Skip to main content
NCBI home page
Journal of Anatomy logoLink to Journal of Anatomy
. 1996 Aug;189(Pt 1):109–115.

Distribution of chondroitin sulphate proteoglycans and peanut agglutinin-binding molecules during bovine fetal palatine ridge formation.

M Takanosu 1, H Amasaki 1, S Matsumoto 1, K Kimata 1
PMCID: PMC1167832  PMID: 8771401

Abstract

The expression of proteoglycans detected by the monoclonal antibodies MO-225, 3B3 and 2B6 and of peanut agglutinin-binding molecules was examined histochemically during the development of bovine palatine ridge (PR) rudiments in fetuses with crown-rump lengths of 4-60 cm. The bovine PR rudiment has 2 characteristic developmental stages: the 1st is the positioning of the epithelial placode (EP) to the predetermined site of PR rudiment formation and the 2nd is the reorientation of the apical edge of PR rudiments to form wave-like patterns from mouth to pharynx. During the 1st stage, chondroitin 6-sulphate (C6S) was expressed strongly at the epithelial basement membrane just beneath the EP. During the 2nd stage, both C6S and disaccharide unit of Glc2sulphate-GalNAc6sulphate (GlcAsSO4-GalNAc6SO4) were distributed at the basement membrane and the mesenchyme just beneath the steeper wall of the PR rudiment. Peanut agglutinin-binding molecules were also detected in the mesenchyme, their distribution being similar to that for C6S and GlcA2SO4-GalNAc6SO4, and additionally in the epithelial cells after formation of the wave-like PR. The distribution of dermatan sulphate was not directly related to the developmental changes of PR rudiments, but it was detected in the lower mesenchymal layer which supported the protruding site of the PR rudiment after the 2nd stage. The results suggest that 2 different types of proteoglycan may be involved in the critical periods during the morphogenesis of the bovine PR rudiments.

Full text

PDF
109

Images in this article

111Fig. 1
on p.111
112Fig. 2
on p.112
112Fig. 3
on p.112
113Fig. 4
on p.113
113Fig. 5
on p.113

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Amasaki H., Matsumoto S., Takanosu M., Daigo M. Distributions of extracellular matrix and carbonic anhydrase-III during bovine palatine ridge development. J Vet Med Sci. 1991 Dec;53(6):1031–1036. doi: 10.1292/jvms.53.1031. [DOI] [PubMed] [Google Scholar]
  2. Bianco P., Fisher L. W., Young M. F., Termine J. D., Robey P. G. Expression and localization of the two small proteoglycans biglycan and decorin in developing human skeletal and non-skeletal tissues. J Histochem Cytochem. 1990 Nov;38(11):1549–1563. doi: 10.1177/38.11.2212616. [DOI] [PubMed] [Google Scholar]
  3. Caterson B., Christner J. E., Baker J. R., Couchman J. R. Production and characterization of monoclonal antibodies directed against connective tissue proteoglycans. Fed Proc. 1985 Feb;44(2):386–393. [PubMed] [Google Scholar]
  4. Fernandez-Teran M., Bayliss M., Archer C. W. Molecular heterogeneity of chondroitin sulphate in the early developing chick wing bud. Anat Embryol (Berl) 1993 Aug;188(2):189–199. doi: 10.1007/BF00186252. [DOI] [PubMed] [Google Scholar]
  5. Fleischmajer R., Fisher L. W., MacDonald E. D., Jacobs L., Jr, Perlish J. S., Termine J. D. Decorin interacts with fibrillar collagen of embryonic and adult human skin. J Struct Biol. 1991 Feb;106(1):82–90. doi: 10.1016/1047-8477(91)90065-5. [DOI] [PubMed] [Google Scholar]
  6. Heine U. I., Munoz E. F., Flanders K. C., Roberts A. B., Sporn M. B. Colocalization of TGF-beta 1 and collagen I and III, fibronectin and glycosaminoglycans during lung branching morphogenesis. Development. 1990 May;109(1):29–36. doi: 10.1242/dev.109.1.29. [DOI] [PubMed] [Google Scholar]
  7. Kaplan E. D., Holbrook K. A. Dynamic expression patterns of tenascin, proteoglycans, and cell adhesion molecules during human hair follicle morphogenesis. Dev Dyn. 1994 Feb;199(2):141–155. doi: 10.1002/aja.1001990207. [DOI] [PubMed] [Google Scholar]
  8. Kimata K., Oike Y., Tani K., Shinomura T., Yamagata M., Uritani M., Suzuki S. A large chondroitin sulfate proteoglycan (PG-M) synthesized before chondrogenesis in the limb bud of chick embryo. J Biol Chem. 1986 Oct 15;261(29):13517–13525. [PubMed] [Google Scholar]
  9. Kitamura K. Distribution of endogenous beta-galactoside-specific lectin, fibronectin and type I and III collagens during dermal condensation in chick embryos. J Embryol Exp Morphol. 1981 Oct;65:41–56. [PubMed] [Google Scholar]
  10. Mark M. P., Baker J. R., Morrison K., Ruch J. V. Chondroitin sulfates in developing mouse tooth germs. An immunohistochemical study with monoclonal antibodies against chondroitin-4 and chondroitin-6 sulfates. Differentiation. 1990 Mar;43(1):37–50. doi: 10.1111/j.1432-0436.1990.tb00428.x. [DOI] [PubMed] [Google Scholar]
  11. Poole A. R., Webber C., Pidoux I., Choi H., Rosenberg L. C. Localization of a dermatan sulfate proteoglycan (DS-PGII) in cartilage and the presence of an immunologically related species in other tissues. J Histochem Cytochem. 1986 May;34(5):619–625. doi: 10.1177/34.5.3701029. [DOI] [PubMed] [Google Scholar]
  12. Ruoslahti E. Proteoglycans in cell regulation. J Biol Chem. 1989 Aug 15;264(23):13369–13372. [PubMed] [Google Scholar]
  13. Shinomura T., Jensen K. L., Yamagata M., Kimata K., Solursh M. The distribution of mesenchyme proteoglycan (PG-M) during wing bud outgrowth. Anat Embryol (Berl) 1990;181(3):227–233. doi: 10.1007/BF00174617. [DOI] [PubMed] [Google Scholar]
  14. Shinomura T., Nishida Y., Ito K., Kimata K. cDNA cloning of PG-M, a large chondroitin sulfate proteoglycan expressed during chondrogenesis in chick limb buds. Alternative spliced multiforms of PG-M and their relationships to versican. J Biol Chem. 1993 Jul 5;268(19):14461–14469. [PubMed] [Google Scholar]
  15. Simo P., Simon-Assmann P., Bouziges F., Leberquier C., Kedinger M., Ekblom P., Sorokin L. Changes in the expression of laminin during intestinal development. Development. 1991 Jun;112(2):477–487. doi: 10.1242/dev.112.2.477. [DOI] [PubMed] [Google Scholar]
  16. Stipp C. S., Litwack E. D., Lander A. D. Cerebroglycan: an integral membrane heparan sulfate proteoglycan that is unique to the developing nervous system and expressed specifically during neuronal differentiation. J Cell Biol. 1994 Jan;124(1-2):149–160. doi: 10.1083/jcb.124.1.149. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Swiderski R. E., Solursh M. Differential co-expression of long and short form type IX collagen transcripts during avian limb chondrogenesis in ovo. Development. 1992 May;115(1):169–179. doi: 10.1242/dev.115.1.169. [DOI] [PubMed] [Google Scholar]
  18. Thesleff I., Partanen A. M., Vainio S. Epithelial-mesenchymal interactions in tooth morphogenesis: the roles of extracellular matrix, growth factors, and cell surface receptors. J Craniofac Genet Dev Biol. 1991 Oct-Dec;11(4):229–237. [PubMed] [Google Scholar]
  19. Trautman M. S., Kimelman J., Bernfield M. Developmental expression of syndecan, an integral membrane proteoglycan, correlates with cell differentiation. Development. 1991 Jan;111(1):213–220. doi: 10.1242/dev.111.1.213. [DOI] [PubMed] [Google Scholar]
  20. Vaahtokari A., Vainio S., Thesleff I. Associations between transforming growth factor beta 1 RNA expression and epithelial-mesenchymal interactions during tooth morphogenesis. Development. 1991 Nov;113(3):985–994. doi: 10.1242/dev.113.3.985. [DOI] [PubMed] [Google Scholar]
  21. Yamagata M., Kimata K., Oike Y., Tani K., Maeda N., Yoshida K., Shimomura Y., Yoneda M., Suzuki S. A monoclonal antibody that specifically recognizes a glucuronic acid 2-sulfate-containing determinant in intact chondroitin sulfate chain. J Biol Chem. 1987 Mar 25;262(9):4146–4152. [PubMed] [Google Scholar]
  22. Yamagata M., Suzuki S., Akiyama S. K., Yamada K. M., Kimata K. Regulation of cell-substrate adhesion by proteoglycans immobilized on extracellular substrates. J Biol Chem. 1989 May 15;264(14):8012–8018. [PubMed] [Google Scholar]
  23. Zimmermann D. R., Dours-Zimmermann M. T., Schubert M., Bruckner-Tuderman L. Versican is expressed in the proliferating zone in the epidermis and in association with the elastic network of the dermis. J Cell Biol. 1994 Mar;124(5):817–825. doi: 10.1083/jcb.124.5.817. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Anatomy are provided here courtesy of Anatomical Society of Great Britain and Ireland

RESOURCES