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  2. Collagen - Wikipedia

    en.wikipedia.org/wiki/Collagen

    Guiding: collagen fibers guide fibroblasts because they migrate along a connective tissue matrix. Chemotaxis: collagen fibers have a large surface area which attracts fibrogenic cells which help healing. Nucleation: in the presence of certain neutral salt molecules, collagen can act as a nucleating agent causing formation of fibrillar structures.

  3. Type I collagen - Wikipedia

    en.wikipedia.org/wiki/Type_I_collagen

    Type I collagen is the most abundant collagen of the human body, consisting of around 90% of the body's total collagen in vertebrates. Due to this, it is also the most abundant protein type found in all vertebrates. Type I forms large, eosinophilic fibers known as collagen fibers, which make up most of the rope-like dense connective tissue in ...

  4. Fibrillogenesis - Wikipedia

    en.wikipedia.org/wiki/Fibrillogenesis

    Fibrillogenesis is the development of fine fibrils normally present in collagen fibers of connective tissue.It is derived from the New Latin fibrilla (meaning fibrils, or pertaining to fibrils) and Greek genesis (to create, the process by which something is created).

  5. Fibroblast - Wikipedia

    en.wikipedia.org/wiki/Fibroblast

    A fibroblast is a type of biological cell typically with a spindle shape [1] that synthesizes the extracellular matrix and collagen, [2] produces the structural framework for animal tissues, and plays a critical role in wound healing. [3] Fibroblasts are the most common cells of connective tissue in animals.

  6. Type IV collagen - Wikipedia

    en.wikipedia.org/wiki/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 ...

  7. Collagen helix - Wikipedia

    en.wikipedia.org/wiki/Collagen_helix

    In 1954, Ramachandran & Kartha (13, 14) advanced a structure for the collagen triple helix on the basis of fiber diffraction data. It consists of a triple helix made of the repetitious amino acid sequence glycine-X-Y, where X and Y are frequently proline or hydroxyproline. [2] [3] Collagen folded into a triple helix is known as tropocollagen.