These observations suggest that both wavelength and cell type influence the cell proliferation response to low-intensity laser irradiation.

Spectrin is a major cytoskeletal component of the brain. At least 2 distinct spectrin subtypes are found in mammalian brain: brain spectrin(240/235) and brain spectrin(240/235E). In the present study spectrin subtypes were localized in the adult mouse brain by immunoelectron microscopy using antibodies that recognize each subtype. Brain spectrin (240/235E) was concentrated in neuronal cell bodies, dendrites, and postsynaptic terminals. It was also prominently associated with the plasma membrane, microtubules, filaments, mitochondria, endoplasmic reticulum, and nuclear envelope, and it appeared to interconnect structural elements within the cell. Brain spectrin(240/235E) also was localized to the plasma membrane, nuclear envelope, and cytoplasmic organelles of glial cell bodies. Brain spectrin(240/235) was detected in axons and presynaptic elements, where it was associated with the plasma membrane, microtubules, filaments, synaptic vesicles, and mitochondria. These results show that (1) spectrin is distributed throughout the cytoplasm of neural cells, (2) the location of spectrin is dependent on subtype, and (3) the cytoplasmic surface of plasma membrane and organelles contains an extensive and intricate spectrin meshwork.Brain spectrin is an analog of erythrocyte spectrin, which, like its erythrocyte counterpart, is an elongated fibrous protein of 2000 8, contour length, with a molecular weight of 1 x lo6 Da and an (c@)* tetrameric subunit composition (for review, see Zagon, 1984, 1986). The a-subunits of brain and red blood cell (rbc) spectrin have an apparent molecular weight of 240 kDa, while the p-subunits are 235 kDa (brain) and 220 kDa (rbc). Other similarities between brain and rbc spectrin include binding sites for actin at the terminal ends of the molecule (Glenney et al., 1982) a binding site for brain ankyrin 800 A from the end of the p-subunit (Davis and Bennett, 1984) a binding site for brain protein 4.1 at the ends of the molecule (Goodman and Zagon, 1986) and a phosphorylated P-subunit (Goodman et al., 1983). In the case of mammalian brain spectrin, both the 01-and P-subunits are distinct gene products from rbc spectrin 01-and P-subunits (for reviews, see Zagon, 1984, 1986).Fodrin, a molecule we now know to be equivalent to brain spectrin, has been localized to the cortical cytoplasm of guinea pig neuronal cell bodies, axons, and dendrites, as well as Schwann cells (Levine and Willard, 198 l), using an antibody directed against the 24@ kDa a-subunit of brain spectrin . Zagon et al. (1984) using an antibody against mouse rbc spectrin, which detected 240 and 235 kDa polypeptides exclu- Received Nov. 21, 1985; revised Jan. 27, 1986; accepted Mar. 28, 1986. This work was supported in part by NIH Grants NS-21246, NS-20623, and NS-20500 (I.S.Z.), and Grants NS-19357 and HL-26059 (S.R.G. sively on immunoautoradiography of total mouse brain protein, localized brain spectrin to neuronal cell bodies and dendrites, but not axons. Staining of glial cell bodies with rbc spectrin antibody was also obser...

While the duration and size of human clinical trials may be difficult to reduce, there are several parameters in pre-clinical vaccine development that may be possible to further optimise. By increasing the accuracy of the models used for pre-clinical vaccine testing, it should be possible to increase the probability that any particular vaccine candidate will be successful in human trials. In addition, an improved model will allow the collection of increasingly more-informative data in pre-clinical tests, thus aiding the rational design and formulation of candidates entered into clinical evaluation. An acceleration and increase in sophistication of pre-clinical vaccine development will thus require the advent of more physiologically-accurate models of the human immune system, coupled with substantial advances in the mechanistic understanding of vaccine efficacy, achieved by using this model. We believe the best viable option available is to use human cells and/or tissues in a functional in vitro model of human physiology. Not only will this more accurately model human diseases, it will also eliminate any ethical, moral and scientific issues involved with use of live humans and animals. An in vitro model, termed “MIMIC” (Modular IMmune In vitro Construct), was designed and developed to reflect the human immune system in a well-based format. The MIMIC® System is a laboratory-based methodology that replicates the human immune system response. It is highly automated, and can be used to simulate a clinical trial for a diverse population, without putting human subjects at risk. The MIMIC System uses the circulating immune cells of individual donors to recapitulate each individual human immune response by maintaining the autonomy of the donor. Thus, an in vitro test system has been created that is functionally equivalent to the donor's own immune system and is designed to respond in a similar manner to the in vivo response.

Results suggest that prophylactic percutaneous laser disk ablation is associated with few complications and may reduce the risk of recurrence of signs of intervertebral disk disease in dogs.

Results indicated that the CO2 laser caused less thermal injury at margins of skin biopsy specimens; therefore, if a surgical laser is used for removal of cutaneous masses or to obtain skin biopsy specimens, use of the CO2 laser is recommended. Veterinarians performing a biopsy by using a surgical laser should be aware that laser-induced artifacts may render small biopsy specimens useless for providing accurate histologic diagnosis.