathology showed a well-differentiated neuroendocrine tumour (primary carcinoid tumour) arising in a tailgut cyst. We reviewed the English literature for all adult cases with this condition. All original articles were reviewed, and data were compiled and tabulated. Including this report, 29 cases of NET developing in a tailgut cyst were found in the English literature. Tailgut cysts have been reported as more common in females, with a mean age of presentation in the fifth decade (Devine, in: Zbar A, Wexner S (eds) Coloproctology. Springer specialist surgery series, Springer, London, 2010; Hjermstad and Helwig in Am J Clin Pathol 89:139-147, 1988). Tailgut cysts may undergo malignant change including adenocarcinoma, sarcoma, and NET (Mathis et al. Br J Surg 97:575-579, 2010; Messick in Dis Colon Rectum 61:151-153, 2018; Patsouras et al. in Colorectal Dis 17:724-729, 2015; Chereau et al in Colorectal Dis 15:e476-e482, 2013). It is difficult to estimate the true incidence of malignant change in a tailgut cyst, with the literature reports only limited to case reports and small-case series. Although rare, our case confirms need to consider the possibility of a malignant component, even in a benign process such as a tailgut cyst. This prompts consideration for upfront definitive management.
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PMID:Neuroendocrine tumour developing within a long-standing tailgut cyst: case report and review of the literature. 3137 38