Proteins related to the mouse L-cell major heat shock protein are synthesized in the absence of heat shock gene expression.

Lowe, David; Moran, Larry A.

doi:10.1073/pnas.81.8.2317

Cited by 65 publications

(48 citation statements)

References 44 publications

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“…The 70-kD protein occurred as a major charge species of pI 5.9, as estimated by comparison with the known isoelectric points of aAz-crystallin (pI 5.92; 11), lens 3' actin (pI 5.45; 29), and vimentin (pI 5.35; 38). The molecular weight and isoelectric point of this rat lens stress protein are in good agreement with published values for the major mammalian heat shock-induced proteins (hsp70), which range between Mr 66,000 and 72,000, and pI 5.6 and 6.3 (26,34,44,48). Also the position after two-dimensional gel electrophoresis of the rat lens 70-kD protein relative to actin, tubulin, and vimentin corresponds very well with published patterns for the major heat shock-or stress-induced protein in other cell types, in culture, or in vivo (6,15,19,26,44).…”

Section: Characterization Of the Heat-induced Rat Lens Proteinssupporting

confidence: 73%

“…The lens protein of 71 kD, of which the synthesis increased upon heat shock, can reasonably be identified as P73 (15,26,49), a constitutive protein present at considerable levels in many investigated normal cell types, and of which the synthesis is indeed stimulated by heat shock. It has been shown that P73 is closely related to SP71 (15,26).…”

Section: Characterization Of the Heat-induced Rat Lens Proteinsmentioning

confidence: 99%

“…It has been shown that P73 is closely related to SP71 (15,26). These proteins correspond indeed to the two primary members of the 70-kD family of heat shock proteins; the former representing the constitutive form, and the latter the highly inducible form.…”

Section: Characterization Of the Heat-induced Rat Lens Proteinsmentioning

confidence: 99%

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Heat shock response of the rat lens.

Jong¹,

Hoekman²,

Mulders³

et al. 1986

The Journal of Cell Biology

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Abstract. The sequence relationship between the small heat shock proteins and the eye lens protein acrystallin (Ingolia, T. D., and E. E. Craig, 1982, Proc. Natl. Acad. Sci. USA, 79:2360-2364 prompted us to subject rat lenses in organ culture to heat shock and other forms of stress. The effects on protein synthesis were followed by labeling with [35S]methionine and analysis by one-and two-dimensional gel electrophoresis and fluorography. Heat shock gave a pronounced induction of a protein that could be characterized as the stress protein SP71. This protein probably corresponds to the major mammalian heat shock protein hsp70. Also two minor proteins of 16 and 85 kD were induced, while the synthesis of a constitutive heat shock-related protein, P73, was considerably increased. The synthesis of SP71 started between 30 and 60 min after heat shock, reached its highest level after 3 h, and had stopped again after 8 h. In rat lenses that were preconditioned by an initial mild heat shock, a subsequent shock did not cause renewed synthesis of SP71. This effect resembles the thermotolerance phenomenon observed in cultured cells. The proline analogue azetidine-2-carboxylic acid, zinc chloride, ethanol, and calcium chloride did not, under the conditions used, induce stress proteins in the rat lens. Sodium arsenite, however, had very much the same effects as heat shock. Calcium ionophore A23187 specifically and effectively induced the synthesis of the glucose-regulated protein GRP78. No special response to stress on crystallin synthesis was noticed.T HE heat shock response of eukaryotic cells is characterized by the induction of a specific set of heat shock or stress proteins, and the concurrent development of thermotolerance, i.e., increased resistance to subsequent stress (34,42). It has been shown that also in vivo and in organ culture several mammalian tissues respond to heat shock or other forms of stress by the synthesis of one or more heat shock proteins (5-7, 9, 10, 28).A study of the effects of stress on the vertebrate eye lens is of interest for a number of reasons. The eye lens might be expected to need a very efficient protection or resistance against chemical and physical insults, because the differentiated lens fiber cells are never broken down or replaced (3, 11), and hence have to maintain a reasonable degree of structural and functional integrity throughout life. On the other hand the lens is quite likely to become exposed to stressful conditions because of its superficial location in combination with the absence of direct blood supply and innervation which hampers an efficient and rapid homeostatic regulation of the intraceUular environment. Moreover, the older lens fiber cells loose their nuclei and ribosomes (3) and hence the ability to respond to stress by the synthesis of heat shock proteins. Chronic exposure of the lens to elevated temperatures induces cortical cataracts (39).Also the intriguing structural relationships between the heat shock proteins and the lens-specific crystallins make a study of ...

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Section: Characterization Of the Heat-induced Rat Lens Proteinssupporting

confidence: 73%

Section: Characterization Of the Heat-induced Rat Lens Proteinsmentioning

confidence: 99%

See 1 more Smart Citation

Heat shock response of the rat lens.

Jong¹,

Hoekman²,

Mulders³

et al. 1986

The Journal of Cell Biology

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“…Other five of these 18 SP-proteins (EGF-like repeat and discoidin I-like domain-containing protein 3, Putative phospholipase B-like 2 isoform 1, Prominin-2, Ezrin and Syntaxinbinding protein 2) have been related with sperm capacitation [63][64][65][66][67]. Heat shock cognate 71 kDa is a protein related to environmental or physiological stresses [68] synthesized by sperm cells [69] that has been recently related to boar sperm cryotolerance [70]. Finally, Ectonucleotide pyrophosphatase/phosphodiesterase family member is an ATPhydrolyzing enzyme described in epididymis suggesting that this protein could be involved in the modulation of the epididymal environment [71].…”

Section: Discussionmentioning

confidence: 99%

Characterization of the porcine seminal plasma proteome comparing ejaculate portions

Pérez-Patiño

Barranco

Parrilla

et al. 2016

Journal of Proteomics

102

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Full identification of SP-proteins remains challenging, particularly in some livestock species such as porcine. This experimental study aims to provide an extensive proteomic analysis of boar SP and to generate a public accessible database of boar SP-proteome. A SP-pool from 33 entire ejaculates from 11 boars (3 ejaculates per boar) was analyzed to characterize the boar SP-proteome. Moreover, 20 ejaculates collected in fractions (P1: first 10 mL of sperm rich ejaculate fraction (SRF), P2: rest of SRF and P3: post-SRF) from 5 boars (4 ejaculates per boar) were analyzed to evaluate differentially expressed SP-proteins among portions. SP-samples were subjected to a combination of SEC, 1-D SDS PAGE and NanoLC-ESI-MS/MS followed by functional bioinformatics analysis.The identified proteins were quantified from normalized LFQ intensity data. A total of 33,557 spectra corresponding to 8,189 peptides and 536 SP-proteins were identified with ≥ 95% Confidence (Unused Score > 1.3) and a false discovery rate (FDR) ≤ 1%. Of the 536 SP-proteins, 409 were identified in Sus Scrofa taxonomy and 374 of them were Biological Significance: This proteomic study provides the major characterization of the boar SP-proteome with more than 250 proteins first reported. The boar SP-proteome is described so that a spectral library can be built for relative 'label free' protein quantitation with SWATH approach. This proteomic profiling allows the creation of a publicly accessible database of the boar SP-proteome, as a first step for further understanding the role of SP-proteins in reproductive outcomes as well as for identification of biomarkers for sperm quality and fertility.

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“…Densitometric scanning of the autoradiograph indicated an approximately fivefold increase in expression of the 70-kDa protein and two-to threefold increases of the 89-and 74-kDa bands at 43°C. Proteins of these sizes have been identified previously as heat shock products in mammalian cells (5,15,16,22,24,25). In melanogaster, it is thought that at least one protein interacts with the heat shock regulatory region located upstream from the 5' end of the heat shock genes (29,38,39).…”

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confidence: 99%