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Biomedical subjects

B G Sharma

Publications and source records attributed to B G Sharma.

8 recordsLinked to original sources
PubMed2003

Duplication of the clavicle with triplication of the coracoid process.

A very rare case of duplication of the clavicle and triplication of the coracoid process of the scapula is presented. Duplication of the clavicle has been described in only six reports based on a search of the world literature. There is no mention of duplication or triplication of the coracoid process of the scapula in the world literature and this would appear to be the first report of this kind. A combination of bifurcation and triplication of the clavicle and coracoid process, respectively, in the present case illustrates that even anomalous bones search for their counterpart to form a joint. The process of duplication or triplication is explained with a new hypothesis.

Adult↗
PubMed2002

A new syndrome of "spondylo-epi-metaphyseal dysplasia: mixed type".

A new type of rare bone dysplasia is described, which shares some common features with spondylo-meta-epiphyseal dysplasia: short limb-abnormal calcification type and lethal metatropic dysplasia. Besides these features, the present case has some additional unusual features. Facial malformation was very obvious and of a different type. The nose and nares were completely flattened. Hypertrophied acetabular bones, round densities on the ilia, premature ossification of many epiphyses and carpal bones, curvilinear calcifications in some joints, fusion of the ischiopubic rami, calcification of many costal cartilages and thick sclerotic base of the skull were a few of the significant findings. On the basis of the clinical and radiological features, the condition has been named "spondylo-epi-metaphyseal dysplasia: mixed type".

Abnormalities, Multiple↗
PubMed2000

Spontaneous intraperitoneal expulsion of an unruptured hydatid cyst.

We report a 43-year-old man with a 20 x 20 cm hydatid cyst, spontaneously extruded out from the left lobe of the liver. This complication of hydatid cyst has not been recorded earlier, and makes the case unique in itself and worth reporting. The patient presented with a rare complication of biliary peritonitis of hydatid disease.

Abdominal Pain↗
PubMed1996

Possible role of tumor necrosis factor-alpha in erythropoietic suppression by endotoxin and granulocyte/macrophage colony-stimulating factor.

Injection of bacterial endotoxin or granulocyte/macrophage colony-stimulating factor (GM-CSF) into exhypoxic polycythemic mice simultaneously with erythropoietin (EPO) suppressed erythroid cell formation, as monitored by 59Fe incorporation into circulating red blood cells. This effect was dose-dependent and time-dependent. GM-CSF did not inhibit erythroid cell formation directly, as the antibody to the GM-CSF did not neutralize the effect of endotoxin, the inducer of GM-CSF. The suppression of both agents could be partially corrected by prior injection of a monoclonal antibody to tumor necrosis factor alpha (anti-TNF alpha). These results indicate that the suppression of EPO-induced erythroid cell formation by endotoxin and GM-CSF was due in part to the production of TNF alpha.

Animals↗
PubMed1995

Characterization of erythropoietin dimerization.

Recombinant human erythropoietin (rHuEPO) is a monomeric glycoprotein hormone when stored under refrigeration. Higher temperatures and various formulation conditions have shown the monomer to partially dimerize followed by aggregation to higher molecular weight species. To protect the product against aggregation, it is critical to understand this dimerization mechanism. The formation of the dimer was analyzed by matrix-assisted laser desorption time-of-flight mass spectrometry, endoproteinase LysC mapping, and N-terminal sequencing. The dimer was shown to have an average molecular mass of 53.5 kDa vs 27.8 kDa for the monomer. The dimer to monomer ratio of 1.9 instead of 2 seemed to be caused by some loss of sialic acids during the purification. The LysC map of the dimer also showed two new peptide peaks not present in the monomer. The sequencing of the new peptides revealed the presence of two types of EPO dimers. The data indicate the dimerization mechanism to involve an initial reduction of the Cys7-Cys161 disulfide bond and subsequent random reoxidation of the free thiols across two EPO molecules. The absence of free thiols in the dimer was confirmed by a fluorescent thiol probe. The higher molecular weight aggregation followed from random intermolecular reoxidation of Cys7 and Cys161.

Amino Acid Sequence↗