Collagen Type IV (COL IV) ELISA Kit for Mouse

This gene encodes the major type IV alpha collagen chain of basement membranes. Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter. [provided by RefSeq, Jul 2008]

Function: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. Ref.12 Ref.17 Ref.18 Ref.19Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin. Ref.12 Ref.17 Ref.18 Ref.19

Subunit structure: There are six type IV collagen isoforms, alpha 1(IV)-alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network.

Subcellular location: Secreted › extracellular space › extracellular matrix › basement membrane.

Tissue specificity: Highly expressed in placenta. Ref.12 Ref.17

Domain: Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain.

Post-translational modification: Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in all cases and bind carbohydrates.Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens.The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues.Proteolytic processing produces the C-terminal NC1 peptide, arresten.

Involvement in disease: Brain small vessel disease with hemorrhage (BSVDH) [MIM:607595]: Brain small vessel diseases underlie 20 to 30 percent of ischemic strokes and a larger proportion of intracerebral hemorrhages. Inheritance is autosomal dominant.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23 Ref.24 Ref.27 Ref.30 Ref.31Hereditary angiopathy with nephropathy aneurysms and muscle cramps (HANAC) [MIM:611773]: The clinical renal manifestations include hematuria and bilateral large cysts. Histologic analysis revealed complex basement membrane defects in kidney and skin. The systemic angiopathy appears to affect both small vessels and large arteries.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.25 Ref.29Porencephaly 1 (POREN1) [MIM:175780]: A neurologic disorder characterized by a fluid-filled cysts or cavities within the cerebral hemispheres, neurologic manifestations, facial paresis, and visual defects. Affected individuals typically have hemiplegia, seizures, and intellectual disability. Porencephaly type 1 is usually unilateral and results from focal destructive lesions such as fetal vascular occlusion or birth trauma.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21 Ref.22 Ref.28

Sequence similarities: Belongs to the type IV collagen family.Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain.