Cell Adhesion Molecules: Implications in Neurological by Lisette Leyton Ph.D., James S. Hagood M.D. (auth.), Vladimir

By Lisette Leyton Ph.D., James S. Hagood M.D. (auth.), Vladimir Berezin, Peter S. Walmod (eds.)

Cell Adhesion Molecules: Implications in Neurological ailments includes evaluate articles on fresh advancements within the box of neural phone adhesion molecules (CAMs). the focus is at the function of cellphone adhesion molecules in a variety of neurological and neurodegenerative ailments. this angle has been basically ignored in lately released books on neural CAMs. moreover, the members conceal many newly pointed out telephone adhesion molecules and a few that experience now not obtained a lot awareness in recent times. This books fills an immense hole within the at present to be had literature. ​

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2 Structural Features of the Extracellular Region of CAR After cleavage of the signal peptide, the mature CAR exhibits a 218 amino acid extracellular domain, which represents about two-third of the protein and comprises two Ig-like domains: one membrane-distal V-type Ig domain and one membrane-proximal C2-type Ig domain (termed D1 and D2 in the following). These two domains are separated by a short junction and are followed by a linker of five, a transmembrane segment of 21, and a cytoplasmic tail of either 107 or 94 amino acid residues, respectively.

2010). The D1–D1-binding interface of CAR has a size of 684 Å2 and is formed by side chains in β-strands GFCC′ and C″ as well as the FG-connecting loop. Four salt bridges and two hydrogen bonds as well as two hydrophobic interactions are implicated in binding (Fig. 3b). Similar observations on the D1 domain were made for the complex of D1 with the fiber knob of the adenovirus and for the homodimer 2 The IgCAMs CAR, BT-IgSF, and CLMP: Structure, Function, and Diseases 25 Fig. 3 (a) Crystal structure of the extracellular region of CAR reveals a U-shaped dimer which is stabilized by binding of their N-terminal D1 domains.

Hematopoietic and stromal stem cells in an undifferentiated state express Thy-1, whereas in neurons, Thy-1 is developmentally regulated and associated with cessation of neurite outgrowth. In the nervous system, Thy-1 is known to modify the phenotypes of neurons and astrocytes and to mediate their interaction, functioning as an adhesion molecule via interactions with integrins and Syndecan-4. It is known that Thy-1 regulates signaling both in trans and in cis. Thy-1 is known to interact also with itself, the reggie proteins, and SFK and to modulate intracellular signaling despite lacking a transmembrane domain.

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