Biosynthesis of Cartilage Collagen

Miller, Edward J.; Woodall, Diane L.; Vail, Margaret S.

doi:10.1016/s0021-9258(19)44242-7

Cited by 61 publications

(15 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Relatively distinct peaks were obtained containing CB8 plus CB9, CB10, and CB11 plus CB12. The separation achieved was similar to that reported by Miller et al (1973), except that the separation of CB7 from CB4 and CB6 was not as complete. Also, CB9 appeared in the same peak as CB8 and did not cochromatograph with CB10 (see below).…”

Section: Resultssupporting

confidence: 84%

“…Separation of the CNBr peptides on CM-cellulose permitted a more complete fractionation of the peptides (Figure 3). The identity of each of these peaks was established by comparison with results published by Miller et al (1973) and Byers et al (1974) and by examination of the eluted peaks by electrophoresis (see below). The first peak contained CB4, CB6, and cpm/fraction (-); absorbance at 230 nm (---).…”

Section: Resultsmentioning

confidence: 99%

“…CB7, small peptides from the two ends of the a chains. Since CB4 does not contain proline (Miller et al, 1973), it was ignored in estimates for degree of hydroxylation of CB6 (Table I). CB7 eluted in the trailing edge of the first peak.…”

Section: Resultsmentioning

confidence: 99%

“…Chromatography of CNBr peptides was carried out on CMcellulose (CM-52; Whatman) according to the procedure of Miller et al (1973). In initial experiments, a column 0.9 cm in diameter and 8 cm high was employed.…”

mentioning

confidence: 99%

See 3 more Smart Citations

Hydroxylation of prolyl residues in type II procollagen in vitro and in cellulo. Lack of preferential hydroxylation of specific regions of the protein

Kimura¹,

Prockop²

1982

Biochemistry

View full text Add to dashboard Cite

[14C]Proline-labeled protocollagen, the unhydroxylated form of procollagen, was isolated from cartilage cells incubated with alpha, alpha'-dipyridyl. For examination of the initial steps in the hydroxylation of the protein, it was incubated in vitro with prolyl hydroxylase so that an average of 1.3-2.7 prolyl residues per chain was hydroxylated. The partially hydroxylated alpha chain were cleaved with cyanogen bromide, and the fragments were separated by polyacrylamide gel electrophoresis or column chromatography. The cyanogen bromide fragments were hydroxylated to the same degree. The results indicated, therefore, that in the initial hydroxylation of alpha chains in vitro, there was no preferential hydroxylation of any specific regions of the protein. In a second series of experiments, cartilage cells were incubated with [14C]proline and alpha, alpha'-dipyridyl so that prolyl hydroxylase in the cells was extensively, but not completely, inhibited. Partially hydroxylated alpha chains were isolated, and cyanogen bromide fragments of the alpha chains from the cells were assayed for hydroxy[14C]proline. The alpha chains contained an average of two residues of hydroxyproline per chain, and the cyanogen bromide fragments were hydroxylated to about the same degree. The results indicated, therefore, that when prolyl hydroxylase activity in cells is low relative to the rate at which pro alpha chains are synthesized, hydroxylation of prolyl residues occurs as it does in vitro, and there is no preferential hydroxylation of a specific region of the protein.

show abstract

Section: Resultssupporting

confidence: 84%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Hydroxylation of prolyl residues in type II procollagen in vitro and in cellulo. Lack of preferential hydroxylation of specific regions of the protein

Kimura¹,

Prockop²

1982

Biochemistry

View full text Add to dashboard Cite

show abstract

“…Amino Acid Analysis. Analyses were performed either on a Beckman 120C amino acid analyzer modified for singlecolumn analysis (Miller and Piez, 1966) or on a Beckman 119 automatic amino acid analyzer (Miller, 1972). Prior to analysis, samples were hydrolyzed at 108 °C for 24 h with constant-boiling 6 N HC1.…”

Section: Methodsmentioning

confidence: 99%

The covalent structure of cartilage collagen. Amino acid sequence of the amino-terminal helical portion of the α1(II) chain

Butler¹,

Miller²,

Finch³

1976

Biochemistry

Self Cite

View full text Add to dashboard Cite

The amino acid sequence of 162 residues from the NH2-terminal region of bovine alpha 1 (II) is reported. Automated sequence analysis of chains from pepsin-treated type II collagen indicated the sequence and order of two CNBr peptides, alpha 1 (II)-CB2 and alpha 1 (II)-CB3, at the beginning of the repetitive triplet sequence of alpha 1 (II). The sequences of alpha 1 (II)-CB6, alpha 1 (II),-CB12, and 39 residues of alpha 1 (II)-CB11 were determined largely by automated Edman degradation. Comparative sequence data are reported which indicate that the level of homology between alpha 1 (I) and alpha 1 (II) chains in the NH2-terminal region is about 80%. A similar level of homology was reported for the central portions of these chains (Butler, W.T., Miller, E.J., Finch, J.E., Jr., and Inagami, T. (1974), Biochem. Biophys. Res. Commun. 57 190). The degree of intraspecies variability between chain types is thus greater than the interspecies variability for a single chain type. Within the sequence reported here, the alpha 1 (II) chain contains glucosylgalactosylhydroxylysine at three positions. The corresponding sequence of alpha 1 (I) contains only one clycosylated hydroxylysine with the other two positions occupied by lysyl residues.

show abstract

Review of articular cartilage collagen research

Lane

Weiss

1975

Arthritis & Rheumatism

148

View full text Add to dashboard Cite

Recent advances in collagen methodology have now permitted a detailed investigation of this major structural protein of articular cartilage. Collagen structure, metabolism, antl morphology have been extensively studied in "soft" connective tissues (1,Z). Tlie difficulty of collagen extraction from cartilage and bone has prevented its characterization in "hard" connective tissues until recently (3). Since September 3, 1974; accepted May 5, 1975. in the rapidly progressing field of articular cartilage collagen research.Articular cartilage is a highly specialized connective tissue consisting of relatively small numbers of cells distributed throughout abundant extracellular matrix. T h e biophysical properties of articular cartilage that allow joints to serve as bearings in locomotion are in part related to tlie unique composition of tlie extracellular matrix. Collagen constitutes approximately 10% of the wet and 50y0 of the dry weight of cartilage (5). Noncollagenous material constitutes approximately the other 507, of the dry mass of articular cartilage matrix, of which the bulk is in the form of heterogenous proteoglycan complexes (6). Rather than being a single compound, the proteoglycans comprise multiple compounds that differ from each other in their sulfate content, amino acicl sequence of the peptide core, glycosaminoglycan composition, and side chain length.T h e biomaterial properties of the cartilage are a consequence of the interaction of the collagen and proteoglycans in the extracellular matrix. T h e chain extensions of the proteoglycans antl the electrostatic charges provide the molecular basis for consequent mechanical matrix stiffness (7). Tlie inability of the sulfate moieties to diffuse away from the glycosaminoglycan side chains influences the partition of water and diffusible electrolytes (8,9). T h e interaction of the proteoglycan with collagen is necessary for them to behave like gels (7). Whether the interaction is chem-

show abstract

Biosynthesis of Cartilage Collagen

Cited by 61 publications

References 24 publications

Hydroxylation of prolyl residues in type II procollagen in vitro and in cellulo. Lack of preferential hydroxylation of specific regions of the protein

Hydroxylation of prolyl residues in type II procollagen in vitro and in cellulo. Lack of preferential hydroxylation of specific regions of the protein

The covalent structure of cartilage collagen. Amino acid sequence of the amino-terminal helical portion of the α1(II) chain

Review of articular cartilage collagen research

Contact Info

Product

Resources

About