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The protein encoded by this gene is similar to insulin in function and structure and is a member of a family of proteins involved in mediating growth and development. The encoded protein is processed from a precursor, bound by a specific receptor, and secreted. Defects in this gene are a cause of insulin-like growth factor I deficiency. Several transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Mar 2009]

GPM6B belongs to the myelin proteolipid protein family and is implicated in neural development. It is expressed in neurons and glia; cerebellar Bergmann glia, in glia within white matter tracts of the cerebellum and cerebrum, and in embryonic dorsal root ganglia.

SPARC (secreted protein acidic and rich in cysteine) is a phosphorylated, acidic, glycine-rich glycoprotein that is secreted by endothelial cells and is present in large amounts in the parietal endoderm of mouse embryos and in human placenta. SPARC-like protein 1 (SPARCL1), also known as high endothelial venule protein (Hevin) or MAST9, is a 664 amino acid member of the SPARC family of proteins. Highly expressed in lymph node, heart, lung, brain, skeletal muscle, ovary, colon and small inte

Mammalian ferritins consist of 24 subunits made up of two types of poly-peptide chains, ferritin heavy chain and ferritin light chain, which each have unique functions. Ferritin heavy chains catalyze the first step in iron storage, the oxidation of FeII, whereas ferritin light chains promote the nucleation of ferrihydrite, enabling storage of FeIII. The most prominent role of mamma-lian ferritins is to provide iron-buffering capacity to cells. In addition to iron buffering, heavy chain ferriti

Mammalian ferritins consist of 24 subunits made up of two types of poly-peptide chains, ferritin heavy chain and ferritin light chain, which each have unique functions. Ferritin heavy chains catalyze the first step in iron storage, the oxidation of FeII, whereas ferritin light chains promote the nucleation of ferrihydrite, enabling storage of FeIII. The most prominent role of mamma-lian ferritins is to provide iron-buffering capacity to cells. In addition to iron buffering, heavy chain ferriti

Mammalian ferritins consist of 24 subunits made up of two types of poly-peptide chains, ferritin heavy chain and ferritin light chain, which each have unique functions. Ferritin heavy chains catalyze the first step in iron storage, the oxidation of FeII, whereas ferritin light chains promote the nucleation of ferrihydrite, enabling storage of FeIII. The most prominent role of mamma-lian ferritins is to provide iron-buffering capacity to cells. In addition to iron buffering, heavy chain ferriti