ANGPTL4, also known as ANGPTL2, is a protein with hypoxia-induced expression in endothelial cells. It contains 1 fibrinogen C-terminal domain and is expressed at high levels in the placenta, heart, liver, muscle, pancreas and lung but expressed poorly in the brain and kidney. ANGPTL4 inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. It may act as a regulator of angiogenesis and modulate tumorigenesis. It inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. It may also exert a protective function on endothelial cells through an endocrine action. ANGPTL4 is directly involved in regulating glucose homeostasis, lipid metabolism, and insulin sensitivity. In response to hypoxia, the unprocessed form of the protein accumulates in the subendothelial extracellular matrix (ECM). The matrix-associated and immobilized unprocessed form limits the formation of actin stress fibers and focal contacts in the adhering endothelial cells and inhibits their adhesion. It also decreases motility of endothelial cells and inhibits the sprouting and tube formation.
Angiopoietin-like 7 (ANGPTL7) is a secreted glycoprotein that is structurally related to the angiopoietins. Members of this protein family contain an N-terminal coiled coil domain and a C-terminal fibrinogen-like domain. ANGPTL7 shares 89% aa sequence identity with mouse and rat ANGPTL7. It is secreted as a 45-50kDa monomer that forms disulfide-linked homotrimers and tetramers via the coiled coil domain. ANGPTL7 is expressed in the corneal stroma, trabecular meshwork, and sclera and is elevated in glaucoma aqueous humor. Its production is up-regulated in trabecular meshwork cells by glucocorticoids and TGF-β and in cartilage by TNF-α. Overexpression of ANGPTL7 in trabecular meshwork cells inhibits the production of collagen and proteoglycans. When overexpressed in tumor cells it promotes collagen and proteoglycan deposition but inhibits tumor xenograft progression and tumor angiogenesis.
The protein specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thereby improving glucose tolerance. It promotes pancreatic beta cell proliferation without insulin resistance. Also it acts as a blood lipid regulator by regulating serum triglyceride levels and possibly by promoting ANGPTL3 cleavage. It interacts with ANGPTL3. It predominantly expressed in liver and also expressed in adipose tissues. The ability of the protein to induce pancreatic beta cell proliferation is promising in diabetes therapy. Betatrophin treatment could supply or replace insulin injections by increasing the number of insulin-producing cells in diabetes.
Annexin A10 (ANXA10) contains four Annexin repeats and is a member of the Annexin family. Members of this calcium-dependent phospholipid-binding protein family play a role in the regulation of cellular growth and in signal transduction pathways. It is reported that ANXA10 may be a clinical relevant marker for predicting outcome in both early and advanced stages of bladder cancer.
Annexin A13 (ANXA13) belongs to the annexin family which plays a role in phospholipase inhibition, cytoskeletal interactions, intracellular signal transduction pathways and regulation of cellular growth. ANXA13 contains four annexin repeats and a pair of annexin repeats may form one binding site for calcium and phospholipid. ANXA13 is highly expressed in intestinal and kidney epithelial cells. The specific function of ANXA13 has not yet been determined; however it is associated with the plasma membrane of undifferentiated, proliferating crypt epithelial cells as well as differentiated villus enterocytes.
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