LMCD1 is transcriptional cofactor which contains a cysteine-rich domain in the N-terminal region and 2 LIM domains in the C-terminal region. It also has several potential phosphorylation and N-myristoylation sites and a single potential N-glycosylation site. LMCD1 is expressed in many tissues with highest abundance in skeletal muscle. LMCD1 restricts GATA6 function by inhibiting DNA-binding, resulting in repression of GATA6 transcriptional activation of downstream target genes. It plays a critical role in the development of cardiac hypertrophy via activation of calcineurin/nuclear factor of activated T-cells signaling pathway.
CD300C is a single-pass type I membrane protein which belongs to the immunoregulatory signaling (IRS) family. CD300C contains one Ig-like V-type domain and is present on the surface of natural killer cells; granulocytes; most myeloid cells; dendritic cells; and a subpopulation of T and B lymphocytes. The CD300C (CMRF-35A) and CD300A (CMRF-35H) molecules are homologous leukocyte surface proteins. CD300a and CD300C play an important role in the cross-regulation of TNF-alpha and IFN-alpha secretion from pDCs. CD300A and CD300C are indistinguishable on the surface of NK cells. The ligand for CD300C is presently unknown.
The cluster of differentiation (CD) system is commonly used as cell markers in immunophynotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules which associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. CD300 is a glycoprotein family of cell surface molecules that regulate a diverse array of cell processes via their triggering and inhibitory receptor functions. The CD300 family of myeloid immunoglobulin receptors includes activating(CD300b, CD300e) and inhibitory members(CD300a, CD300f), as well as CD300c and CD300d, whose function is uncertain.
The nuclear lamina consists of a two-dimensional matrix of proteins located next to the inner nuclear membrane. The lamin family of proteins make up the matrix and are highly conserved in evolution. During mitosis, the lamina matrix is reversibly disassembled as the lamin proteins are phosphorylated. Lamin proteins are thought to be involved in nuclear stability, chromatin structure and gene expression. Vertebrate lamins consist of two types, A and B. Alternative splicing results in multiple transcript variants. Mutations in this gene lead to several diseases: Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome.
LPL (LipoProtein Lipase, also LIPD) is a 53-56 kDa glycoprotein member of the Lipase family, AB Hydrolase superfamily of molecules. It is produced by multiple cell types, including adipocytes, skelelal muscle cells and macrophages. Once secreted, the circulating enzyme ultimately becomes immobilized on the surface of endothelium by binding to cell surface heparan sulfate. Here, it hydrolyzes triglycerides embedded in chylomicrons and VLDLs by homodimerizing and interacting with apoC2.
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