We are analyzing https://link.springer.com/article/10.1007/s12192-019-01044-5.

Title:
Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes | Cell Stress and Chaperones
Description:
Heat shock proteins (HSPs), a large group of highly evolutionary conserved proteins, are considered to be main elements of the cellular proteoprotection system. HSPs are encoded by genes activated during the exposure of cells to proteotoxic factors, as well as by genes that are expressed constitutively under physiological conditions. HSPs, having properties of molecular chaperones, are involved in controlling/modulation of multiple cellular and physiological processes. In the presented review, we summarize the current knowledge on HSPs in the biology of epidermis, the outer skin layer composed of stratified squamous epithelium. This tissue has a vital barrier function preventing from dehydratation due to passive diffusion of water out of the skin, and protecting from infection and other environmental insults. We focused on HSPB1 (HSP27), HSPA1 (HSP70), HSPA2, and HSPC (HSP90), because only these HSPs have been studied in the context of physiology and pathophysiology of the epidermis. The analysis of literature data shows that HSPB1 plays a role in the regulation of final steps of keratinization; HSPA1 is involved in the cytoprotection, HSPA2 contributes to the early steps of keratinocyte differentiation, while HSPC is essential in the re-epithelialization process. Since HSPs have diverse functions in various types of somatic tissues, in spite of multiple investigations, open questions still remain about detailed roles of a particular HSP isoform in the biology of epidermal keratinocytes.
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Keywords {🔍}

pubmed, google, scholar, article, cas, keratinocytes, skin, hspa, expression, human, protein, heat, cells, hspb, shock, hsp, cell, epidermal, hspc, proteins, epidermis, central, wound, dermatol, stress, differentiation, healing, mice, gene, keratinocyte, role, studies, hsps, response, levels, irradiation, chaperones, mouse, trautinger, invest, biol, scieglinska, increased, basal, cancer, treatment, phosphorylation, hacat, level, found,

Topics {✒️}

lrp-1/cd91-mediated pro-migratory signaling α-melanocyte stimulating hormone hsf1/sesn3/p21cip1/waf1 pathways testis-specific hsp70-related gene uv-b-induced dna damage mitogen-activated protein kinases article download pdf hpv16 e6/e7 oncoproteins small heat-shock proteins laser-assisted pre-heating chaperone-defective hspc1-δ mutant ultraviolet b-induced apoptosis low-level light/laser therapy radioactive protein-labelling techniques fast-dividing progenitor cells testis-specific protein critical testis-enriched hspa2 protein transforming growth factor-alpha activate pro-inflammatory responses ultraviolet b-mediated phosphorylation telomerase-immortalized keratinocytes revealed parp-dependent energy crisis fast-cycling stem cells tnf-α induced phosphorylation tnf-α-activated cells gamal el din streptococcal-induced autoimmune response p38-mapk-mediated phosphorylation uv-induced cell death short-duration high temperature heat-shocked skin cells rabbit monoclonal anti-hspa2 laser-assisted skin closure laser-mediated skin heating long-lived stem cell hspc1-δ variant deficient hspb1del/del mice showed stress-induced intracellular sorting paraffin-embedded human skin cell-type specific fashion ethylene diamine inhibits algal uv-absorbing compounds uvb-induced oxidative stress anti-apoptotic protein hsp27 dab-mediated immunohistochemical staining x-linked recessive ichthyosis central basal cell heat-inducible hspa genes reduced clone-forming ability metal chelator nnnnn-tetrakis

Questions {❓}

Arrigo AP, Ducasse C (2002) Expression of the anti-apoptotic protein Hsp27 during both the keratinocyte differentiation and dedifferentiation of HaCaT cells: expression linked to changes in intracellular protein organization?
Calderwood SK (2018) Heat shock proteins and cancer: intracellular chaperones or extracellular signalling ligands?
Guo J, Chang C, Li W (2017) The role of secreted heat shock protein-90 (Hsp90) in wound healing—how could it shape future therapeutics?
Jeanmaire C, Pauly G, Moser P, Danoux L, Bardey V, Moussou P (2003) What is the most suitable strategy for stress proteins in cosmetics?
Radons J (2016) The human HSP70 family of chaperones: where do we stand?

Schema {🗺️}

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         headline:Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes
         description:Heat shock proteins (HSPs), a large group of highly evolutionary conserved proteins, are considered to be main elements of the cellular proteoprotection system. HSPs are encoded by genes activated during the exposure of cells to proteotoxic factors, as well as by genes that are expressed constitutively under physiological conditions. HSPs, having properties of molecular chaperones, are involved in controlling/modulation of multiple cellular and physiological processes. In the presented review, we summarize the current knowledge on HSPs in the biology of epidermis, the outer skin layer composed of stratified squamous epithelium. This tissue has a vital barrier function preventing from dehydratation due to passive diffusion of water out of the skin, and protecting from infection and other environmental insults. We focused on HSPB1 (HSP27), HSPA1 (HSP70), HSPA2, and HSPC (HSP90), because only these HSPs have been studied in the context of physiology and pathophysiology of the epidermis. The analysis of literature data shows that HSPB1 plays a role in the regulation of final steps of keratinization; HSPA1 is involved in the cytoprotection, HSPA2 contributes to the early steps of keratinocyte differentiation, while HSPC is essential in the re-epithelialization process. Since HSPs have diverse functions in various types of somatic tissues, in spite of multiple investigations, open questions still remain about detailed roles of a particular HSP isoform in the biology of epidermal keratinocytes.
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      headline:Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes
      description:Heat shock proteins (HSPs), a large group of highly evolutionary conserved proteins, are considered to be main elements of the cellular proteoprotection system. HSPs are encoded by genes activated during the exposure of cells to proteotoxic factors, as well as by genes that are expressed constitutively under physiological conditions. HSPs, having properties of molecular chaperones, are involved in controlling/modulation of multiple cellular and physiological processes. In the presented review, we summarize the current knowledge on HSPs in the biology of epidermis, the outer skin layer composed of stratified squamous epithelium. This tissue has a vital barrier function preventing from dehydratation due to passive diffusion of water out of the skin, and protecting from infection and other environmental insults. We focused on HSPB1 (HSP27), HSPA1 (HSP70), HSPA2, and HSPC (HSP90), because only these HSPs have been studied in the context of physiology and pathophysiology of the epidermis. The analysis of literature data shows that HSPB1 plays a role in the regulation of final steps of keratinization; HSPA1 is involved in the cytoprotection, HSPA2 contributes to the early steps of keratinocyte differentiation, while HSPC is essential in the re-epithelialization process. Since HSPs have diverse functions in various types of somatic tissues, in spite of multiple investigations, open questions still remain about detailed roles of a particular HSP isoform in the biology of epidermal keratinocytes.
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         Heat shock proteins
         Epidermis
         Keratinocytes
         Cytoprotection
         Epidermal homeostasis
         Keratinocyte differentiation
         Biomedicine
         general
         Cell Biology
         Biochemistry
         Immunology
         Cancer Research
         Neurosciences
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