Heat shock proteins: Molecules with assorted functions

Sarkar, Surajit; Singh, Mayanglambam Dhruba; Yadav, Renu; Arunkumar, Kallare P.; Pittman, Geoffrey W.

doi:10.1007/s11515-011-1080-3

Cited by 20 publications

(13 citation statements)

References 197 publications

(207 reference statements)

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“…In addition to their function as molecular chaperones, they function in protein disaggregation and protein degradation when removal of potentially harmful polypeptides arising from misfolding, denaturation, or aggregation are important for the maintenance of cellular homeostasis. The mechanism for rescuing proteins from aggregation is proposed to include the cooperation HSP100 (Kregel, 2002;Sarkar et al, 2011). HSPs are typically induced when cells are exposed to various types of environmental stresses.…”

Section: Biological or Biochemical Functions Of Flood-and Heat-responmentioning

confidence: 99%

Comparative proteomic analysis of cauliflower under high temperature and flooding stresses

Lin

Chen

et al. 2015

Scientia Horticulturae

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a b s t r a c tHigh-temperature and waterlogging are major abiotic stresses that affect the yield and quality of cauliflower. Cauliflower cultivars 'H41' and 'H69' are tolerant to high temperature and flooding, respectively; however, 'H71' is sensitive to both stresses. The objectives of this study were to identify the proteins that were differentially regulated and the physiological changes that occurred during different time periods in 'H41', 'H69', and 'H71' when responding to treatments of flooding, 40 • C, and both stresses combined. Changes in the leaf proteome were analyzed by matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS) and identified by Mascot peptide mass fingerprint (PMF) and database searching. Stress treatments caused significant reductions in electrolyte leakage, chlorophyll fluorescence Fv/Fm, chlorophyll content, and water potential as stress times were prolonged. By the comparative proteomic analysis, 85 protein peaks that were differentially expressed in response to combination treatments at 0, 6, and 24 h, 69 (33 in 'H41', 29 in 'H69', and 9 in 'H71') were identified, of which were cultivar specific. Differentially regulated proteins predominantly functioned in photosynthesis and to a lesser extent in energy metabolism, cellular homeostasis, transcription and translation, signal transduction, and protein biosynthesis. This is the first report that utilizes proteomics to discover changes in the protein expression profile of cauliflower in response to heat and flooding.

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Section: Biological or Biochemical Functions Of Flood-and Heat-responmentioning

confidence: 99%

Comparative proteomic analysis of cauliflower under high temperature and flooding stresses

Lin

Chen

et al. 2015

Scientia Horticulturae

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“…The majority of chaperone proteins identified were part of the chaperonin-containing TCP1 complex (CCT complex), which is composed of eight unique subunits that are stacked like two donuts on top of each other to create a barrel. It is thought to primarily fold and stabilise cytoskeletal proteins due to the continuous presence of tubulin and actin in the CCT complex (Sarkar et al 2011). The CCT complex shows a unique plasma membrane localisation (bull; Byrne et al 2012, boar;Belleannee et al 2011, human;Redgrove et al 2011 and mouse;Dun et al 2011) in spermatozoa and has been shown to associate with proteins of zona-binding affinity.…”

Section: Chaperone-related Proteins Correlated With Ram Sperm Functiomentioning

confidence: 99%

Ram seminal plasma and its functional proteomic assessment

Leahy¹,

Rickard²,

Bernecic³

et al. 2019

Reproduction

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Ejaculation results in the confluence of epididymal spermatozoa with secretions of the accessory sex glands. This interaction is not a prerequisite for fertilisation success, but seminal factors do play a crucial role in prolonging the survival of spermatozoa both in vitro and in vivo by affording protection from handling induced stress and some selective mechanisms of the female reproductive tract. Reproductive biologists have long sought to identify specific factors in seminal plasma that influence sperm function and fertility in these contexts. Many seminal plasma proteins have been identified as diagnostic predictors of sperm function and have been isolated and applied in vitro to prevent sperm damage associated with the application of artificial reproductive technologies. Proteomic assessment of the spermatozoon, and its surroundings, has provided considerable advances towards these goals and allowed for greater understanding of their physiological function. In this review, the importance of seminal plasma will be examined through a proteomic lens to provide comprehensive analysis of the ram seminal proteome and detail the use of proteomic studies that correlate seminal plasma proteins with ram sperm function and preservation ability.

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“…Hsps or stress proteins are also known as molecular chaperones, because they are synthesized in increased amounts after brief exposure of cells to an elevated temperature, or a variety of other stresses such as irradiation, viral infection, oxidative stress, etc. [14]. They represent groups of ubiquitous and highly conserved protein families which utilize ATPs to stabilize unfolded proteins, or unfold them for translocation through membranes, or mark them for degradation [14].…”

Section: Heat Shock Proteins and Agingmentioning

confidence: 99%