Localization of Collagen Types in Tissues

K, von der Mark

doi:10.1016/b978-0-12-363709-3.50012-7

Cited by 153 publications

(54 citation statements)

References 329 publications

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“…It was long considered specific for cartilage where it is the major constituent of the extracellular matrix and forms heterotypic fibrils with minor collagen types IX and XI (Mendler et al, 1989). Later type I1 collagen was also detected in the vitreous of the eye and the nucleus pulposus (von der Mark, 1980Mark, ,1981. During development transient occurrence of small amounts of type I1 collagen or its mRNA has been observed especially at epithelio-mesenchymal interfaces of both cartilaginous and non-cartilaginous tissues (Thorogood et al, 1986;Hayashi et al, 1988;Fitch et al, 1989;Kosher and Solursh, 1989;Cheah et al, 1991;Wood et al, 1991;Swiderski and Solursh, 1992;Sandberg et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

Developmental expression of a type II collagen/β‐galactosidase fusion gene in transgenic mice

Metsäranta¹,

Garofalo²,

Smith³

et al. 1995

Developmental Dynamics

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The correct temporal and spatial expression of the type I1 collagen gene is believed to be important for normal development and growth of the skeleton and the eye, i.e., tissues where the protein product is predominantly found. To study transcriptional activation of type I1 collagen gene in skeletal and nonskeletal tissues we produced transgenic mice carrying murine proal(I1) collagen@-galactosidase fusion gene constructs. The expression of the fusion gene was found to depend on the presence of intron 1 sequences: constructs with most of intron 1 deleted failed to reveal any p-galactosidase activity confirming the important role of regulatory sequences within intron 1 of the gene. High-level expression of the functional construct was clearly confined to cartilaginous tissues but transient low-level expression was also observed in extraskeletal locations, such as the developing brain and the notochord. The results demonstrate that the regulatory elements in the prooll(I1) collagen@-galactosidase fusion gene construct confer both temporal and spatial specificity indistinguishable from that of the endogenous proal(I1) collagen gene as determined by the presence of the corresponding mRNA by in situ hybridization. Furthermore the p-galactosidase activity correlated well with the progression of chondrogenesis as seen by staining of whole mouse embryos with Alizarin red S and Alcian blue in the hybrid mouse strain used for microinjections. The transgenic mouse line produced should prove useful for studies on various aspects of chondrogenesis. Furthermore, the data shows that the regulatory elements present in the construct are sufficient for targetting the expression of other genes in cartilage.

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Section: Introductionmentioning

confidence: 99%

Developmental expression of a type II collagen/β‐galactosidase fusion gene in transgenic mice

Metsäranta¹,

Garofalo²,

Smith³

et al. 1995

Developmental Dynamics

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“…The limitations of this method include insufficient purification of the antigens (it being difficult to remove all the contaminating non-collagenous proteins), and of the antibodies, since all unspecific antibodies must be removed (voN DER MARK, 1981). Equally important, but often difficult to control or evaluate, is the fact that collagen fibers may be partially masked or may not react completely with the antibody reagents, since it has been shown that each collagen type interacts differently (considering both the quantitative and qualitative aspects) with the ground substance (JUNQUEIRA et al, 1980a;JUNQUEIRA, TOLEDO and MONTES, 1981).…”

Section: Immunohistologymentioning

confidence: 99%

Biology of collagen-proteoglycan interaction.

Junqueira

Montes

1983

Arch. Histol. Jap., Arch. Histol. Jpn

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“…To date, of the 11 genetically different collagen types described [I], 4 have been detected in the human cornea [2,3]. These are type I, which is the predominant cornea1 component, type V and small amounts of types III and IV.…”

Section: Introductionmentioning

confidence: 99%

Type VI collagen is a major component of the human cornea

Zimmermann¹,

Trüeb²,

Winterhalter³

et al. 1986

FEBS Letters

117

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Collagen type VI is shown to be present in the human cornea. This finding is based on comparative peptide mapping relative to type VI collagen isolated from placenta and on immunoblotting using antibodies specific for human type VI collagen. Scanning of polyacrylamide gels indicates that type VI collagen comprises as much as one quarter of the dry weight of the cornea. Indirect immunofluorescence shows this collagen to be distributed throughout the cornea1 stroma. Thus, type VI collagen must be considered a major component of the extracellular matrix of the human cornea.Collagen Extracellular matrix (Cornea, Human)

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Localization of Collagen Types in Tissues

Cited by 153 publications

References 329 publications

Developmental expression of a type II collagen/β‐galactosidase fusion gene in transgenic mice

Developmental expression of a type II collagen/β‐galactosidase fusion gene in transgenic mice

Biology of collagen-proteoglycan interaction.

Type VI collagen is a major component of the human cornea

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