Community hub
Recent from talks
Knowledge base stats:
Talk channels stats:
Members stats:
Type IV collagen
Collagen IV (ColIV or Col4) is a type of collagen found primarily in the basal lamina. The collagen IV C4 domain at the C-terminus is not removed in post-translational processing, and the fibers link head-to-head, rather than in parallel. Also, collagen IV lacks the regular glycine in every third residue necessary for the tight, collagen helix. This makes the overall arrangement more sloppy with kinks. These two features cause the collagen to form in a sheet, the form of the basal lamina. Collagen IV is the more common usage, as opposed to the older terminology of "type-IV collagen".[citation needed] Collagen IV exists in all metazoan phyla, to whom it served as an evolutionary stepping stone to multicellularity.
There are six human genes associated with it:
Type IV collagen is a type of collagen that is responsible for providing a scaffold for stability and assembly. It is also predominantly found in extracellular basement membranes. It aids in cell adhesion, migration, survival, expansion, and differentiation.
To begin, this type of collagen is synthesized by the assembly of a specific trimer, when the three NC1 domains initiate molecular interactions between the three α-chains. Protomer trimerization then proceeds from the carboxy terminus to yield the fully assembled protomer. The next step in assembly is collagen IV dimerization. Two collagen IV protomers associate through the carboxy-terminal NC1 trimer to form the NC1 hexamer. These interactions form the core of the type IV collagen scaffold. The scaffold evolves into a collagen IV superstructure by "end-to-end" and lateral connections between collagen IV protomers. The collagen molecule is then formed. Lastly, the type IV collagen molecules bind together to form a complex protein network.
To summarize, the process of collagen synthesis occurs mainly in the cells of fibroblasts which are specialized cells with the main function of synthesizing collagen. Collagen synthesis occurs both intracellularly and extracellularly. However, when looking specifically at type IV collagen, it is mostly synthesized extracellularly.
The C4 Domain at the C-terminus is not removed in the post-translational process, and as a result, the structure of the fibers are linked in a "head-to-head" format instead of in a parallel fashion. It also lacks a glycine in every third amino acid residue that is responsible for the tight collagen helix, as a result it will be more flexible and kinked than other types of collagen.
The most common collagen is type I collagen which makes up 90% of all collagen. It is found in all dermal layers at high proportions while type IV collagen is only found at the basement membrane of the epidermal junction. Despite their differences in commonality, they are both strongly altered during aging or cancer progression.[citation needed]
Depending on genetic and nongenetic factors including alterations in gene expression, splice variations, post-translational modifications, and the chain-specific assembly of particular α-chains, different organs can be affected during their development and in the adult life span.
Hub AI
Type IV collagen AI simulator
(@Type IV collagen_simulator)
Type IV collagen
Collagen IV (ColIV or Col4) is a type of collagen found primarily in the basal lamina. The collagen IV C4 domain at the C-terminus is not removed in post-translational processing, and the fibers link head-to-head, rather than in parallel. Also, collagen IV lacks the regular glycine in every third residue necessary for the tight, collagen helix. This makes the overall arrangement more sloppy with kinks. These two features cause the collagen to form in a sheet, the form of the basal lamina. Collagen IV is the more common usage, as opposed to the older terminology of "type-IV collagen".[citation needed] Collagen IV exists in all metazoan phyla, to whom it served as an evolutionary stepping stone to multicellularity.
There are six human genes associated with it:
Type IV collagen is a type of collagen that is responsible for providing a scaffold for stability and assembly. It is also predominantly found in extracellular basement membranes. It aids in cell adhesion, migration, survival, expansion, and differentiation.
To begin, this type of collagen is synthesized by the assembly of a specific trimer, when the three NC1 domains initiate molecular interactions between the three α-chains. Protomer trimerization then proceeds from the carboxy terminus to yield the fully assembled protomer. The next step in assembly is collagen IV dimerization. Two collagen IV protomers associate through the carboxy-terminal NC1 trimer to form the NC1 hexamer. These interactions form the core of the type IV collagen scaffold. The scaffold evolves into a collagen IV superstructure by "end-to-end" and lateral connections between collagen IV protomers. The collagen molecule is then formed. Lastly, the type IV collagen molecules bind together to form a complex protein network.
To summarize, the process of collagen synthesis occurs mainly in the cells of fibroblasts which are specialized cells with the main function of synthesizing collagen. Collagen synthesis occurs both intracellularly and extracellularly. However, when looking specifically at type IV collagen, it is mostly synthesized extracellularly.
The C4 Domain at the C-terminus is not removed in the post-translational process, and as a result, the structure of the fibers are linked in a "head-to-head" format instead of in a parallel fashion. It also lacks a glycine in every third amino acid residue that is responsible for the tight collagen helix, as a result it will be more flexible and kinked than other types of collagen.
The most common collagen is type I collagen which makes up 90% of all collagen. It is found in all dermal layers at high proportions while type IV collagen is only found at the basement membrane of the epidermal junction. Despite their differences in commonality, they are both strongly altered during aging or cancer progression.[citation needed]
Depending on genetic and nongenetic factors including alterations in gene expression, splice variations, post-translational modifications, and the chain-specific assembly of particular α-chains, different organs can be affected during their development and in the adult life span.