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  • 1
    ISSN: 1058-8388
    Keywords: TIMP-3 ; Metalloproteinases ; Extracellular matrix ; Epithelium ; Cartilage ; Muscle ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Remodeling of the extracellular matrix (ECM) is an essential component of normal development and is also involved in the pathogenesis of arthritis and the spread of cancer. The matrix metalloproteinases and their natural inhibitors, the tissue inhibitors of metalloproteinases (TIMPs), play an important role in this context. We have isolated mouse cDNA clones encoding a novel member of the TIMP family, designated TIMP-3. We have assigned the Timp-3 locus to the [C1-D1] region of mouse chromosome 10 using both genetic and cytogenetic methods. The conceptual translation product of the Timp-3 cDNA shows a high degree of similarity with ChIMP-3, a recently cloned chicken metalloproteinase inhibitor, as well as significant structural similarity with the amino acid sequences of the previously isolated members of this family, TIMP-1 and TIMP-2. The pattern of expression of Timp-3 in the developing mouse embryo is distinct from that previously reported for Timp-1. Timp-3 is expressed in cartilage and skeletal muscle, in myocardium, in the skin, oral and nasal epithelium, in the newborn mouse liver, in the epithelium of some tubular structures such as the developing bronchial tree, oesophagus, colon, urogenital sinus, bile duct, in the kidney, salivary glands, and in the choroid plexus of the brain. The patterns of Timp-3 expression in surface epithelia and in the epithelial lining of many tubular organs suggests that TIMP-3 may be involved in regulating ECM remodeling during the folding of epithelia and during the formation, branching, and expansion of epithelial tubes. In the mouse placenta, expression is seen in the trophoblast, raising the possibility that TIMP-3 may be involved in regulating trophoblastic invasion of the uterus. We propose a role for TIMP-3 in musculoskeletal and cardiac development, in the morphogenesis of certain epithelial structures, and placental implantation. © 1994 Wiley-Liss, Inc.
    Additional Material: 14 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 247 (1987), S. 105-109 
    ISSN: 1432-0878
    Keywords: Collagen ; Fibrillogenesis ; Chick tibia ; Amino propeptide ; Carboxyl propeptide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Collagen fibrillogenesis was studied in tibiae of chick embryos, 9, 11, and 14 days old. Specimens were incubated with antibodies against the amino and the carboxyl propeptides of type-I collagen and subjected to ferritin-la-belling immuno-electron microscopy. The amino propeptide was found in thin fibrils, 20–40 nm in diameter, distributed at 60-nm periodicity. The carboxyl propeptide antibody labelled a wide spectrum of fibrils, although the majority were in the range of 40–100 nm, distinctly larger than those labelled with the amino propeptide antibody. The presence of pN (amino propeptide plus collagen) and pC (carboxyl propeptide plus collagen) collagen was also demonstrated by Western blotting in all specimens. This study suggests that the sequence of propeptide removal may regulate collagen fibril diameter.
    Type of Medium: Electronic Resource
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