type I collagen


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type I col·la·gen

the most abundant collagen, which forms large well-organized fibrils having high tensile strength.
References in periodicals archive ?
In this paper, a system of co-culture of HKC and HFB under 3.4 kPa pressure were formed to determine the effects on type I collagen, type III collagen, IL-1[alpha] and MMP-3 mRNA expression and the protein concentration of culture supernatant.
Complete primary structure of rainbow trout type I collagen consisting of a1 (I) a3(I) heterotrimers.
Franz, "Quantitative analysis of type I collagen fibril regulation by lumican and decorin using AFM," Journal of Structural Biology, vol.
Mirastschijski, "Tumor necrosis factor-alpha-accelerated degradation of type I collagen in human skin is associated with elevated matrix metalloproteinase (MMP)-1 and MMP-3 ex vivo," European Journal of Cell Biology, vol.
In vivo, type I collagen molecules are assembled into fibrillar or membranes structures when the collagen solution is adjusted to specific concentration of collagen, pH, and ionic strength, which can be applied in the composition of engineering scaffolds of bones, cartilage, skin, muscles, or food packaging engineering materials for its structural features and biological characteristics.
These results that identify collagen from a waste source such as fish processing by-products have also been reported by Nagai and Suzuki (1999) who revealed that type I collagen could be isolated from fish skin bones and fins.
In the above list synthesis of Type I collagen is described.
Type I collagen consists of two identical a1 chains and one different [alpha]2 chain, hence the chain designation for type I collagen is denoted [[[alpha]1(I)].sub.2][alpha]2(I)].
Type I collagen with original concentration of 3.75 mg/ mL was purchased from BD Biosciences (Franklin Lakes, NJ).
Type analysis of the collagen produced indicated that inhibition of the collagen production observed was mainly a reflection of a reduction in type I collagen. The accumulation of pro alpha 1(I) and pro alpha 2(I) mRNAs and the transcriptional activity of these genes were determined in human skin fibroblasts in order to investigate site(s) of regulation of type I collagen production by human EGF in the absence and presence of L-ascorbic acid 2-phosphate (Asc 2-P), a long-acting vitamin C derivative.
Peptan is a type I collagen that typically comprises 92% protein, 7% moisture and 1% ash.