The Biosynthesis of Collagen and Its Disorders

Prockop, Darwin J.; Kivirikko, Kari I.; Tuderman, Leena; Guzman, Norberto A.

doi:10.1056/nejm197907123010204

Cited by 572 publications

(245 citation statements)

References 80 publications

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“…As these cytokines act synergistically in many biological assays, it is important to assess their interactions for elucidating the pathogenesis of RA. The matrix-degrading enzymes are considered to play key roles in joint destruction because of their participation in the cell migration and rapid local tissue remodelling observed during inflammation (22,23). Indeed, MMPs including MMP-1 provide essentially all the proteolytic activities necessary to hydrolyze collagens of the synovium and cartilage matrix (3,24,25).…”

Section: Discussionmentioning

confidence: 99%

Interleukin‐4 stimulates rheumatoid synovial fibroblasts to express matrix metalloproteinase‐1 (tissue collagenase) and histamine H1 receptor mRNA

et al. 1996

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SUMMARY : In the present study, we investigated the effect of interleukin-4 (IL-4) on metalloproteinase 1 (MMP-1/tissue collagenase) production in human rheumatoid synovial fibroblasts. Northern blot analysis revealed that addition of IL-4 with or without histamine stimulated the cells to increase the amount of proMMP-1 mRNA, and the IL-4 with histamine addition resulted in a 3.3-fold increase compared with histamine only. Furthermore, IL-4 itself stimulated the expression of histamine H1 receptor mRNA. These results suggest that 11+-4 may play an important role in joint destruction in RA.

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Section: Discussionmentioning

confidence: 99%

Interleukin‐4 stimulates rheumatoid synovial fibroblasts to express matrix metalloproteinase‐1 (tissue collagenase) and histamine H1 receptor mRNA

et al. 1996

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“…We examined incorporation of [3H]mannose to explore observations (14) indicating that there may be a structural alteration in the type I procollagen synthesized by fibroblasts from a patient who had OI. The presence of mannose in the COOH-terminal propeptide of type I procollagen (9,11,18,19) indicates that the carbohydrate substituent is of the Asn-GIcNAc-type (for review, see ref. 20).…”

Section: Discussionmentioning

confidence: 99%

“…He (14). The cultures at confluency were incubated for 24 hr with [2-3H]mannose (8)(9)(10)(11)(12)(13)(14)(15) ,gCi/ml; 1 Ci = 3.7 X 101 becquerels) (Amersham) and either '4C-labeled mixture of amino acids (1.5-2.0 liCi/ml) (New England Nuclear) or [14C]proline (2 ,uCi/ml) (New England Nuclear) (14). The labeled procollagen was isolated by (NH4)2SO4 precipitation and chromatography on DEAE-cellulose (Whatman DE-52) in 2 M urea, using minor modifications of the procedure of Smith et al (15).…”

mentioning

confidence: 99%

A defect in the structure of type I procollagen in a patient who had osteogenesis imperfecta: excess mannose in the COOH-terminal propeptide.

Peltonen¹,

Palotie²,

Prockop³

1980

Proc. Natl. Acad. Sci. U.S.A.

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Fibroblasts from normal human subjects and from a patient who had osteogenesis imperfecta were incubated with [3H]mannose, and types I and III procolla ens were isolated from the culture medium. The type I procowuaen from the patient's fibroblasts contained [2][3] These results appear to provide evidence for an alteration in the structure of procollagen in osteogenesis imperfecta. Osteogenesis imperfecta (OI) is a heterogeneous group of genetic disorders that are characterized by increased fragility of bone (1, 2). In the most severe forms, death occurs in utero. In more moderate forms, there are severe bone deformities because of repeated multiple fractures. The increased fragility of bone is frequently accompanied by blue sclerae, opalescent teeth, hearing impairment, and thin and translucent skin. A number of observations have been made that suggest that many forms of OI involve changes in the structure or synthesis of collagen. These changes include a decrease in the amount of type I collagen relative to that of type III collagen in skin extracts (3); a decrease in the synthesis of type I procollagen relative to that of type III procollagen by cultured skin fibroblasts (4); a decrease in the total amount of collagen synthesized by cultured skin fibroblasts (5); the presence of type III collagen in bone, a tissue that normally does not contain this protein (6); the presence in skin extracts of collagen that has increased amounts of hydroxylysine and glycosylated hydroxylysine (7); and a relative increase in the amount of immature crosslinks in collagen extracted from skin (8). It has been difficult, however, to determine which of these observations reflect primary genetic defects and which are secondary events. For example, a variety of experimental conditions can influence the posttranslational processing of procollagen and thereby alter the amounts of hydroxylysine and glycosylated hydroxylysine and the kinds of crosslinks found in collagen without any change in its genetically determined primary structure (for reviews, see refs. 9-11). Also, it is not apparent whether the relative amounts of type I and type III procollagens synthesized by fibroblasts are a genetically determined property of such cells or whether this varies with experimental conditions, such as the density of the cell cultures (12, 13).The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "adve-rtisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact. 6179We recently examined the type I and type III procollagens synthesized by the fibroblasts from a patient who had OI and found that the type I procollagen formed insoluble aggregates more readily than normal type I procollagen (14). We here report further studies of the same fibroblasts; these studies appear to provide evidence for an alteration in the structure of procollagen in some OI patients.MATERIALS AND METHODS Cultured Fibroblasts. The studies described here were carried out by u...

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“…Collagen represents a major class of proteins in mammals and plays a fundamental role in the structure and function of most connective tissues (1,2). Collagen is synthesized from procollagen, a precursor composed ofthree pro-a chains.…”

mentioning

confidence: 99%

“…Collagen is synthesized from procollagen, a precursor composed ofthree pro-a chains. At least five genetically and biochemically distinct types of collagen are found in different tissues, and they have a characteristic developmental distribution (1)(2)(3). Type I collagen, [al(I)]2a2, is present in bones, skin, tendons, and lungs, and it is believed to be directly or indirectly involved in inherited diseases of the connective tissue in man such as some forms of osteogenesis imperfecta (1).…”

mentioning

confidence: 99%

Cloning a cDNA for the pro-alpha 2 chain of human type I collagen.

Myers¹,

Chu²,

Faro³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

173

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Poly(A)-RNA enriched for type I procollagen sequences was isolated from normal human fibroblasts and used as template to synthesize double-stranded cDNA with avian myeloblastosis virus (AMV) reverse transcriptase. After the ends had been blunted with nuclease SI and dGMP tails had been added with terminal deoxynucleotidyltransferase, the double-stranded cDNA was annealed with pBR322 DNA that had previously been cleaved with EcoRI, blunted with AMV reverse transcriptase, and dCMP-tailed with terminal deoxynucleotidyltransferase. The chimeric molecule was used to transform Escherichia coli strain HB1O1. Ninety-five recombinant clones were obtained and screened by dot hybridization analysis using 32P-labeled cDNA synthesized from the original poly(A)-RNA collagen-enriched population. Three positive clones were isolated and further characterized by blot hybridization techniques and by EcoRil digestion. One clone with an insert of 2.2 kilobases was shown to contain sequences encoding for the pro-a2 chain of human type I procollagen. DNA sequence analysis of a 172-nucleotide fragment demonstrated that the cloned cDNA extends from amino acid position 450 of the a2 chain to the middle of the COOH-terminal propeptide.Collagen represents a major class of proteins in mammals and plays a fundamental role in the structure and function of most connective tissues (1, 2). Collagen is synthesized from procollagen, a precursor composed ofthree pro-a chains. At least five genetically and biochemically distinct types of collagen are found in different tissues, and they have a characteristic developmental distribution (1-3). Type I collagen, [al(I)]2a2, is present in bones, skin, tendons, and lungs, and it is believed to be directly or indirectly involved in inherited diseases of the connective tissue in man such as some forms of osteogenesis imperfecta (1). Although a great deal of information is available about posttranslational events leading to the maturation of the human procollagen chains, very little is known about the structure, the genetics, and the mode of expression of this family of genes in man.In the past few years recombinant DNA techniques have proved to be a powerful tool for enhancing our understanding ofthe structure ofeukaryotic genes and their altered phenotypic expression, as exemplified by the human globin genes (4). Recently cloned cDNAs for type I procollagen from chicken have been prepared (5-7), and the entire chicken pro-a2 gene (8)(9)(10) MATERIALS AND METHODS Materials. Reverse transcriptase (RNA-dependent DNA polymerase) from avian myeloblastosis virus (AMV) was purified (13) from plasma kindly supplied by Joseph Beard (Life Sciences, Gulfport, FL). Nuclease S1 was purchased from Miles. Calf thymus terminal deoxynucleotidyltransferase was a generous gift from Sidney Pestka (Roche Institute of Molecular Biology). Rabbit reticulocyte lysate was purchased from Amersham. Restriction enzymes were purchased from New England BioLabs and were used according to the supplier's recommendations. Nitrocel...

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The Biosynthesis of Collagen and Its Disorders

Cited by 572 publications

References 80 publications

Interleukin‐4 stimulates rheumatoid synovial fibroblasts to express matrix metalloproteinase‐1 (tissue collagenase) and histamine H1 receptor mRNA

Interleukin‐4 stimulates rheumatoid synovial fibroblasts to express matrix metalloproteinase‐1 (tissue collagenase) and histamine H1 receptor mRNA

A defect in the structure of type I procollagen in a patient who had osteogenesis imperfecta: excess mannose in the COOH-terminal propeptide.

Cloning a cDNA for the pro-alpha 2 chain of human type I collagen.

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