Skip to main content
Molecular and Cellular Biology logoLink to Molecular and Cellular Biology
. 1993 Mar;13(3):1516–1521. doi: 10.1128/mcb.13.3.1516

Hibernation-associated gene regulation of plasma proteins with a collagen-like domain in mammalian hibernators.

N Takamatsu 1, K Ohba 1, J Kondo 1, N Kondo 1, T Shiba 1
PMCID: PMC359463  PMID: 8441393

Abstract

In mammals, hibernation is expressed by only a limited number of species, and the molecular mechanisms underlying hibernation are not well understood. Recently, we have found plasma proteins which disappear from blood specifically during hibernation in a mammalian hibernator, the chipmunk. Here, we report the cDNA cloning of these chipmunk hibernation-related proteins, HP-20, -25, and -27, and analyses of their expression. All three proteins contain a collagen-like domain near the N terminus and are highly homologous to each other. Their mRNAs were detected only in liver in nonhibernating chipmunks, and in hibernating chipmunks, the amounts were reduced to less than 1/10 of those in nonhibernating chipmunks, indicating that HP-20, -25, and -27 mRNA expression is regulated similarly in association with hibernation. Southern blot analyses of the squirrel family with each of chipmunk HP-20, -25, and -27 cDNA revealed that a nonhibernating species (tree squirrel) as well as another hibernating species (ground squirrel) retained the corresponding genes. However, their transcripts were detected only with the hibernating species, and in hibernating ground squirrels, their levels were greatly reduced compared with those in nonhibernating animals, as were the cases with the chipmunk. These observations are the first line of evidence for occurrence of hibernation-associated gene regulation. The results would indicate the commitment of HP-20, -25, and -27 to hibernation and support the idea that genetic controls are involved in mammalian hibernation.

Full text

PDF
1516

Images in this article

Selected References

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

  1. Benson B., Hawgood S., Schilling J., Clements J., Damm D., Cordell B., White R. T. Structure of canine pulmonary surfactant apoprotein: cDNA and complete amino acid sequence. Proc Natl Acad Sci U S A. 1985 Oct;82(19):6379–6383. doi: 10.1073/pnas.82.19.6379. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Blondel A., Thillet J. A fast and convenient way to produce single stranded DNA from a phagemid. Nucleic Acids Res. 1991 Jan 11;19(1):181–181. doi: 10.1093/nar/19.1.181. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Drickamer K., Dordal M. S., Reynolds L. Mannose-binding proteins isolated from rat liver contain carbohydrate-recognition domains linked to collagenous tails. Complete primary structures and homology with pulmonary surfactant apoprotein. J Biol Chem. 1986 May 25;261(15):6878–6887. [PubMed] [Google Scholar]
  4. Drickamer K. Two distinct classes of carbohydrate-recognition domains in animal lectins. J Biol Chem. 1988 Jul 15;263(20):9557–9560. [PubMed] [Google Scholar]
  5. Flink I. L., Bailey T. J., Gustafson T. A., Markham B. E., Morkin E. Complete amino acid sequence of human thyroxine-binding globulin deduced from cloned DNA: close homology to the serine antiproteases. Proc Natl Acad Sci U S A. 1986 Oct;83(20):7708–7712. doi: 10.1073/pnas.83.20.7708. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hammond G. L., Smith C. L., Goping I. S., Underhill D. A., Harley M. J., Reventos J., Musto N. A., Gunsalus G. L., Bardin C. W. Primary structure of human corticosteroid binding globulin, deduced from hepatic and pulmonary cDNAs, exhibits homology with serine protease inhibitors. Proc Natl Acad Sci U S A. 1987 Aug;84(15):5153–5157. doi: 10.1073/pnas.84.15.5153. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hirayoshi K., Kudo H., Takechi H., Nakai A., Iwamatsu A., Yamada K. M., Nagata K. HSP47: a tissue-specific, transformation-sensitive, collagen-binding heat shock protein of chicken embryo fibroblasts. Mol Cell Biol. 1991 Aug;11(8):4036–4044. doi: 10.1128/mcb.11.8.4036. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Kodama T., Freeman M., Rohrer L., Zabrecky J., Matsudaira P., Krieger M. Type I macrophage scavenger receptor contains alpha-helical and collagen-like coiled coils. Nature. 1990 Feb 8;343(6258):531–535. doi: 10.1038/343531a0. [DOI] [PubMed] [Google Scholar]
  9. Kondo N., Kondo J. Identification of novel blood proteins specific for mammalian hibernation. J Biol Chem. 1992 Jan 5;267(1):473–478. [PubMed] [Google Scholar]
  10. Krejci E., Coussen F., Duval N., Chatel J. M., Legay C., Puype M., Vandekerckhove J., Cartaud J., Bon S., Massoulié J. Primary structure of a collagenic tail peptide of Torpedo acetylcholinesterase: co-expression with catalytic subunit induces the production of collagen-tailed forms in transfected cells. EMBO J. 1991 May;10(5):1285–1293. doi: 10.1002/j.1460-2075.1991.tb08070.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Lee Y. M., Leiby K. R., Allar J., Paris K., Lerch B., Okarma T. B. Primary structure of bovine conglutinin, a member of the C-type animal lectin family. J Biol Chem. 1991 Feb 15;266(5):2715–2723. [PubMed] [Google Scholar]
  12. Reid K. B. Proteins involved in the activation and control of the two pathways of human complement. Biochem Soc Trans. 1983 Jan;11(1):1–12. doi: 10.1042/bst0110001. [DOI] [PubMed] [Google Scholar]
  13. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Staunton D. E., Marlin S. D., Stratowa C., Dustin M. L., Springer T. A. Primary structure of ICAM-1 demonstrates interaction between members of the immunoglobulin and integrin supergene families. Cell. 1988 Mar 25;52(6):925–933. doi: 10.1016/0092-8674(88)90434-5. [DOI] [PubMed] [Google Scholar]
  15. Thiel S., Reid K. B. Structures and functions associated with the group of mammalian lectins containing collagen-like sequences. FEBS Lett. 1989 Jun 19;250(1):78–84. doi: 10.1016/0014-5793(89)80689-1. [DOI] [PubMed] [Google Scholar]

Articles from Molecular and Cellular Biology are provided here courtesy of Taylor & Francis

RESOURCES