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.
Insulin-like growth factor I (IGF1) belongs to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGFs are generated by proteolytic processing of inactive precursor proteins; which contains the N- and C-terminal propeptide regions. Mature human IGF-I consisting of 70 amino acids has 94% identity with mouse IGF-I and exhibits cross-species activity. IGF-1 binds IGF-IR; IGF-IIR; and the insulin receptor and plays a key role in cell cycle progression; cell proliferation and tumor progression. IGF-1 expression is regulated by growth hormone. R3 IGF-1 is an 83 amino acid analog of IGF-1 comprising the complete human IGF-1 sequence with the substitution of an Arg (R) for the Glu(E) at position three; hence R3; and a 13 amino acid extension peptide at the N terminus. R3 IGF-1 has been produced with the purpose of increasing biological activity. R3 IGF-1 is significantly more potent than human IGF-I in vitro.
Leukocyte-derived arginine aminopeptidase (LRAP), also known as endoplasmic reticulum-aminopeptidase 2 (ERAP2), is the second identified aminopeptidase localized in the in the lumenal side of endoplasmic reticulum (ER) processing antigenic peptides presented to major histocompatibility complex (MHC) class I molecules. It is a 960-amino acid protein with significant homology to placental leucine aminopeptidase and adipocyte-derived leucine aminopeptidase. LRAP preferentially hydrolyzes the basic residues Arg and Lys, and contains the HEXXH(X)18E zinc-binding motif, which is the characteristic of the M1 family of zinc metallopeptidases which also includes PILS/ARTS1/ERAP1 and LNPEP/PLAP. Induced by interferon-gamma, LRAP is able to trim various MHC class I antigenic peptide precursors.
LRG1 belongs to the leucine-rich repeat (LRR) family. Members of this family are involved in protein-protein interaction, signal transduction, and cell adhesion and development. LRG1 is expressed during granulocyte differentiation. It contains 4 LIM zinc-binding domains and 1 Rho-GAP domain.
LRG1 is a secreted protein and contains eight LRR repeats and one LRRCT domain; It can be expressed during granulocyte differentiation. LRG1 has been shown to be involved in protein-protein interaction; signal transduction; cell adhesion and development. Levels of the LRG protein are markedly elevated in acute appendicitis and therefore could be used as a diagnostic aid.
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