type I collagen

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.

Regulation of Collagen Metabolism in Keratinocyte-Fibroblast Organotypic Co-culture by Pressure

Complete primary structure of rainbow trout type I collagen consisting of a1 (I) a3(I) heterotrimers.

Extraction and Characterization of Collagen from Broiler Chicken Feet (Gallus gallus domesticus)--Biomolecules from Poultry Waste

Franz, "Quantitative analysis of type I collagen fibril regulation by lumican and decorin using AFM," Journal of Structural Biology, vol.

Atomic Force Microscopy for Collagen-Based Nanobiomaterials

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 Situ Cytokine Expression and Morphometric Evaluation of Total Collagen and Collagens Type I and Type III in Keloid Scars

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.

Observing Effects of Calcium/Magnesium Ions and pH Value on the Self-Assembly of Extracted Swine Tendon Collagen by Atomic Force Microscopy

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.

ISOLATION AND CHARACTERISATION OF COLLAGEN FROM THE WASTE MATERIAL OF TWO IMPORTNT FRESHWATER FISH SPECIES

In the above list synthesis of Type I collagen is described.

The extracellular matrix contributes to mechanotransduction in uterine fibroids

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)].

Collagen scaffolds in bone sialoprotein-mediated bone regeneration

Type I collagen with original concentration of 3.75 mg/ mL was purchased from BD Biosciences (Franklin Lakes, NJ).

Cell matrix remodeling ability shown by image spatial correlation

High-level production of human type I collagen in the yeast Pichia pastoris.

Design and construction of two yeast shuttle vectors containing human procollagen genes expression cassette for expression in yeast

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.

Epidermal growth factor inhibits transcription of type I collagen genes and production of type I collagen in cultured human skin fibroblasts in the presence and absence of L-ascorbic acid 2-phosphate, a long-acting vitamin C derivative

Peptan is a type I collagen that typically comprises 92% protein, 7% moisture and 1% ash.

Hydrolyzed collagen: a versatile protein for joint and bone health, nutrition and beauty