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Expression of Stress Proteins (HSP-70 and HSP-90) in the Rabbit Urinary Bladder Subjected to Partial Outlet Obstruction

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Publisher Springer
Specialty Biochemistry
Date 1994 Jan 12
PMID 8190120
Citations 7
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Abstract

Partial obstruction of the rabbit bladder outlet induces a rapid hypertrophy characterized by increased bladder mass, increased smooth muscle content, and increased collagen deposition. In addition, partial outlet obstruction induces decreased contractile responses to both field stimulation and postsynaptic receptor stimulation. Although the morphological and contractile responses to partial outlet obstruction have been well characterized, there is little information on the cellular and molecular mechanisms of these changes. In a previous study, we demonstrated that one of the earliest genes to be expressed following partial outlet obstruction in rabbits was the gene expressing stress protein-70 (HSP-70). In order to further define the genetic and molecular basis of these responses, the expression of stress gene products HSP-70 and HSP-90 in rabbit urinary bladder subjected to partial outlet obstruction has been quantitatively evaluated by Western blot coupled with laser densitometry using anti-HSP-70 and -90 monoclonal antibodies. The data show that stress gene products HSP-70 and HSP-90 are constitutively expressed in control rabbit bladder tissue and transiently increased following partial outlet obstruction. Increased content of HSP-70 was detected at 6 hr after obstruction and reached a maximum (2.7-fold over the control level) at 24 hr. Increased HSP-90 was also detected at 6 hr but reached a maximum (4.5-fold over the control level) at 12 hr. By 7 day post-obstruction, the content of these two proteins returned to the control levels.(ABSTRACT TRUNCATED AT 250 WORDS)

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References
1.
BURDON R . Heat shock and the heat shock proteins. Biochem J. 1986; 240(2):313-24. PMC: 1147420. DOI: 10.1042/bj2400313. View

2.
Malkowicz S, Wein A, Elbadawi A, Van Arsdalen K, Ruggieri M, Levin R . Acute biochemical and functional alterations in the partially obstructed rabbit urinary bladder. J Urol. 1986; 136(6):1324-9. DOI: 10.1016/s0022-5347(17)45331-6. View

3.
Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

4.
Zhao Y, Levin R, Monson F, Chacko S . Expression of constitutive heat shock protein-70 in normal (non-stressed) rabbit urinary bladder tissue. Mol Cell Biochem. 1993; 121(1):13-9. DOI: 10.1007/BF00928695. View

5.
Caltabiano M, Koestler T, Poste G, Greig R . Induction of 32- and 34-kDa stress proteins by sodium arsenite, heavy metals, and thiol-reactive agents. J Biol Chem. 1986; 261(28):13381-6. View