Transcription of the genes encoding the small heat shock protein ubiquitin is unchanged in patients with systemic lupus erythematosus.

The heat shock proteins hsp90 and hsp70 have been shown to be over-expressed in peripheral blood mononuclear cells from SLE patients. We show, however, that transcription of the three genes encoding the small hsp ubiquitin is not enhanced in these patients. The over expression of hsp90 and hsp70 in SLE is likely therefore to reflect cellular events resulting in the specific induction of these hsps rather than a generalized induction of all hsp synthesis due to the stress of the disease or the presence of fever.

[1]  Latchman Ds.  Heat shock proteins and human disease. , 1991 .

[2]  S. Kishimoto,et al.  Enhanced expression of the heat shock protein gene in peripheral blood mononuclear cells of patients with active systemic lupus erythematosus. , 1990, Annals of the rheumatic diseases.

[3]  D. Isenberg,et al.  Elevated levels of the 90 kd heat shock protein in a proportion of SLE patients with active disease. , 1989, Journal of autoimmunity.

[4]  S. Muller,et al.  Presence of antibodies to ubiquitin during the autoimmune response associated with systemic lupus erythematosus. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[5]  M. Peterson,et al.  Mitogen activation induces the enhanced synthesis of two heat-shock proteins in human lymphocytes , 1988, Journal of Cell Biology.

[6]  S. Kishimoto,et al.  Heat-shock protein synthesis by human peripheral mononuclear cells from SLE patients. , 1987, Biochemical and biophysical research communications.

[7]  S. Krane,et al.  Hormone 1 alpha,25-dihydroxyvitamin D3 modulates heat shock response in monocytes. , 1987, The American journal of physiology.

[8]  R. Baker,et al.  The human ubiquitin gene family: structure of a gene and pseudogenes from the Ub B subfamily. , 1987, Nucleic acids research.

[9]  D. Latchman,et al.  Transcriptional induction of cellular gene expression during lytic infection with herpes simplex virus , 1986, Bioscience reports.

[10]  D. Latchman,et al.  Isolation of cDNA clones derived from a cellular gene transcriptionally induced by herpes simplex virus. , 1986, Nucleic acids research.

[11]  R. Steinman,et al.  Lymphokine and nonlymphokine mRNA levels in stimulated human T cells. Kinetics, mitogen requirements, and effects of cyclosporin A , 1986, The Journal of experimental medicine.

[12]  P. Schiller,et al.  Isolation and functional analysis of a human 70,000-dalton heat shock protein gene segment. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[13]  J. Vuust,et al.  The human ubiquitin multigene family: some genes contain multiple directly repeated ubiquitin coding sequences. , 1985, The EMBO journal.

[14]  G. Stein,et al.  Evidence for a human histone gene cluster containing H2B and H2A pseudogenes. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[15]  H. Pelham.  A regulatory upstream promoter element in the Drosophila Hsp 70 heat-shock gene , 1982, Cell.

[16]  S. Koyasu,et al.  Autoantibodies to the heat-shock protein hsp90 in systemic lupus erythematosus. , 1988, The Journal of clinical investigation.

[17]  S. Lindquist,et al.  The heat-shock proteins. , 1988, Annual review of genetics.

[18]  S. Lindquist.  The heat-shock response. , 1986, Annual review of biochemistry.

[19]  J. Winfield,et al.  Brief Definitive Report AUTOANTIBODIES TO THE CONSTITUTIVE 73-kD MEMBER OF THE hsp70 FAMILY OF HEAT SHOCK PROTEINS IN SYSTEMIC LUPUS ERYTHEMATOSUS , 2022 .