Heat shock proteins: the search for functions.

Schlesinger, Milton J.

doi:10.1083/jcb.103.2.321

Cited by 370 publications

(122 citation statements)

References 77 publications

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“…Heat-shock proteins are classified into four families, namely, HSP90, HSP70, HSP60, and low molecular weight heat-shock proteins. Among these, HSP90 and HSP70 are the major ones [26,27].…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of an endogenous inhibitor specific to the Z‐Leu‐Leu‐Leu‐MCA degrading activity in proteasome and its identification as heat‐shock protein 90

1994

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We previously identified a benzyloxycarbonyl(Z)-Leu-Leu-Leu-4-methylcoumaryl-7-amide (ZLLL-MCA) degrading activity in proteasome as a candidate for the regulator of neurite outgrowth. As its counterpart, we purified a protein from bovine brain that specifically inhibits the ZLLL-MCA degrading activity in proteasome. This protein is heat stable and has no effect on the other catalytic activities in proteasome, or on the activities of trypsin, chymotrypsin, or m-and p-calpains either. The molar ratio ofinhibitor-to-proteasome that inhibits 50% of the ZLLL-MCA degrading activity of proteasome is 1:1. The inhibitory mechanism of the inhibitor against proteasome is non-competitive. Finally, the inhibitor was identified as heat-shock protein 90 (HSP90) by partial amino acid sequencing and immunodetection. The results suggest that HSP90 initiates neurite outgrowth through the inhibition of the ZLLL-MCA degrading activity in proteasome.

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“…Heat-shock proteins are classified into four families, namely, HSP90, HSP70, HSP60, and low molecular weight heat-shock proteins. Among these, HSP90 and HSP70 are the major ones [26,27].…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of an endogenous inhibitor specific to the Z‐Leu‐Leu‐Leu‐MCA degrading activity in proteasome and its identification as heat‐shock protein 90

1994

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“…The most prominent HSPs of mammalian cells have molecular weights of approximately 90,000 (HSP90), and 70,000 (HSP70) [1], [3]. Many studies have suggested a possible correlation between the expression of HSPs and the growth and differentiation of tumor cells [4][5][6][7][8][9].…”

Section: Introductionmentioning

confidence: 99%

The expression of glucose regulated protein-94 in colorectal carcinoma cells treated by sodium butyrate

Jin

2000

Cell Res

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The expression of glucose regulated protein 94 (GRP94) during the treatment of human colorectal carcinoma cell lineClone A cells with sodium butyrate was studied. Sodium butyrate (SB) can cause functional and morphological effects on Clone A cells including growth arrest at G 0 /G 1 stage and cell differentiation as observed by morphological changes, MTT and flow cytometry assays, as well as reduced Grp94 gene expression as shown by Northern blot and Western blot assays. The possible mechanism of the correlation between Grp94 gene expression and tumor growth inhibition and cell differentiation is briefly discussed.

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“…Recent focus has been placed on the ability of 70K heatshock proteins (70K hsps) to modulate virus phenotypic expression (Schlesinger, 1986). The 70K and 90K hsps are the major heat-shock protein families expressed by mammalian cells (Welch et al, 1982).…”

Section: Interaction Of Canine Distemper Virus Nucleocapsid Variants mentioning

confidence: 99%

Interaction of canine distemper virus nucleocapsid variants with 70K heat-shock proteins

Oglesbee

Ringler

Krakowka

1990

Journal of General Virology

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Heat shock proteins: the search for functions.

Cited by 370 publications

References 77 publications

Purification and characterization of an endogenous inhibitor specific to the Z‐Leu‐Leu‐Leu‐MCA degrading activity in proteasome and its identification as heat‐shock protein 90

Purification and characterization of an endogenous inhibitor specific to the Z‐Leu‐Leu‐Leu‐MCA degrading activity in proteasome and its identification as heat‐shock protein 90

The expression of glucose regulated protein-94 in colorectal carcinoma cells treated by sodium butyrate

Interaction of canine distemper virus nucleocapsid variants with 70K heat-shock proteins

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