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  2. Collagen - Wikipedia

    en.wikipedia.org/wiki/Collagen

    Collagen is also abundant in corneas, blood vessels, the gut, intervertebral discs, and the dentin in teeth. [3] In muscle tissue, it serves as a major component of the endomysium. Collagen constitutes 1% to 2% of muscle tissue and 6% by weight of skeletal muscle. [4] The fibroblast is the most common cell creating collagen in animals.

  3. FACIT collagen - Wikipedia

    en.wikipedia.org/wiki/FACIT_collagen

    FACIT collagen is found in various tissue areas to modulate the surface properties of collagen fibrils and generate tissue-specific three-dimensional patterns in the extracellular matrix. [3] For example, collagen XIV connects the fibrillar networks of the cartilage and skin, [ 3 ] and XII is found in connective tissues, particularly at the ...

  4. C-terminal telopeptide - Wikipedia

    en.wikipedia.org/wiki/C-terminal_telopeptide

    The C-terminal telopeptide (CTX), also known as carboxy-terminal collagen crosslinks, is the C-terminal telopeptide of fibrillar collagens such as collagen type I and type II. It is used as a biomarker in the serum to measure the rate of bone turnover .

  5. Collagen, type III, alpha 1 - Wikipedia

    en.wikipedia.org/wiki/Collagen,_type_III,_alpha_1

    The COL3A1 gene is located on the long (q) arm of chromosome 2 at 2q32.2, between positions 188 974 372 and 189 012 745. The gene has 51 exons and is approximately 40 kbp long. [7] The COL3A1 gene is in tail-to-tail orientation with a gene for another fibrillar collagen, namely COL5A2. [7]

  6. Homogenization (biology) - Wikipedia

    en.wikipedia.org/wiki/Homogenization_(biology)

    If freezing the tissue is possible, cryohomogenization can be performed under "dry" conditions, and is often the method of choice whenever it is desirable to collect several distinct molecular classes (e.g. both protein and RNA) from a single sample, or combined set of samples, or when long-term storage of part of the sample is desired.

  7. Type II collagen - Wikipedia

    en.wikipedia.org/wiki/Type_II_collagen

    Type II collagen is the basis for hyaline cartilage, including the articular cartilages at joint surfaces. It is formed by homotrimers of collagen, type II, alpha 1 chains. It makes up 50% of all protein in cartilage and 85–90% of collagen of articular cartilage.

  8. N-terminal telopeptide - Wikipedia

    en.wikipedia.org/wiki/N-terminal_telopeptide

    The N-terminal telopeptide (NTX), also known as amino-terminal collagen crosslinks, is the N-terminal telopeptide of fibrillar collagens such as collagen type I and type II. It is used as a biomarker to measure the rate of bone turnover. NTX can be measured in the urine (uNTX) or serum (serum NTX). [1]

  9. Type XVIII collagen - Wikipedia

    en.wikipedia.org/wiki/Type_XVIII_collagen

    When type XVIII collagen is mutated at the COL18A1 gene, exon 2 in the sequence is skipped, which results in production of an early termination codon in exon 4 of this gene's transcript. This type of mutation particularly affects only one isoform of type XVIII collagen - the short isoform type, while the medium and long isoforms are unaffected. [5]