Search results for ACAN

Showing 15 results out of 37

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Protein (10 results from a total of 32)

Identifier: R-HSA-2105015
Species: Homo sapiens
Compartment: lysosomal lumen
Primary external reference: UniProt: ACAN: P16112
Identifier: R-HSA-2046164
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: ACAN: P16112
Identifier: R-HSA-2046224
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: ACAN: P16112
Identifier: R-HSA-2046287
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: ACAN: P16112
Identifier: R-HSA-2046195
Species: Homo sapiens
Compartment: lysosomal lumen
Primary external reference: UniProt: ACAN: P16112
Identifier: R-HSA-2046278
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: ACAN: P16112
Identifier: R-HSA-2046200
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: ACAN: P16112
Identifier: R-HSA-2046174
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: ACAN: P16112
Identifier: R-HSA-2046207
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: ACAN: P16112
Identifier: R-HSA-2046311
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: ACAN: P16112

Reaction (2 results from a total of 2)

Identifier: R-HSA-8855825
Species: Homo sapiens
Compartment: extracellular region
Extracellular HTRA1 (High-temperature requirement A serine peptidase 1) catalyzes the hydrolysis of a specific peptide bond in ACAN (Aggrecan) (Chamberland et al. 2009; Hu et al. 1998). The enzyme is a homotrimer (Truebestein et al. 2011). HTRA1 is thereby implicated in the degradation of extracellular matrix. Indirect studies in mouse model systems (e.g., Oka et al. 2004) that HTRA1 may modulate the activity of Tgf-beta and thereby play additional roles, not annotated here, in the turnover of extracellular matrix both normally and during inflammation.
Identifier: R-HSA-2318623
Species: Homo sapiens
Compartment: extracellular region
In articular cartilage the major non-fibrous macromolecules are aggrecan, hyaluronan (HA) and hyaluronan and proteoglycan link protein 1 (HAPLN1). The high negative charge density of these molecules leads to the binding of large amounts of water (Bruckner 2006). HA is bound by large aggregating proteoglycans (the hyalectans). Aggrecan (ACAN) is predominantly expressed in cartilage, versican is widely distributed, while brevican and neurocan are largely restricted to nervous tissues. ACAN is ~90% carbohydrate. The core protein is highly glycosylated, mostly by the glycosaminoglycan (GAG) chains chondroitin sulphate (CS) and keratan sulphate (KS). Each ACAN molecule has ~100 CS chains of around 20 kDa and ~60 KS chains of 5-15 kDa. CS is attached to an extended domain between globular domains 2 and 3, while KS is widely distributed. The core protein also contains sites for the attachment of N-linked and O-linked oligosaccharides (Nilsson et al. 1982).

The G1 N-terminal domain of ACAN has a lectin-like binding site with high affinity for HA (Watanabe et al. 1997, Hardingham 2006). HA is a long unbranched, unsulphated GAG synthesized free from protein attachment by three HA synthases (Spicer & McDonald 1998). It has an average molecular weight of several million Da. HA content steadily rises in aging cartilage and can reach 10% of the total GAG. ACAN, HA and the small glycoprotein HAPLN1, known as Link protein, are found in huge multi-molecular aggregates comprised of numerous ACAN monomers non-covalently bound to HA, stabilized by HAPLN1 which forms a ternary complex with the G1 domain of ACAN and HA (Ratcliffe & Hardingham 1983, Grover & Roughley 1994, Kiani et al. 2002).

Set (3 results from a total of 3)

Identifier: R-HSA-8855843
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-8855819
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-2318622
Species: Homo sapiens
Compartment: extracellular region
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