Isolation of Stomatococcus mucilaginosus from drug user with endocarditis.

Stomatococcus mucilaginosus was isolated from the blood of a patient with endocarditis and a past history of drug abuse and aortic valve replacement. At autopsy, Gram stain of the aortic valve revealed gram-positive cocci. Our isolate was atypical for S. mucilaginosus in that colonies were nonmucoid and nonadherent to agar surfaces. Cellular capsules were demonstrated by light and electron microscopy. Phenotypic characteristics identified by conventional methods as well as profile numbers obtained by using two commercial identification systems for staphylococci, the API Staph-Ident and the dms Staph Trac, are presented. Practical tests that differentiate S. mucilaginosus from the genera Micrococcus and Staphylococcus include growth on nutrient agar containing salt and lysostaphin susceptibility. Additional tests that helped differentiate our isolate from group D streptococci included hydrolysis of L-pyrrolidonyl-beta-naphthylamide and streptococcal serogrouping.     

Allergic fungal sinusitis— A clinico-pathological study

The co-existence of fungal elements in allergic nasal Polyposis, has given rise to a distinct clinical entity known as ‘Allergic fungal sinusitis ’ (AF’S). Many a time, these fungal elements may not be diagnosed pre-operatively by routine diagnostic nasal endoscopy or CT scan of paranasal sinuses, due to the florid presentation of nasal polyps, which usually obscure the underlying fungal pathology. The diagnosis is often made intra-operatively. The post-operative confirmation of AFS is by histopathology, fungal smear, fungal culture, allergic murin study and fungal specific IgE titres. We report a series often such cases done in our institution, which highlight that AFS should be considered as a differential diagnosis in Sinonasal Polyposis cases, for their effective management.     

Subselective embolisation in management of JNA

Role of Embolisation in preoperative management of Nasopharyngeal angiofibroma is well established in present day therapeutic modalities. An improvised technique i.e., subselective embolisation has been provided by Interventional radiologists to fortify the therapeutic results. This study compares the final outcome of seven cases, four of which were embolised pre operatively. Each case was dealt with varying surgical approaches.     

Enhancement of cisplatin sensitivity of cisplatin-resistant human cervical carcinoma cells by bryostatin 1.

PURPOSE: Bryostatin 1, a unique protein kinase C (PKC) activator, is already in the clinical trials. An understanding of complex regulation of PKC by bryostatin 1 is essential for effective use of bryostatin 1 in the clinic. We have previously shown that the ability of bryostatin 1 to enhance cisplatin sensitivity correlated with its ability to down-regulate PKCdelta in HeLa cells. We have investigated how bryostatin 1 influences PKCdelta regulation in cisplatin-resistant HeLa (HeLa/CP) cells, and if bryostatin 1 could be used to reverse cisplatin resistance. EXPERIMENTAL DESIGN: Phorbol 12,13-dibutyrate (PDBu), bryostatin 1, and small interfering RNA were used to manipulate PKC level/activation status. Cell death was monitored by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay, Annexin V dye-binding assay, and analysis of hypodiploid peak in a flow cytometer. RESULTS: Bryostatin 1 elicited a biphasic concentration response on PKCdelta down-regulation and cisplatin-induced cell death in HeLa/CP cells; the maximum effect was achieved with 1 nmol/L bryostatin 1. Down-regulation of PKCalpha increased with increasing concentrations of bryostatin 1. PDBu induced down-regulation of PKCalpha in HeLa and HeLa/CP cells but it had little effect on PKCdelta down-regulation in HeLa/CP cells. However, both PDBu and bryostatin 1 enhanced the sensitivity of HeLa/CP cells to cisplatin. Knockdown of PKCdelta by small interfering RNA inhibited cisplatin-induced apoptosis but knockdown of PKCalpha enhanced cisplatin-induced cell death. CONCLUSIONS: These results suggest that although PKCdelta acts as a proapoptotic protein, full-length PKCdelta may inhibit cisplatin-induced cell death. Thus, persistent activation/down-regulation of PKCdelta by bryostatin 1 was associated with cisplatin sensitization. Furthermore, PKCalpha acts as an antiapoptotic protein and down-regulation of PKCalpha by PDBu was associated with cellular sensitization to cisplatin.