Skip to main content
NCBI home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1985 Jan 1;100(1):18–26. doi: 10.1083/jcb.100.1.18

Glycoprotein 115, a glycoprotein isolated from chick blood vessels, is widely distributed in connective tissue

PMCID: PMC2113488  PMID: 3880750

Abstract

An extracellular glycoprotein (gp 115) with an apparent Mr = 115,000 isolated from chick aortas (Bressan, G. M., I. Castellani, A. Colombatti, and D. Volpin, 1983, J. Biol. Chem., 258:13262-13267), was used to immunize mice. The antisera were shown to specifically recognize gp 115 by numerous criteria: a major band around Mr = 115,000 plus minor bands of lower Mr were visible by immunoblotting on aorta extracts, and a similar pattern was observed with a monoclonal antibody; no cross-reactivity was detected by radioimmunobinding with other extracellular proteins, namely, fibronectin, laminin, and collagen types I, III, IV, V, and VI. Antigen distribution on frozen tissue sections from newborn chicks was investigated by using affinity- purified antibody. Strong immunoreactivity was always found in blood vessels. In the digestive tract, the fluorescent staining was localized both at the level of muscular layers and in the stromal matrix of the villi. Within skeletal muscle and myocardium, staining was associated with large connective tissue bundles and the matrix around each muscle fiber. Intense fluorescence was observed in the kidney, in smooth muscle cells rich areas of parabronchi, and within the portal space and along liver sinusoids. The antigen was not detected at the epidermal- dermal junction; immunoreactivity in the dermis was present as a diffuse fibrillar pattern. That the antigen detected by immunofluorescence in the various organs was indeed gp 115 was demonstrated by immunoblotting analysis: as in aorta extracts, a major band around Mr = 115,000 was detected in several tissues. Antibody- reacting material was also incorporated into the extracellular matrix produced by embryo smooth muscle cells grown in vitro and was organized as a meshwork of fine fibrils.

Full Text

The Full Text of this article is available as a PDF (3.3 MB).

Selected References

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

  1. Barnes D. W., Silnutzer J. Isolation of human serum spreading factor. J Biol Chem. 1983 Oct 25;258(20):12548–12552. [PubMed] [Google Scholar]
  2. Bornstein P., Sage H. Structurally distinct collagen types. Annu Rev Biochem. 1980;49:957–1003. doi: 10.1146/annurev.bi.49.070180.004521. [DOI] [PubMed] [Google Scholar]
  3. Boselli J. M., Macarak E. J., Clark C. C., Brownell A. G., Martinez-Hernandez A. Fibronectin: its relationship to basement membranes. I. Light microscopic studies. Coll Relat Res. 1981 Sep;1(5):391–404. doi: 10.1016/s0174-173x(81)80024-6. [DOI] [PubMed] [Google Scholar]
  4. Bressan G. M., Castellani I., Colombatti A., Volpin D. Isolation and characterization of a 115,000-dalton matrix-associated glycoprotein from chick aorta. J Biol Chem. 1983 Nov 10;258(21):13262–13267. [PubMed] [Google Scholar]
  5. Bressan G. M., Castellani I., Colombatti A., Volpin D. Isolation and characterization of a 115,000-dalton matrix-associated glycoprotein from chick aorta. J Biol Chem. 1983 Nov 10;258(21):13262–13267. [PubMed] [Google Scholar]
  6. Bressan G. M., Prockop D. J. Synthesis of elastin in aortas from chick embryos. Conversion of newly secreted elastin to cross-linked elastin without apparent proteolysis of the molecule. Biochemistry. 1977 Apr 5;16(7):1406–1412. doi: 10.1021/bi00626a026. [DOI] [PubMed] [Google Scholar]
  7. Carlin B., Jaffe R., Bender B., Chung A. E. Entactin, a novel basal lamina-associated sulfated glycoprotein. J Biol Chem. 1981 May 25;256(10):5209–5214. [PubMed] [Google Scholar]
  8. Chamley-Campbell J. H., Campbell G. R., Ross R. Phenotype-dependent response of cultured aortic smooth muscle to serum mitogens. J Cell Biol. 1981 May;89(2):379–383. doi: 10.1083/jcb.89.2.379. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Chamley-Campbell J., Campbell G. R., Ross R. The smooth muscle cell in culture. Physiol Rev. 1979 Jan;59(1):1–61. doi: 10.1152/physrev.1979.59.1.1. [DOI] [PubMed] [Google Scholar]
  10. Hay E. D. Extracellular matrix. J Cell Biol. 1981 Dec;91(3 Pt 2):205s–223s. doi: 10.1083/jcb.91.3.205s. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hayman E. G., Pierschbacher M. D., Ohgren Y., Ruoslahti E. Serum spreading factor (vitronectin) is present at the cell surface and in tissues. Proc Natl Acad Sci U S A. 1983 Jul;80(13):4003–4007. doi: 10.1073/pnas.80.13.4003. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kleinman H. K., Klebe R. J., Martin G. R. Role of collagenous matrices in the adhesion and growth of cells. J Cell Biol. 1981 Mar;88(3):473–485. doi: 10.1083/jcb.88.3.473. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  14. Linder E., Vaheri A., Ruoslahti E., Wartiovaara J. Distribution of fibroblast surface antigen in the developing chick embryo. J Exp Med. 1975 Jul 1;142(1):41–49. doi: 10.1084/jem.142.1.41. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Olmsted J. B. Affinity purification of antibodies from diazotized paper blots of heterogeneous protein samples. J Biol Chem. 1981 Dec 10;256(23):11955–11957. [PubMed] [Google Scholar]
  16. Poole A. R., Pidoux I., Reiner A., Cöster L., Hassell J. R. Mammalian eyes and associated tissues contain molecules that are immunologically related to cartilage proteoglycan and link protein. J Cell Biol. 1982 Jun;93(3):910–920. doi: 10.1083/jcb.93.3.910. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Rohde H., Wick G., Timpl R. Immunochemical characterization of the basement membrane glycoprotein laminin. Eur J Biochem. 1979 Dec;102(1):195–201. doi: 10.1111/j.1432-1033.1979.tb06280.x. [DOI] [PubMed] [Google Scholar]
  18. Stefanini M., De Martino C., Zamboni L. Fixation of ejaculated spermatozoa for electron microscopy. Nature. 1967 Oct 14;216(5111):173–174. doi: 10.1038/216173a0. [DOI] [PubMed] [Google Scholar]
  19. Stenman S., Vaheri A. Distribution of a major connective tissue protein, fibronectin, in normal human tissues. J Exp Med. 1978 Apr 1;147(4):1054–1064. doi: 10.1084/jem.147.4.1054. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES