Hydroxyproline stabilizes the triple helix of chick tendon collagen

Jimenez, Sergio A.; Harsch, Margaret; Rosenbloom, Joel

doi:10.1016/0006-291x(73)90960-1

Cited by 191 publications

(72 citation statements)

References 16 publications

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“…AsA is essential for hydroxylation of the proline residues of procollagen molecule in rER (Kivirikko and Myllyla, 1985;Schwarz et al, 1987), and stimulates collagen secretion through its effect on proline hydroxylation (Blanck and Peterkofsky, 1975). The hydroxylation appears to increase the thermal stability of collagen (Berg and Prockop, 1973), and to be required for the formation of the triple helix of procollagen molecules Ramaley et al, 1973;Rosenbloom and Harsch, 1973), which may be necessary for normal secretion of procollagen (Uitto et al, 1972;Jimenez et al, 1973;Ramaley et al, 1973;Rosenbloom and Harsch, 1973). In osteoblasts, as in fibroblasts, type I collagen precursors are processed along the rough endoplasmic reticulum-Golgi-secretory granule pathway (Leblond, 1989).…”

Section: Osteoblasts and Osteoclastsmentioning

confidence: 99%

Morphological influence of ascorbic acid deficiency on endochondral ossification in osteogenic disorder Shionogi rat

Sakamoto

Takano

2002

Anat. Rec.

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The influences of chronic deficiency of L-ascorbic acid (AsA) on the differentiation of osteo-chondrogenic cells and the process of endochondral ossification were examined in the mandibular condyle and the tibial epiphysis and metaphysis by using Osteogenic Disorder Shionogi (ODS) rats that bear an inborn deficiency of L-gulonolactone oxidase. Weanling male rats were kept on an AsA-free diet for up to 4 weeks, until the symptoms of scurvy became evident. The tibiae and condylar processes of scorbutic rats displayed undersized and distorted profiles with thin cortical and scanty cancellous bones. In these scorbutic bones, the osteoblasts showed characteristic expanded round profiles of rough endoplasmic reticulum, and lay on the bone surface where the osteoid layer was missing. Trabeculae formation was deadlocked, although calcification of the cartilage matrix proceeded in both types of bone. Scorbutic condylar cartilage showed severe disorganization of cell zones, such as unusual thickening of the calcification zone, whereas the tibial cartilage showed no particular alterations (except for a moderately decreased population of chondrocytes). In condylar cartilage, hypertrophic chondrocytes were encased in a thickened calcification zone, and groups of nonhypertrophic chondrocytes occasionally formed cell nests surrounded by a metachromatic matrix in the hypertrophic cell zone. These results indicate that during endochondral ossification, chronic AsA deficiency depresses osteoblast function and disturbs the differentiation pathway of chondrocytes. The influence of scurvy on mandibular condyle cartilage is different from that on articular and epiphyseal cartilage of the tibia, suggesting that AsA plays different roles in endochondral ossification in the mandibular condyle and long bones. Anat Rec 268: 93-104, 2002.

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Section: Osteoblasts and Osteoclastsmentioning

confidence: 99%

Morphological influence of ascorbic acid deficiency on endochondral ossification in osteogenic disorder Shionogi rat

Sakamoto

Takano

2002

Anat. Rec.

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“…The presence of Hyp residues in the XЈaa position confers a thermal stability greater than that conferred by Pro residues. Inhibition of post-translational hydroxylation leads to a decrease in the melting temperature of type I collagen by ϳ15°C (12,13), whereas recombinant human collagen homotrimers of type I ␣1-chains that are unhydroxylated have a T m ϳ 11°C lower than that of the hydroxylated form (14). Confirmation of Hyp stabilization of the triple helix and its position-specific nature is seen in model peptides, where T m ϳ 60°C for (Pro-Hyp-Gly) 10 , T m ϳ 30°C for (Pro-Pro-Gly) 10 , and T m Ͻ 0°C for (Hyp-Pro-Gly) 10 (15).…”

mentioning

confidence: 99%

Mechanism of Stabilization of a Bacterial Collagen Triple Helix in the Absence of Hydroxyproline

Mohs¹,

Silva²,

Yoshida³

et al. 2007

Journal of Biological Chemistry

120

158

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The Streptococcus pyogenes cell-surface protein Scl2 contains a globular N-terminal domain and a collagen-like domain, (GlyXaa-Xaa) 79 , which forms a triple helix with a thermal stability close to that seen for mammalian collagens. Hyp is a major contributor to triple-helix stability in animal collagens, but is not present in bacteria, which lack prolyl hydroxylase. To explore the basis of bacterial collagen triple-helix stability in the absence of Hyp, biophysical studies were carried out on recombinant Scl2 protein, the isolated collagen-like domain from Scl2, and a set of peptides modeling the Scl2 highly charged repetitive (GlyXaa-Xaa) n sequences. At pH 7, CD spectroscopy, dynamic light scattering, and differential scanning calorimetry of the Scl2 protein all showed a very sharp thermal transition near 36°C, indicating a highly cooperative unfolding of both the globular and triple-helix domains. The collagen-like domain isolated by trypsin digestion showed a sharp transition at the same temperature, with an enthalpy of 12.5 kJ/mol of tripeptide. At low pH, Scl2 and its isolated collagen-like domain showed substantial destabilization from the neutral pH value, with two thermal transitions at 24 and 27°C. A similar destabilization at low pH was seen for Scl2 charged model peptides, and the degree of destabilization was consistent with the strong pH dependence arising from the GKD tripeptide unit. The Scl2 protein contained twice as much charge as human fibril-forming collagens, and the degree of electrostatic stabilization observed for Scl2 was similar to the contribution Hyp makes to the stability of mammalian collagens. The high enthalpic contribution to the stability of the Scl2 collagenous domain supports the presence of a hydration network in the absence of Hyp.Collagens are considered to be the characteristic structural molecules of the extracellular matrix of multicellular animals. Fibril-forming collagens and basement membrane collagens are ubiquitous in vertebrates and invertebrates, whereas families of more specialized collagens have developed in different organisms such as the 28 distinct collagen types found in vertebrates (1-3) and the ϳ100 cuticle collagen genes in Caenorhabditis elegans (4). In recent years, the range of occurrence of collagen-like sequences with Gly as every 3rd residue and a high Pro content has been extended from metazoans to Ͼ100 proteins in bacteria and bacteriophage (5). An understanding of the structure and stabilization of such bacterial collagens presents new challenges because they lack the Hyp post-translational modification characteristic of animal collagens.A high content of Hyp is a unique stabilizing feature of animal collagens. The characteristic structural motif of all collagens is the triple helix, composed of three left-handed polyproline II-type chains (3 residues/turn) wound around the central axis to form a right-handed superhelix (6 -8). The close packing of each chain near the central axis constrains every 3rd residue of the amino acid sequence to be G...

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“…When these samples were analyzed by SDS-polyacrylamide slab-gel electrophoresis, only 2 major bands were seen in both preparations, their mobilities corresponding to those of the pro-al and pro-a2 chains ( fig.1). Some of preparations were subjected to limited pepsin digestion to remove the propeptides, and in these samples 2 major bands were found with the Three different compounds were used to inhibit triple helix formation of the pro-cw chains, namely &,a-bipyridyl [25,26] , L-azetidine-2-carboxylic acid [27], and dithiothreitol [ 16,281. The cells were incubated with [2-3H]mannose for 2 h and the intracellular protein was analyzed by SDS-polyacrylamide slab-gel electrophoresis.…”

Section: Resultsmentioning

confidence: 99%

Evidence for the transfer of mannose to the extension peptides of procollagen within the cisternae of the rough endoplasmic reticulum

Anttinen¹,

Oikarinen²,

Ryhänen³

et al. 1978

FEBS Letters

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Hydroxyproline stabilizes the triple helix of chick tendon collagen

Cited by 191 publications

References 16 publications

Morphological influence of ascorbic acid deficiency on endochondral ossification in osteogenic disorder Shionogi rat

Morphological influence of ascorbic acid deficiency on endochondral ossification in osteogenic disorder Shionogi rat

Mechanism of Stabilization of a Bacterial Collagen Triple Helix in the Absence of Hydroxyproline

Evidence for the transfer of mannose to the extension peptides of procollagen within the cisternae of the rough endoplasmic reticulum

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