GLORIA

GEOMAR Library Ocean Research Information Access

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Developmental patterns of two α1(IX) collagen mRNA isoforms in mouse (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Developmental Dynamics 198 (1993), S. 150-157 
    Details
    ISSN: 1058-8388
    Keywords: Mouse development ; Retina ; Non-pigmented ciliary epithelium ; Col9a1 gene ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Northern blot hybridization, reverse-transcription polymerase chain reaction (RT-PCR), and RNase protection assays were used to examine the expression of twoα1(IX) collagen mRNA species (long and short form) in developing mouse tissues. Furthermore, in situ hybridization was used to identify cells expressing the Col9a1 gene during eye development. The results indicate that during embryonic development eye and heart preferentially express the short form; lung and cartilage express the long form; whereas liver expresses a very low level of long formα1(IX) mRNA which can only be detected by RT-PCR. In situ hybridization demonstrated that at 10.5 day postcoitum (d.p.c.), theα1(IX) collagen mRNAs were first expressed in optic cup (neural ectoderm) but not in lens vesicle (surface ectoderm). By 13.5 d.p.c., the cells that express theα1(IX) mRNA progressively were concentrated to ward the anterior part of the neural retina. By 16.5-18.5 d.p.c., the hybridization signals were found exclusively in the inner non-pigmented layer of the presumptive ciliary epithelium. As ciliary epithelial cells become well differentiated 3 weeks after birth, cells expressing the Col9a1 gene were limited to the junction between mature ciliary folds and the neural retina. No hybridization signal could be detected in ocular tissues of mouse older than 6 weeks. It is of interest to note that a hybridization signal was not detected in cornea at the various developmental stages examined, suggesting that mouse cornea does not significantly expressα1(IX) mRNA during embyronic development. This differs from that of chick cornea development. In summary, the expression of the Col9a1 gene shows a temporospatial pattern throughout mouse eye development. It is suggested that the short form collagen IX may play an important role in eye development. © 1993 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aja.1001980208
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Gene encoding a novel murine tissue inhibitor of metalloproteinases (TIMP), TIMP-3, is expressed in developing mouse epithelia, cartilage, and muscle, and is located on mouse chromosome 10 (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Developmental Dynamics 200 (1994), S. 177-197 
    Details
    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
    URL: http://dx.doi.org/10.1002/aja.1002000302
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Primary structure of the long and short splice variants of mouse collagen XII and their tissue-specific expression during embryonic development (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Developmental Dynamics 204 (1995), S. 432-445 
    Details
    ISSN: 1058-8388
    Keywords: Collagen XII ; Alternative splicing ; Mouse development ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Type XII collagen, a member of the FACIT group of extracellular matrix proteins, consists of molecules that are trimers of α1(XII) chains. The three chains in each molecule form a cross-shaped structure with a central globule from which a triple-helical tail and three finger-like regions (containing von Willebrand factor A-like domains and fibronectin type III repeats) extend. cDNA cloning/sequencing of chicken α1(XII) collagen and protein studies with mouse, bovine, and human material suggest that the α1(XII) collagen gene gives rise to two molecular variants, differing in the length of the finger-like regions, by alternative splicing of the primary transcript. To provide a basis for studies of the function of the two variants in an organism that can be genetically manipulated, we have isolated and sequenced mouse cDNAs encoding both splice variants. The sequence provides the first complete nucleotide and amino acid sequence of mammalian type XII collagen. From these cDNAs we have generated digoxigenin-labeled RNA probes for in situ hybridization of developing mouse embryos to find out whether the splicing mechanism responsible for generation of the two forms is developmentally regulated. The results, combined with Northern blot and RT-PCR analysis of RNA from embryos at various developmental stages, demonstrate that the long form of collagen XII, XIIA, is the predominant form at early stages (ED7 and 11); at later stages of development (ED15 and 17) the short form, XIIB, becomes the major form. As the short form becomes the major product, the long splice variant continues to be expressed in several tissues, even after birth. An exception is dermis, which is positive for the long form up to embryonic day 15, but negative at day 18, when only the short form RNA can be detected. © 1995 wiley-Liss, Inc.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aja.1002040409
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Tissue-specific expression of type XII collagen during mouse embryonic development (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Developmental Dynamics 196 (1993), S. 37-46 
    Details
    ISSN: 1058-8388
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Polyclonal antibodies were raised in rabbits against a fusion peptide representing a portion of the amino-terminal non-triplehelical domain of mouse type XII collagen. The antibodies reacted with bands of 220 and 350 kDa on Western blots of mouse tissue extracts. Immunohistochemical analyses of mouse embryos demonstrated that type XII collagen is expressed mainly in dense connective tissues of tendons, ligaments, dermis, cornea, blood vessel walls, meninges, and developing membranous bones. Comparison of skin extracts and medium of cultured mouse skin fibroblasts by Western blotting showed that while tissues contain short 220 kDa type XII collagen polypeptides as well as the long form, cultured cells produce mainly the long form with 350 kDa polypeptides. © 1993 wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aja.1001960105
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Spatiotemporal pattern of type X collagen gene expression and collagen deposition in embryonic chick vertebrae undergoing endochondral ossification (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 229 (1991), S. 462-472 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: We examined the spatio-temporal pattern of type X collagen mRNA and its protein in the embryonic chick vertebrae undergoing ossification by in situ hybridization and immunohistochemistry. Hypertrophic chondrocytes, producing type X collagen, were developed as islands of cells in a few vertebral body segments of stage 36 embryos. These cells were increased in number at stages 37 and 38 and they expressed high levels of type X collagen mRNA and deposited its protein in the matrix. Blood vessels entered from the perichondrium at stage 37 and invaded deeply into hypertrophic cartilage at stage 38. As the vertebrae grew further at stage 40, the leading front of active hypertrophic chondrocytes with high levels of type X mRNA shifted from the midvertebral perivascular area towards intervertebral borders, while the perivascular area retained a number of inactive hypertrophic chondrocytes with low levels of type X mRNA. Type X collagen was found in large amounts throughout the matrix areas containing both active and inactive hypertrophic chondrocytes. Calcium was detected by von Kossa's technique in hypertrophic cartilage matrix in a small amount at stage 37, in parts of the matrix with type X collagen deposition in succeeding stages, and finally in almost the entire area of type X collagen deposition at stage 45. The vertebral segments of stage 45 embryos also showed a clearly reversed pattern of expression between type X collagen mRNA and types II and IX collagen mRNAs. The results demonstrate that the production of type X collagen by hypertrophic chondrocytes precedes both vascular invasion and mineralization of the matrix, suggesting that hypertrophic chondrocytes have an important role in regulating these events.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092290405
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Amino and carboxyl propeptides in bone collagen fibrils during embryogenesis (1987)
    Springer
    Cell & tissue research 247 (1987), S. 105-109 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00216552
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...