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  2. Interstitial collagenase - Wikipedia

    en.wikipedia.org/wiki/Interstitial_collagenase

    n/a Ensembl n/a n/a UniProt n a n/a RefSeq (mRNA) n/a n/a RefSeq (protein) n/a n/a Location (UCSC) n/a n/a PubMed search n/a n/a Wikidata View/Edit Human Interstitial collagenase, also known as fibroblast collagenase and matrix metalloproteinase-1 (MMP-1), is an enzyme that in humans is encoded by the MMP1 gene. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3 ...

  3. Extracellular matrix - Wikipedia

    en.wikipedia.org/wiki/Extracellular_matrix

    The animal extracellular matrix includes the interstitial matrix and the basement membrane. [7] Interstitial matrix is present between various animal cells (i.e., in the intercellular spaces). Gels of polysaccharides and fibrous proteins fill the interstitial space and act as a compression buffer against the stress placed on the ECM. [8]

  4. Interstitium - Wikipedia

    en.wikipedia.org/wiki/Interstitium

    Three-dimensional schematic of the interstitium, a fluid-filled space supported by a network of collagen. In anatomy, the interstitium is a contiguous fluid-filled space existing between a structural barrier, such as a cell membrane or the skin, and internal structures, such as organs, including muscles and the circulatory system.

  5. Collagen - Wikipedia

    en.wikipedia.org/wiki/Collagen

    Collagen is a vital protein in skin, hair, nails, and other tissues. Its production decreases with age and factors like sun damage and smoking. Collagen supplements, derived from sources like fish and cattle, are marketed to improve skin, hair, and nails. Studies show some skin benefits, but these supplements often contain other beneficial ...

  6. Type V collagen - Wikipedia

    en.wikipedia.org/wiki/Type_V_collagen

    Type V collagen is a part of the Extracellular Matrix (ECM). [5] Collagen V is gene expression modulated by TGF-β. Type V collagen has shown that it is resistant to digestion by interstitial collagenases. Denatured collagen V on the other hand, can be degraded by gelatinases as well as metalloproteinases. [5]

  7. Matrix metalloproteinase - Wikipedia

    en.wikipedia.org/wiki/Matrix_metalloproteinase

    MMPs were described initially by Jerome Gross and Charles Lapiere in 1962, who observed enzymatic activity (collagen triple helix degradation) during tadpole tail metamorphosis (by placing a tadpole tail in a collagen matrix plate). [5] Therefore, the enzyme was named interstitial collagenase .

  8. Chondroblast - Wikipedia

    en.wikipedia.org/wiki/Chondroblast

    The extracellular matrix secreted by chondroblasts is composed of fibers, collagen, hyaluronic acid, proteoglycans, glycoproteins, water, and a host of macromolecules. Within finished cartilage, collagen fibers compose 10-20% of the volume, water 65-80%, and the proteoglycan-hyaluronic acid aggregates the remaining portion.

  9. Cartilage - Wikipedia

    en.wikipedia.org/wiki/Cartilage

    In embryogenesis, the skeletal system is derived from the mesoderm germ layer. Chondrification (also known as chondrogenesis) is the process by which cartilage is formed from condensed mesenchyme tissue, which differentiates into chondroblasts and begins secreting the molecules (aggrecan and collagen type II) that form the extracellular matrix.