Evaluation of an Immunochromatographic Assay as a Canine Rabies Surveillance Tool in Goa, India.

Rabies is a fatal zoonotic disease transmitted by the bite of a rabid animal. More than 95% of the human rabies cases in India are attributed to exposure to rabid dogs. This study evaluated the utility of a lateral flow immunochromatographic assay (LFA) (Anigen Rapid Rabies Ag Test Kit, Bionote, Hwaseong-si, Korea) for rapid post mortem diagnosis of rabies in dogs.

The problem of stray dogs.

The effective management of stray dogs is critically important in any rabies vaccination programme. In many rabies-endemic countries, stray dogs represent a significant proportion of both the free-roaming and total dog populations, and to ensure that rabies elimination programmes are successful, it is essential that this portion of the dog population (stray dogs) is vaccinated at high coverage. However, there are a number of challenges to managing and delivering rabies vaccinations to stray dogs.

Investigation of productivity in a south Indian Malabari goat herd shows opportunities for planned animal health management to improve food security.

Here the authors report the objective veterinary clinical measurement of productivity in a representative south Indian Malabari goat herd. The authors show failure to meet pragmatic production targets that are commensurate with the animals' genetic potential or adequate to meet the demands of global food security. The authors suggest that this situation may have arisen as a consequence of animal husbandry constraints and protein undernutrition and imply the involvement of nematode parasitism.

Immune cell profile in infants' lung tissue.

Little is known about the normal immune cell profile in the lungs of infants without pulmonary disease. Normal lung samples obtained at autopsy of 10 infants that died either due to incidental or inflicted causes or non-pulmonary diseases were stained for antibodies against B and T lymphocytes, macrophages, NK cells, cytotoxic cells, dendritic cells and mast cells. Cells were quantified in the airway epithelial layer, inner layer (between the epithelium and the outer smooth muscle border), outer layer (between the outer smooth muscle border and the external limits of the airway) and alveolar septa.

Bcl-2 is a monomeric protein: prevention of homodimerization by structural constraints.

The pro-apoptotic activity of the Bcl-2 family member Bax has been shown to be facilitated by homodimerization. However, it is unknown whether Bcl-2 or Bcl-x(L) have to homodimerize to protect cells from apoptosis. Here we show by co-immunoprecipitation and FPLC analyses that while Bax multimerizes and forms heterodimers with Bcl-2, there is no evidence for Bcl-2 homodimerization, even in conditions under which Bcl-2 protects cells from apoptosis.

Defects in the ubiquitin pathway induce caspase-independent apoptosis blocked by Bcl-2.

Apoptosis requires the activation of caspases (formerly interleukin 1beta-converting enzyme-like proteases), in particular those related to the caspase-3/7/6 subfamily. Recent data, however, revealed that, although caspase-specific inhibitors delay apoptosis, they are often incapable of preventing it. To obtain evidence for caspase-independent steps of apoptosis, we artificially created a high amount of short-lived or aberrant proteins by blocking the ubiquitin degradation pathway.

The binding properties and biological activities of Bcl-2 and Bax in cells exposed to apoptotic stimuli.

The oncogene product Bcl-2 protects cells from apoptosis whereas its homolog Bax functions to kill cells. Several binding partners of Bcl-2 and Bax have been isolated, but none of them has yet provided clues as to exactly how Bcl-2 and Bax work. According to one view, Bcl-2 and Bax interact with survival and death effector molecules, respectively, and neutralize each other through heterodimerization.

Role of an acidic compartment in tumor-necrosis-factor-alpha-induced production of ceramide, activation of caspase-3 and apoptosis.

Tumor necrosis factor-alpha (TNF-alpha) apoptosis by recruiting a complex of cytosolic proteins at its plasma membrane receptor. Among them is caspase-8, an interleukin-1beta-converting enzyme (ICE)-like protease that initiates an amplified protease cascade to activate the cell-death machinery. The latter comprises at least caspase-3 and caspase-7, which execute cell death by cleaving numerous protein substrates, including poly(ADP-ribose) polymerase.

Bcl-2 does not require Raf kinase activity for its death-protective function.

It has been widely accepted that the oncogene product bcl-2 protects mammalian cells from programmed cell death (apoptosis). The molecules and signalling pathways upon which bcl-2 acts are, however, still ill-defined. Recently, bcl-2 was shown to interact with c-raf-1 in vitro.

Bcl-2 overexpression blocks activation of the death protease CPP32/Yama/apopain.

The C. elegans gene product ced-9 inhibits programmed cell death by negatively regulating the death-mediating protease ced-3. The mammalian homolog of ced-9 is the oncoprotein Bcl-2.