Dendrites, domain structures

A consideration often overlooked in BAM studies is the possible influence of the compression rate on the domain structures. In the case of A-acylamino acid monolayers, the associations due to amide-amide hydrogen bonding are very strong and promote rapid domain growth and also make it unlikely that relaxation to an equilibrium domain shape can occur on any realistic experimental timeframe. Domain shape relaxation kinetics are noted to be dependent on the strength of intermolecular forces for example, dendritic condensed-phase domains formed in a phospholipid monolayer required 5 h to relax to equilibrium shapes and, for the phospholipid DMPE, compression rates as slow as 0.2 per molecule per minute were needed to observe equilibrium domain shapes. Examination of the variation of domain structure with time after then-formation or with compression rates are not commonly reported however, it is advisable to consider examining these variables when carrying out BAM experiments. 

Chung, Y. D., Zhu, J., Han, Y. and Kernan, M. J. nompA encodes a PNS-specific, ZP domain protein required to connect mechanosensory dendrites to sensory structures. Neuron 29 415-428,2001. 

However, only the extracellular domains immediately adjacent to the cell membrane and the (32 microglobulin peptide have clear homology with the immunoglobulin domains. The al and ct2 segments of class I and the al and (31 domains in class II have quite an unusual structure. Class I molecules are present on virtually every cell in the body, the most notable exception being the syncytial trophoblast of the placenta. Class II expression is far more restricted B cells, dendritic cells which present antigen to T cells, and macrophage express abundant class II molecule on their surfaces. However, most other tissues can be induced to express class II molecules under the influence of soluble mediators such as 7-interferon. 

Ion channels are large proteins which form pores through the neuronal membrane. The precise structure and function of the ion channels depend on their physiological function and distribution along the dendrites and cell body. These include specialized neurotransmitter-sensitive receptor channels. In addition, some ion channels are activated by specific metal ions such as sodium or calcium. The structure of the voltage-dependent sodium channel has been shown to consist of a complex protein with both a hydrophilic and a hydrophobic domain, the former domain occurring within the neuronal membrane while the latter domain occurs both inside and outside the neuronal membrane. 

The similarities between the cytoplasmic processes of bones cells and the stereocilia of hair cells are that they both (1) measure mechanical deformations (vibrations of a fluid domain), (2) communicate their measurement to a network, (3) do this with dendritic structures, (4) the dendrites of both cells are constructed of similar materials (e.g., actin and fimbrin) and (5) the initial signaling in both cases consists of opening ion channels. While the hair cells communicate their information to a network that feeds to the brain, the bones cells connect to a lower level network (CCN) with (potentially) local decision-making software. 

C-type lectin receptors (CLRs) are a family of proteins containing one or more structurally-related C-type, lectin-like domains. Transmembrane CLRs which mediate fungal binding include the mannose receptor (MR), Dectin 1, Dectin 2 and the dendritic cell receptor, DC-SIGN (reviewed in). ... 

---