Search results for C9

Showing 16 results out of 17

×

Species

Types

Compartments

Reaction types

Search properties

Species

Types

Compartments

Reaction types

Search properties

Protein (3 results from a total of 3)

Identifier: R-HSA-173717
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: C9: P02748
Identifier: R-HSA-68730
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PSMA4: P25789
Identifier: R-HSA-174324
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: PSMA4: P25789

Set (1 results from a total of 1)

Identifier: R-HSA-8852568
Species: Homo sapiens
Compartment: extracellular region

Complex (4 results from a total of 4)

Identifier: R-HSA-8852569
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-2530426
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-2530442
Species: Homo sapiens
Compartment: extracellular region

C8

Identifier: R-HSA-173713
Species: Homo sapiens
Compartment: extracellular region

Reaction (5 results from a total of 6)

Identifier: R-HSA-173725
Species: Homo sapiens
Compartment: external side of plasma membrane
The membrane attack complex (MAC) is the cytolytic end product of the complement cascade, composed of one C5:C6:C7:C8 complex and 12 to 15 C9 molecules (Podack et al. 1982, Biesecker et al. 1993). 12 C9 molecules are represented in this reaction. C9 peptides polymerize to form a ring-shaped transmembrane channel, which causes osmotic lysis of the target cell (Kondos et al. 2010). While formation of a pore is typically associated with necrotic cell death, there is evidence of membrane permeabilization from MACs containing one C9 molecule per C5b–8 complex (Sims et al. 1983).
Identifier: R-HSA-8852580
Species: Homo sapiens
Compartment: extracellular region
Clusterin is a dimer of two fragments of the same translation product, which are disulfide bonded by five cysteines on each peptide (Tobe et al. 1991). It is able to modulate the terminal complement cascade in vitro and prevent cellular lysis by the membrane attack complex (MAC), C5b-9. Clusterin forms complexes with C5b:C6:C7, or C5b:C6:C7:C8 or C5b:C6:C7:C8:C9, as the proteins assemble into the amphiphilic MAC. Clusterin binding renders the complexes soluble and lytically inactive (Jenne & Tschopp 1989, Choi et al. 1989, Murphy et al. 1989, Tschopp et al. 1993).
Identifier: R-HSA-2530429
Species: Homo sapiens
Compartment: extracellular region
Complement proteins C8 and C9 can bind to VTN:C5b:C6:C7 to form soluble C5b-C9 complex in plasma. The vitronectin binding to C5b-C9 complex prevents C9 polymerization by rendering it water-soluble and lytic inactive.
Identifier: R-HSA-2530445
Species: Homo sapiens
Compartment: plasma membrane, extracellular region
CD59, the major inhibitor of the complement membrane attack complex, is an 18–20 kDa glycoprotein, linked to the membrane via a glycosylphosphatidylinositol (GPI)-anchor. It interacts with complement components C8 and C9 during assembly of the membrane attack complex (MAC) and inhibits C9 polymerization, thus preventing the formation of MAC [Lehto T and Meri S. 1993;Rollins SA et al 1991]
Identifier: R-HSA-2464822
Species: Homo sapiens
Compartment: cytosol, photoreceptor inner segment membrane
The reversible, NADP(H)-dependent reduction of all-trans-retinal (atRAL) to all-trans-retinol (atROL) occurs in both rod and cone photoreceptor cells where multiple retinol dehydrogenases (RHDs) are located. RHDs belong to the short-chain dehydrogenase/reductase (SDR) superfamily. RDH12 (located in photoreceptor inner segments) is partially responsible, together with other RDHs, for mediating this reaction (Belyaeva et al. 2005).

Pathway (1 results from a total of 1)

Identifier: R-HSA-166665
Species: Homo sapiens
After cleavage of C5, C5b undergoes conformational changes and exposes a binding site for C6. C5b6 binds C7 resulting in the exposure of membrane binding sites and incorporation into target membranes. The membrane-bound C5b-7 complex can then bind C8. C5b-8 acts as a polymerizing agent for C9. The first C9 bound to C5b-8 undergoes major structural changes enabling formation of an elongated molecule and allows binding of additional C9 molecules and insertion of C9 cylinders into the target membrane. The number of C9 molecules varies from 1-12 in the membrane, although polymers containing up to fifteen C9 molecules are also possible.

Icon (2 results from a total of 2)

C9

Species: Homo sapiens
Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C9 is the pore-forming subunit of the MAC
Species: Homo sapiens
The membrane attack complex (MAC) or terminal complement complex (TCC) is a structure typically formed on the surface of pathogen cell membranes as a result of the activation of the host's complement system, and as such is one of the effector proteins of the immune system. MAC forms transmembrane channels that disrupt the cell membrane of target cells, leading to cell lysis and death. Active MAC is composed of the subunits C5b, C6, C7, C8 and several C9 molecules
Cite Us!