Cadherin-8 (CDH8) is a type II classical cadherin from the cadherin superfamily. Member of the Cadherin superfamily are integral membrane proteins that mediate calcium-dependent cell-cell adhesion. Cadherin proteins are composed of a large N-terminal extracellular domain, a single membrane-spanning domain, and a small highly conserved C-terminal cytoplasmic domain. Cadherins are calcium dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells. The extracellular domain of CDH8 contains five cadherin domains. CDH8 is expressed in brain and is putatively involved in synaptic adhesion, axon outgrowth and guidance.
Cell Adhesion Molecules (CAMs) are proteins located on the cell surface involved with the binding with other cells or with the extracellular matrix (ECM) in the process called cell adhesion. These proteins are typically transmembrane receptors and are composed of three domains: an intracellular domain that interacts with the cytoskeleton, a transmembrane domain, and an extracellular domain that interacts either with other CAMs of the same kind (homophilic binding) or with other CAMs or the extracellular matrix (heterophilic binding). Cell adhesion molecule 3, also known as Immunoglobulin superfamily member 4B, CADM3, and NECL1, is a neural tissue-specific immunoglobulin-like cell-cell adhesion molecule which has Ca(2+)-independent homo- or heterophilic cell-cell adhesion activity and plays an important role in the formation of synapses, axon bundles and myelinated axons. Isoform 1 of CADM3 is expressed mainly in adult and fetal brain. Isoform 2 of CADM3 is highly expressed in adult brain and weakly expressed in placenta. In brain, Isoform 2 is highly expressed in cerebellum. CADM3 is involved in the cell-cell adhesion. It has both calcium-independent homophilic cell-cell adhesion activity and calcium-independent heterophilic cell-cell adhesion activity with IGSF4, PVRL1 and PVRL3. The interaction with EPB41L1 may regulate structure or function of cell-cell junctions. CADM3 may act as a tumor suppressor in glioma and loss of it in glioma may be caused by histone deacetylation.
Cell Adhesion Molecular Proteins are proteins located on the cell surface involved with the binding with other cells or with the extracellular matrix in the cell adhesion process. These proteins consists of three domains, an transmembrane domain, an intracellular domain that interacts with the cytoskeleton, and an extracellular domain that interacts with other CAMs of the same kind or with other CAMs or the extracellular matrix. Cell Adhesion Molecular 3 (CADM3) is a neural tissue-specific member of the nectin-like family of immunoglobulin superfamily. CADM3 interacts with EPB41L1 may regulate structure or function of cell-cell junctions. CADM3 has both calcium-independent homophilic cell-cell adhesion activity and calcium-independent heterophilic cell-cell adhesion activity with IGSF4, PVRL1 and PVRL3.
Immunoglobulin superfamily member 4C (IGSF4C), also known as CADM4 or NECL-4, is an immunoglobulin (Ig) superfamily molecule showing significant homology with a lung tumor suppressor, TSLC1. CADM4/IGSF4C/NECL-4 protein is mainly expressed in the kidney, bladder, and prostate in addition to the brain. Experiments have reported the biological significance of CADM4/IGSF4C/NECL-4 in the urinary tissues. An immunohistochemical study reveals that CADM4 is expressed at the cell-cell attachment sites in the renal tubules, the transitional epithelia of the bladder, and the glandular epithelia of the prostate. IGSF4-immunoreactivity (IR) was observed diffusely in the telencephalic wall, whereas it became rather confined to the subplate, the cortical plate and the subventricular zone as the development proceeded. IGSF4-IR gradually decreased after birth and disappeared in adulthood. IGSF4 remained at low levels throughout embryonic stage, whereas it increased after birth. These spatiotemporal patterns of the expression suggest that IGSF4 plays crucial roles in the development of both telencephalon and cerebellum. CADM4/IGSF4C/NECL-4 is ectopically expressed in adult T-cell leukemia (ATL) cells, providing not only a diagnostic marker for ATL, but also a possible therapeutic target against its invasion. The distinct roles of CADM4/IGSF4C/NECL-4 in the oncogenesis of carcinomas and ATL could be due to tissue-specific differences in the downstream cascades, and is a novel concept with respect to cell adhesion in human oncogenesis.
CALCB; also known as CGPR and calcitonin 2; belongs to the calcitonin family. CALCB is a calcitonin (CT) peptide which may play a role in the mediation of human inflammatory diseases. It is highly expressed in the skin; blood; and cerebrospinal fluid. CGRP immunolabeling (IL) was detected in epidermal keratinocytes at levels that were especially high and widespread in the skin of humans from locations afflicted with postherpetic neuralgia (PHN) and complex region pain syndrome type 1 (CRPS); of monkeys infected with simian immunodeficiency virus; and of rats subjected to L5/L6 spinal nerve ligation; sciatic nerve chronic constriction; and subcutaneous injection of complete Freund's adjuvant. Increased CGRP-IL was also detected in epidermal keratinocytes of transgenic mice with keratin-14 promoter driven overexpression of noggin; an antagonist to BMP-4 signaling. CGPR dilates a variety of vessels including the coronary; cerebral and systemic vasculature.
CALCB is a member of the calcitonin family. CALCB is produced in both peripheral and central neurons. It is a potent peptide vasodilator and can function in the transmission of pain. In the spinal cord; the function and expression of CGRP may differ depending on the location of synthesis. CALCB is derived mainly from the cell bodies of motor neurons when synthesized in the ventral horn of the spinal cord and may contribute to the regeneration of nervous tissue after injury.
Calcineurin Subunit B Type 1 belongs to the calcineurin regulatory subunit family. Calcineurin Subunit B Type 1 is a Ser/Thr-specific calcium and calmodulin-dependent protein phosphatase. It is composed of a catalytic subunit (A) and a regulatory subunit (B). It contains four EF-hand domains and four functional calcium-binding sites. Calcineurin Subunit B Type 1 plays an improtant role in the T cell activation pathway.
Calcitonin is a secreted protein which belongs to the calcitonin family. Calcitonin is cleaved into the following two chains: Calcitonin and Katacalcin. Katacalcin is a potent plasma calcium-lowering peptide. Calcitonin is a 32-amino acid linear polypeptide hormone. Calcitonin acts to reduce blood calcium (Ca2+); opposing the effects of parathyroid hormone (PTH). Its importance in humans has not been as well established as its importance in other animals; as its function is usually not significant in the regulation of normal calcium homeostasis. Calcitonin causes a rapid but short-lived drop in the level of calcium and phosphate in blood by promoting the incorporation of those ions in the bones.
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