Advertisement

Human Genetics

, Volume 82, Issue 1, pp 49–54 | Cite as

The absence of type II collagen and changes in proteoglycan structure of hyaline cartilage in a case of Langer-Saldino achondrogenesis

  • S. P. Feshchenko
  • I. A. Rebrin
  • V. P. Sokolnik
  • B. M. Sher
  • B. P. Sokolov
  • V. N. Kalinin
  • G. I. Lazjuk
Original Investigations

Summary

Structural analysis of hyaline cartilage extracellular matrix components from the ribs and knee joint of a stillborn female with type II achondrogenesis was carried out. The absence of type II collagen, a decrease in the amount of proteoglycans (PG), and structural changes in PG, namely, increased electrophoretic mobility of PG, lower relative content of chondroitin 4-sulfate (Ch4-S), lower molecular weight and decreased total chondroitin sulfate (ChS) sulfation, were detected. Increased amounts of type I and type III collagens, atypical for hyaline cartilage, were revealed. Among the link proteins (LPs), a large protein with a mol. wt. of 48 kDa was predominant. Molecular and cellular mechanisms of the pathogenesis of achondrogenesis (“chondrogenesis imperfecta”) are discussed. The data obtained suggest that the primary defect in type II achondrogenesis involves ChS or type II collagen synthesis.

Keywords

Collagen Lower Molecular Weight Knee Joint Electrophoretic Mobility Relative Content 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Bitter T, Muir HM (1962) A modified uronic acid carbasole reaction. Anal Biochem 4:330–334Google Scholar
  2. Bradford M (1976) A rapid and sensitive method for the quantities of protein utilising the principle of protein-dye binding. Anal Biochem 72:248–254Google Scholar
  3. Buckwalter JA (1983) Proteoglycan structure in calcifying cartilage. Clin Orthop 172:207–232Google Scholar
  4. Burgeson RE, Hollister DW (1979) Collagen heterogeneity in human cartilage. Identification of several new collagen chains. Biochem Biophys Res Commun 87:1124–113Google Scholar
  5. Chen H, Liu CT, Yang SS (1981) Achondrogenesis: a review with special consideration of achondrogenesis type II (Langer-Saldino). Am J Med Genet 10:379–394Google Scholar
  6. Dorfman HD, Lorenzo J (1980) Case report 122. Skeletal Radiol 5:189–192Google Scholar
  7. Eng CEL, Pauli RM, Strom CM (1985) Nonrandom association of a type II procollagen genotype with achondroplasia. Proc Natl Acad Sci USA 82:5465–5469Google Scholar
  8. Eng CEL, Pauli RM, Strom CM (1986) Retraction. Proc Natl Acad Sci USA 83:5354Google Scholar
  9. Eyre DR, Upton MP, Shapiro FD, Wilkinson RH, Vawter GF (1986) Nonexpression of cartilage type II collagen in a case of Langer-Saldino achondrogenesis. Am J Hum Genet 39:52–67Google Scholar
  10. Feshchenko SP, Krasnopolskaya KD, Shishkin SS (1984) Study of components of proteoglycan aggregates of human hyaline cartilage. Biochemistry USSR 49:1439–1444Google Scholar
  11. Feshchenko SP, Gornyak L, Krasnopolskaya KD, Shishkin SS (1985a) Study of proteoglycan sulfation in human hyaline cartilage from normal individuals and patients with lethal osteochondrodysplasias. Biull Eksp Biol Med 99:502Google Scholar
  12. Feshchenko SP, Krasnopolskaya KD, Shishkin SS, Erber IR (1985b) Heterogeneity of link proteins of proteoglycan aggregates of human hyaline cartilage under normal conditions and in systemic bone dysplasias. Biochemistry USSR 50:586–591Google Scholar
  13. Feshchenko SP, Rebrin IA, Leibiger IB, Sokolnik VP, Chanturia AV (1987) Biochemical markers for different morphofunctional changes of hyaline cartilage in inherited osteochondrodysplasias. 16th Symposium of the European Society of Osteoarthrology “Joint Destruction”, Sochi 1987, p 5/42 (abstr)Google Scholar
  14. Feshchenko SP, Krasnopolskaya KD, Rebrin IA, Rudakov SS (1989) Molecular heterogeneity of proteoglycan aggregates from human hyaline cartilage of normal individuals and patients with systemic bone dysplasias. Vopr Med Khim 35 (in press)Google Scholar
  15. Hascall VC, Kimura JH (1982) Proteoglycans: isolation and characterization. Methods Enzymol 82:769–800Google Scholar
  16. Hollister DW, Burgeson RE, Rimoni DL (1975) Abnormal cartilage collagen in thanatophoric dwarfism. Am J Hum Genet 27:783Google Scholar
  17. Horton WA, Machado MA, Chou JW, Campbell D (1987) Achondrogenesis type II, abnormalities of extracellular matrix. Pediatr Res 22:324–329Google Scholar
  18. Hsu D-S, Hoffman P, Mashburn TA (1974) Fractionation of chondroitin sulfate and determination of molecular weight by PAAG-electrophoresis. Biochem Biophys Acta 338:254–264Google Scholar
  19. Kocher RA (1983) The chondroblast and the chondrocyte. In: Hall BK (ed) Cartilage. Academic Press, New York London, pp 59–85Google Scholar
  20. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685Google Scholar
  21. Lazjuk GI, Shved IA, Cherstvoy ED, Feshchenko SP (1987) Campomelic syndrome: concepts of the bowing and shortening in the lower limbs. Teratology 35:1–8Google Scholar
  22. Leibiger IB, Feshchenko SP, Kozlov EA, Krasnopolskaya KD, Burakov VV, Delvig AA, Shishkin SS, Rudakov SS (1986) Study of collagen proteins of human hyaline cartilage of normal individuals and patients with systemic bone dysplasias. Biokhimia 51: 505–515Google Scholar
  23. McDevitt CA, Muir H (1971) Gel electrophoresis of proteoglycans and glycosaminoglycans on large pore composite polyacrylamide-agarose gels. Anal Biochem 44:612–622Google Scholar
  24. McKeown-Longo PI, Velleman SG, Goetinck PF (1983) The independent synthesis and secretion of cartilage proteoglycan and link protein by embryonic chicken chondrocytes. J Biol Chem 258: 10779–10785Google Scholar
  25. Mort JS, Poole AR, Roughley PI (1983) Age-related changes in the structure of proteoglycan link proteins present in normal human articular cartilage. Biochem J 214:269–272Google Scholar
  26. Ogilwie D, Wordsworth P, Thompson E, Sykes B (1986) Evidence against the structural gene encoding type II collagen (COL2A1) as the mutant locus in achondroplasia. J Med Genet 23:19–22Google Scholar
  27. Orkin RW, Pratt RM, Martin GR (1976) Undersulfated chondroitin sulfate in the cartilage matrix of brachymorphic mice. Dev Biol 50:82–85Google Scholar
  28. Sage H, Bornstein P (1982) Preparation and characterization of procollagens and procollagen-collagen intermediates. Methods Enzymol 82:96–127Google Scholar
  29. Saito H, Yamagata T, Suzuki S (1968) Enzymatic methods for the determination of small quantities of isomeric chondroitin sulfates. J Biol Chem 243:1536–1539Google Scholar
  30. Seegmiller RE, Chandrasekhar S, Brown K (1985) Molecular differences in cartilage among chondrodystrophic mice. Teratology 31: 43AGoogle Scholar
  31. Stanescu V, Maroteaux P, Sobezak E (1973) Gel electrophoresis of the proteoglycans of the growth and of the articular cartilage from various species. Biomedicine 19:460–463Google Scholar
  32. Stanescu V, Stanescu R, Maroteaux P (1984) Pathogenic mechanisms in osteochondrodysplasias. J Bone Joint Surg 66:817–836Google Scholar
  33. Sugahara K, Schwartz NB (1982a) Defect in 3′-phosphoadenosine 5′-phosphosulfate synthesis in brachymorphic mice. I. Characterization of the defect. Arch Biochem Biophys 214:589–601Google Scholar
  34. Sugahara K, Schwartz NB (1982b) Defect in 3′-phosphoadenosine 5′-phosphosulfate synthesis in brachymorphic mice. II. Tissue distribution of the defect. Arch Biochem Biophys 214:602–609Google Scholar
  35. Vasan NS, Lash JW (1977) Heterogeneity of proteoglycans in developing chick limb cartilage. Biochem J 164:179–183Google Scholar
  36. Wasserman L, Ber A, Allalouf D (1977) Use of thin-layer chromatography in the separation of disaccharides resulting from digestion of chondroitin sulfates with chondroitinases. J Chromatogr 136:341–347Google Scholar
  37. Wessler E (1971) Electrophoresis of acidic glycosaminoglycans in hydrochloric acid. A micro method for sulfate determination. Anal Biochem 41:67–70Google Scholar
  38. Whitley CB, Gorlin RJ (1983) Achondrogenesis: new nosology with evidence of genetic heterogeneity. Radiology 148:693–698Google Scholar
  39. Wieslander J, Heinegard D (1979) Immunochemical analysis of cartilage proteoglycans. Antigenic determinants of substructures. Biochem J 179:35–45Google Scholar

Copyright information

© Springer-Verlag 1989

Authors and Affiliations

  • S. P. Feshchenko
    • 1
  • I. A. Rebrin
    • 2
  • V. P. Sokolnik
    • 1
  • B. M. Sher
    • 2
  • B. P. Sokolov
    • 2
  • V. N. Kalinin
    • 2
  • G. I. Lazjuk
    • 1
  1. 1.Byelorussian Institute for Hereditary DiseasesMinskUSSR
  2. 2.Institute of Medical Genetics of the USSR Academy of Medical SciencesMoscowUSSR

Personalised recommendations