Hepatoma-Derived Growth Factor is a original member of the HDGF family. HDGF is a cytoplasmic protein and contains one PWWP domain. HDGF expression levels are high in the nucleus and cytoplasm of smooth muscle and endothelial cells. HDGF has proliferative, angiogenic and neurotrophic activity. HDGF was initially characterized as a secreted mitogen from the Huh-7 human hepatoma cell line. As a heparin-binding protein, which is highly expressed in tumor cells where it stimulates proliferation. HDGF has mitogenic activity for fibroblasts and acts as a transcriptional repressor. It has been shown that HDGF is linked with tumorigenesis and the growth of cancer.
Hepatoma-Derived Growth Factor-Related Protein 3 (HDGFRP3) belongs to the HDGF family. HDGFRP3 can be found in testis, heart, spinal cord and brain. HDGFRP3 localizes to the nucleus and contains one PWWP domain. HDGFRP3 enhances DNA synthesis and may have a role in cell proliferation.
Haloacid Dehalogenase-Like Hydrolase Domain-Containing Protein 22 (HDHD2) is a member of the HAD-like hydrolase superfamily. HDHD2 includes L-2-Haloacid Dehalogenase, Epoxide Hydrolases and Phosphatases. There are two active sites in HDHD2 - an L-2-Haloacid Dehalogenase and a Carboxylate group. The L-2-Haloacid Dehalogenase active site catalyzes the hydrolytic dehalogenation of D- and L-2-Haloalkanoic Acids, producing L- and D-2-Hydroxyalkanoic Acids.
Human CD34 is high glycosylated type I transmembrane protein, and it could act as a scaffold for the attachment of lineage specific glycans, allowing stem cells to bind to lectins expressed by stromal cells or other marrow components. CD34 is found on multipotent precursors, bone marrow stromal cells, embryonic fibroblasts, vascular endothelia, as well as some populations of mesenchymal stem cells, and tumor cell lines, and it is a common marker for diverse progenitors.
Hemojuvelin, also known as HFE2, is a membrane-bound and soluble protein which belongs to the repulsive guidance molecule (RGM) family. It is known that RGMs function through Neogenin, a homologue of the Netrin receptor deleted in colon cancer. In mammals, RGM family consists of three glycoproteins which have discrete expression patterns and functions (RGM-A, RGM-B, and RGM-C). Hemojuvelin is expressed in adult and fetal liver, heart, and skeletal muscle. Hemojuvelin acts as a bone morphogenetic protein (BMP) coreceptor. Enhancement of BMP signaling regulates hepcidin (HAMP) expression and iron metabolism. It plays a key role in iron metabolism. Hemojuvelin represents the cellular receptor for hepcidin. It may be a component of the signaling pathway which activates hepcidin or it may act as a modulator of hepcidin expression. Defects in hemojuvelin are the cause of hemochromatosis type 2A, also known as juvenile hemochromatosis (JH).
Hemopexin (HPX) is plasma glycoprotein belongs to the family of the acute-phase proteins whose synthesis is induced after an inflammatory event. Hemopexin with two four-bladed beta -propeller folds has been found in other proteins including collagenases and provides sites for protein-protein interactions. The liver is the major synthesizing organ. Hemopexin participates in maintaining and recycling the iron pool by utilizing its high binding affinity toward heme composed of protoporphyrin IX and iron. It also functions in preventing oxidation caused by heme after hemolysis. Hydrophobic heme molecules can intercalate into lipid membranes and participate in the oxidation of lipid membrane components through the Fenton reaction resulting in lipid peroxidation. Hemopexin undergoes a conformational change upon the binding of heme. The conformational change allows hemopexin to interact with a specific receptor, forming a complex which is then internalized. Heme concentrations in plasma increase after hemolysis, which is associated with several pathological conditions such as reperfusion injury and ischemia.
Hepatocyte Cell Adhesion Molecule (HEPACAM) is a single-pass type I membrane protein that localizes to the cytoplasmic side of the cell membrane. HEPACAM includes a signal sequence (amino acid 1-33), an extracellular region (amino acid 34-240) with one Ig-like C2-type domain and one Ig-like V-type domain, a transmembrane segment (amino acid 241-261), and a cytoplasmic domain (amino acid 262 - 416). The cytoplasmic domain plays an important role in regulation of cell-matrix adhesion and cell motility. HEPACAM acts as a homodimer and dimer formation occurs predominantly through cis interactions on the cell surface. HEPACAM is involved in cell motility and cell-matrix interactions. The expression of this gene is down-regulated or undetectable in many cancer cell lines, so this may be a tumor suppressor gene.
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