Structural Diversity and Domain Composition of a Unique Collagenous Fragment (intima Collagen) Obtained from Human Placenta

Overview

Journal Biochem J

Specialty Biochemistry

Date 1983 May 1

PMID 6870834

Citations 30

Authors

E Odermatt

J Risteli

V van Delden

R Timpl

Affiliations

Soon will be listed here.

Abstract

Intima collagen was obtained from pepsin digests of human placenta in two forms, which differ to some extent in the size of their constituent polypeptide chains (Mr 50 000-70 000). These chains are connected by disulphide bonds to large aggregates. The aggregates are arranged in a triple-helical conformation with a remarkably high thermal stability (Tm 41-62 degrees C) and are resistant to further proteolytic digestion. Reduction of as little as 5% of the disulphide bonds produces mainly monomeric triple helices (Mr about 160 000) with Tm 32 degrees C. Partially reduced material can be separated into triple-helical and non-collagenous domains by proteolysis. Pepsin releases a collagenous component with chains of Mr 38 000. Bacterial collagenase liberates two non-collagenous segments (Mr 15 000-30 000) rich in cystine. Treatment with collagenase before reduction separates intima collagen into a large fragment composed of collagenous (Tm 41 degrees C) and non-collagenous structures and a single non-collagenous segment. The data support the electron-microscopical model of intima collagen [Furthmayr, Wiedemann, Timpl, Odermatt & Engel (1983) Biochem. J. 211, 303-311], indicating that the basic unit of the fragment consists of a continuous triple helix joining two globular domains.

Citing Articles

Structure of a collagen VI α3 chain VWA domain array: adaptability and functional implications of myopathy causing mutations.

Solomon-Degefa H, Gebauer J, Jeffries C, Freiburg C, Meckelburg P, Bird L J Biol Chem. 2020; 295(36):12755-12771.

PMID: 32719005 PMC: 7476709. DOI: 10.1074/jbc.RA120.014865.

Three-dimensional architecture of collagen type VI in the human trabecular meshwork.

Koudouna E, Young R, Ueno M, Kinoshita S, Quantock A, Knupp C Mol Vis. 2014; 20:638-48.

PMID: 24868138 PMC: 4021673.

Tenomodulin is necessary for tenocyte proliferation and tendon maturation.

Docheva D, Hunziker E, Fassler R, Brandau O Mol Cell Biol. 2005; 25(2):699-705.

PMID: 15632070 PMC: 543433. DOI: 10.1128/MCB.25.2.699-705.2005.

Mutations in COL6A3 cause severe and mild phenotypes of Ullrich congenital muscular dystrophy.

Demir E, Sabatelli P, Allamand V, Ferreiro A, Moghadaszadeh B, Makrelouf M Am J Hum Genet. 2002; 70(6):1446-58.

PMID: 11992252 PMC: 419991. DOI: 10.1086/340608.

Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds beta1 integrins, collagens and fibronectin.

Sasaki T, Brakebusch C, Engel J, Timpl R EMBO J. 1998; 17(6):1606-13.

PMID: 9501082 PMC: 1170508. DOI: 10.1093/emboj/17.6.1606.

References

Furthmayr H, Timpl R . Characterization of collagen peptides by sodium dodecylsulfate-polyacrylamide electrophoresis. Anal Biochem. 1971; 41(2):510-6. DOI: 10.1016/0003-2697(71)90173-4. View

Brown 3rd F, Di Corato A, Lorenzi G, BLOUT E . Synthesis and structural studies of two collagen analogues: poly (L-prolyl-L-seryl-glycyl) and poly (L-prolyl-L-alanyl-glycyl). J Mol Biol. 1972; 63(1):85-99. DOI: 10.1016/0022-2836(72)90523-2. View

Gollwitzer R, Becker U, Timpl R . Isolation and chemical characterization of reduced and aminoethylated polypeptide chains of bovine fibrinogen. FEBS Lett. 1974; 47(1):177-80. DOI: 10.1016/0014-5793(74)80453-9. View

Chung E, Rhodes K, Miller E . Isolation of three collagenous components of probable basement membrane origin from several tissues. Biochem Biophys Res Commun. 1976; 71(4):1167-74. DOI: 10.1016/0006-291x(76)90776-2. View

Nowack H, Olsen B, Timpl R . Characterization of the amino-terminal segment in type III procollagen. Eur J Biochem. 1976; 70(1):205-16. DOI: 10.1111/j.1432-1033.1976.tb10971.x. View

Timpl R, Bruckner P, FIETZEK P . Characterization of pepsin fragments of basement membrane collagen obtained from a mouse tumor. Eur J Biochem. 1979; 95(2):255-63. DOI: 10.1111/j.1432-1033.1979.tb12961.x. View

Furuto D, Miller E . Isolation of a unique collagenous fraction from limited pepsin digests of human placental tissue. Characterization of one of the constituent polypeptide chains. J Biol Chem. 1980; 255(1):290-5. View

Bornstein P, SAGE H . Structurally distinct collagen types. Annu Rev Biochem. 1980; 49:957-1003. DOI: 10.1146/annurev.bi.49.070180.004521. View

Risteli J, Bachinger H, Engel J, Furthmayr H, Timpl R . 7-S collagen: characterization of an unusual basement membrane structure. Eur J Biochem. 1980; 108(1):239-50. DOI: 10.1111/j.1432-1033.1980.tb04717.x. View

10.

Laurain G, Delvincourt T, Szymanowicz A . Isolation of a macromolecular collagenous fraction and AB2 collagen from calf skin. FEBS Lett. 1980; 120(1):44-8. DOI: 10.1016/0014-5793(80)81042-8. View

11.

Jander R, Rauterberg J, Voss B, von Bassewitz D . A cysteine-rich collagenous protein from bovine placenta. Isolation of its constituent polypeptide chains and some properties of the non-denatured protein. Eur J Biochem. 1981; 114(1):17-25. View

12.

Furuto D, Miller E . Characterization of a unique collagenous fraction from limited pepsin digests of human placental tissue: molecular organization of the native aggregate. Biochemistry. 1981; 20(6):1635-40. DOI: 10.1021/bi00509a035. View

13.

Gibson M, Cleary E . A collagen-like glycoprotein from elastin-rich tissues. Biochem Biophys Res Commun. 1982; 105(4):1288-95. DOI: 10.1016/0006-291x(82)90926-3. View

14.

Furthmayr H, Wiedemann H, Timpl R, Odermatt E, Engel J . Electron-microscopical approach to a structural model of intima collagen. Biochem J. 1983; 211(2):303-11. PMC: 1154360. DOI: 10.1042/bj2110303. View

15.

Rich A, Crick F . The molecular structure of collagen. J Mol Biol. 1961; 3:483-506. DOI: 10.1016/s0022-2836(61)80016-8. View