PubMed Health⌕ Search

Biomedical subjects

F A Hashim

Publications and source records attributed to F A Hashim.

25 records · Page 2Linked to original sources
PubMed1985

Interaction of autoantibodies to thyrotropin receptor with a hydrophilic subunit of the thyrotropin receptor.

Reduction of human thyroid membranes with dithiothreitol caused the release of a water-soluble glycoprotein which neutralized the thyrotropin (TSH) receptor-binding and thyroid-stimulating activities of Graves' serum. Analysis of the protein by gel filtration and sucrose density gradient centrifugation allowed estimates of 3.45 nm for the Stokes' radius, 3.6 S for the s20,w and 47 000 +/- 5000 (mean +/- S.D.; n = 4) for the Mr. The material released by dithiothreitol treatment could be crosslinked to 125I-labelled TSH coupled to N-hydroxysuccinimidyl 4-azidobenzoate (125I-HSAB-TSH), suggesting that it contained a component of the TSH receptor. Furthermore, analysis of the crosslinked material by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis indicated that it contained the TSH receptor A subunit (Mr 50 000). Several factors suggested therefore that the glycoprotein released by dithiothreitol treatment of human thyroid membranes was the TSH receptor A subunit. In particular, (a) both preparations were hydrophilic and were released from membranes by reduction, (b) they had similar Mr values and (c) both preparations crosslinked to 125I-HSAB-TSH. Material similar to the TSH receptor A subunit was released from thyroid membranes by treatment with papain, probably as a result of cleavage of the receptor A subunit at a site close to the interchain disulphide bridge. A similar mechanism, involving thyroid proteinases, was probably involved in release of material with similar properties to the TSH receptor A subunit during freezing and thawing of human thyroid homogenates.

Autoantibodies↗
PubMed1985

Thyrotropin receptor antibodies.

The thyrotropin (TSH) receptor is an integral membrane protein which contains 2 subunits linked by a disulphide bridge. The A subunit (mol. wt. 50,000) is water soluble and forms the binding site for TSH, whereas the B subunit (mol. wt. 30,000) penetrates the lipid bilayer and probably forms the site for interaction with adenylate cyclase. Autoantibodies to the TSH receptor are found in the sera of patients with Graves' disease. The antibodies bind to the same region of the receptor's A subunit as TSH and usually act as TSH agonists, causing hyperthyroidism. Occasionally, TSH receptor autoantibodies are found which can act as TSH antagonists. Isoelectric focusing and binding studies indicate that these antibodies also bind to the same region of the receptor A subunit as TSH.

Animals↗
PubMedDate not supplied

Kala-azar in western Upper Nile province in the southern Sudan and its spread to a nomadic tribe from the north.

Since the start in 1988 of the present epidemic of kala-azar (visceral leishmaniasis) in western Upper Nile state in southern Sudan, the epidemiology of the disease in all parts of the Sudan where kala-azar has been reported was reassessed by the Leishmaniasis Research Group in Khartoum. In this paper, the spread of the epidemic is described among a nomadic tribe originating from southern Kordofan state, who migrate every year with their cattle to the Bentiu area in western Upper Nile state where the epidemic is still raging. 200 cases from this tribe were seen in Khartoum; another 56 cases were found during a field trip to the area. In addition, the Bentiu area was visited, where 301 cases were under treatment and another 52 of 1120 individuals screened were confirmed parasitologically. 20 cases of post-kala-azar dermal leishmaniasis were found. Parasites isolated from the nomadic tribe were of the same zymodeme as parasites isolated previously from the Nuer in western Upper Nile. The epidemiological findings in each state are discussed in relation to the tribes that were affected and the ecology of the area.

Adolescent↗