Minor collagens of chicken hyaline cartilage

Reese, Charles A.; Mayne, Richard

doi:10.1021/bi00522a014

Cited by 210 publications

(134 citation statements)

References 14 publications

Supporting

Mentioning

123

Contrasting

Unclassified

Order By: Relevance

“…With reduction the X3 chain gave rise to at least 3 major components ( fig.le,i) called X3R1, X3R 2 and X3R 3 of 40 000, 37 000 and 31 000 Mr. The electrophoretic behaviour and the amino acid composition (table 1) of the X3 chain are similar to those reported for the collagenous components M [2,3], CPSI [5,6], I-IMW [7,8] and M1 [9]. However, with reduction M and CPSI both give rise to only one chain of 33 000 Mr.…”

Section: Immunofluorescence Staining Proceduressupporting

confidence: 70%

“…With reduction the X4 chain gave rise to one component of 13 000 Mr. The amino acid composition of the X4 chain (table 1) is different from that reported for CF2 [3] and is rather similar to that of CPS2 [6], LMW [7] and M2 [9]. In particular the X4 chain contains much less hydroxyproline and proline (110 and 116 residues/1000) than CF2 (198.5 and 146.8 residues/1000).…”

Section: Immunofluorescence Staining Proceduresmentioning

confidence: 76%

“…However, with reduction M and CPSI both give rise to only one chain of 33 000 Mr. The X3 chain can rather be compared to HMW [7,8] or MI [9] giving rise with reduction, respectively, to 3 and 4 components but with different Mr-values.…”

Section: Immunofluorescence Staining Proceduresmentioning

confidence: 99%

“…The X4 chain ( fig.If,j) is a disulfide-bonded collagenous fragment, of 31 500 Mr by SDS-polyacrylamide gel electrophoresis and 33 000 Mr by molecular sieve chromatography, which can be compared to CF2 [3], CPS2 [6], LMW [7,8] and M2 [9]. With reduction the X4 chain gave rise to one component of 13 000 Mr.…”

Section: Immunofluorescence Staining Proceduresmentioning

confidence: 99%

“…The la, 2a and 3a chains were extracted from human and bovine hyaline cartilage [1]. Other minor collagenous components were extracted from neonatal pig and human cartilage noted M, CFI, CF2 [2][3][4], from bovine nasal cartilage and human intervertebral disc noted CPS1, CPS2 [5,6] and from chicken sternal cartilage noted HMW, LMW [7,8] and M 1, M 2 [9].…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Biochemical properties and immunolocalization of minor collagens in foetal calf cartilage

Herbage²,

et al. 1982

View full text Add to dashboard Cite

Section: Immunofluorescence Staining Proceduressupporting

confidence: 70%

Section: Immunofluorescence Staining Proceduresmentioning

confidence: 76%

Section: Immunofluorescence Staining Proceduresmentioning

confidence: 99%

Section: Immunofluorescence Staining Proceduresmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Biochemical properties and immunolocalization of minor collagens in foetal calf cartilage

Herbage²,

et al. 1982

View full text Add to dashboard Cite

Notochord of chick embryos secretes short‐form type IX collagen prior to the onset of vertebral chondrogenesis

Hayashi

Iyama

et al. 1992

Developmental Dynamics

Self Cite

View full text Add to dashboard Cite

The notochord of embryonic chicks produces type IX collagen, as well as type I1 collagen, prior to the onset of vertebral chondrogenesis. To address the question of whether the notochord secretes the "long-form" type IX collagen found in cartilage or the "short-form" type IX found in the cornea and vitreous humor, we examined immunoreactivity of the notochordal type IX collagen using two different monoclonal antibodies. The antibody 2C2 recog nizes an epitope close to the carboxyl-terminus of the HMW fragment, which is present in both the long-and short-form type IX collagens, whereas another antibody 4D6 recognizes an epitope in the NC4 domain of the long-form type IX collagen, which is absent in the short-form type IX collagen. Therefore, the long-form is recognized by its reaction with both 2C2 and 4D6, while the short-form by its reaction with only 2C2 and no reaction with 4D6. Immunostaining of vertebral sections with 2C2 shows an identical distribution of staining with that for type I1 collagen, although the staining with 2C2 is less intense. The ZCZ-reactive type IX collagen is found within the notochord at stage 14 and in the notochordal sheath at stage 20. Deposition of this collagen in the perinotochordal matrix increases with time and reaches a level comparable with that for type I1 at stage 31. In contrast, the 4D6-reactive type IX collagen is not found within the notochord nor in the notochordal sheath. The collagen becomes detectable, however, in the perinotochordal matrix at stages 27 to 28 and is markedly increased at stage 29, reaching the levels for the 2C2-reactive type IX at stage 31. A highly sensitive immuno-dot blot assay has confirmed that the notochord from chick embryos at stages 19 to 20 produces type IX collagen that reacts with 2C2 but does not react with 4D6. The present study indicates (1) that the short-form type IX collagen is secreted from the notochord and also from the sclerotome cells, and (2)

show abstract

Cartilage collagens. What Is Their Function, and Are They Involved in Articular Disease?

Mayne

1989

Arthritis & Rheumatism

Self Cite

183

View full text Add to dashboard Cite

During the last decade, remarkable progress has been made in the study of different collagen types. At present, 13 collagens have been identified, and several more candidate proteins wait in the wings. For physicians who study and treat connective tissue diseases, this list has become bewildering, especially since the criteria for designating a new collagen type have become somewhat lax.At the very least, a new collagen should possess a typical collagen triple helix, and should be clearly shown to have a structural function in the extracellular matrix. For some of the new collagens, as discussed later for type X collagen, a structural function has still not been demonstrated. The designation "collagen" does not imply the formation of typical crossbanded fibrils with the quarter-staggered arrangement of molecules that are easily recognized by electron microscopy. At present, only 5 of the various collagens (types I, 11, 111, V, and XI) are known to be involved in this type of fibril formation, although other collagens (e.g., type IX) are associated with the surface of fibrils. From The University of Alabama at Birmingham MedicalSupported by NIH grants AR-30481 and AR-37984. Richard Mayne, DPhil:

show abstract

Minor collagens of chicken hyaline cartilage

Cited by 210 publications

References 14 publications

Biochemical properties and immunolocalization of minor collagens in foetal calf cartilage

Biochemical properties and immunolocalization of minor collagens in foetal calf cartilage

Notochord of chick embryos secretes short‐form type IX collagen prior to the onset of vertebral chondrogenesis

Cartilage collagens. What Is Their Function, and Are They Involved in Articular Disease?

Contact Info

Product

Resources

About