non-collagenous

The non-collagenous components of extracellular matrix will vary depending on the tissue in which it is found.

This non-collagenous protein is secreted by osteoblasts and plays an essential role in the formation of mineral in bone.

The antigen is a component of the non-collagenous 1 (NC1) domain of the alpha-3 chain of type IV collagen in the glomerular basement membrane.

Non-collagenous domain basement membrane collagen type IV is autoantigen (target antigen) of autoantibodies in the autoimmune disease Goodpasture's syndrome.

BSP is a significant component of the bone extracellular matrix and has been suggested to constitute approximately 8% of all non-collagenous proteins found in bone and cementum.

In osteoporosis, the bone mineral density (BMD) is reduced, bone microarchitecture is disrupted, and the amount and variety of non-collagenous proteins in bone is altered.

The family of non-collagenous proteins known as SIBLING proteins, standing for small integrin-binding ligand, N-linked glycoprotein, are components of the extracellular matrix of bone and dentin.

The large C-terminal ectodomain with a molecular mass of approximately 120 kDa consists of 15 collagenous subdomains, characterized by typical collagenous G-X-Y repeat sequences, flanked by 16 short non-collagenous stretches.

She also is a leading researcher on dentin matrix proteins and is working on cloning phosphophoryn genes, the most abundant non-collagenous extracellular component in dentin, and on synthesizing protein-based templates for bone and dentin regeneration.

Each type IV collagen contains a long triple-helical collagenous domain flanked by a short 7S domain of 25 amino acids and a globular non-collagenous C4 domain of 230 amino acids at the N and C terminus, respectively.

It is believed to be a type II hypersensitivity-like autoimmune reaction to Goodpasture's antigens on the basement membrane of the glomerulus of the kidneys and the pulmonary alveolus, specifically the non-collagenous domain of the alpha-3 chain of Type IV collagen.

It is a non-collagenous SIBLING protein that is later cleaved into three functional proteins: dentin phosphoprotein (also known as phosphophoryn), taken from the C-terminal end, dentin sialoprotein from the N-terminal end, and dentin glycoprotein from the middle of the molecule.