scholarly journals Distribution of the collagen binding heat-shock protein in chicken tissues.

1992 ◽  
Vol 40 (7) ◽  
pp. 1021-1029 ◽  
Author(s):  
O Miyaishi ◽  
K Sakata ◽  
M Matsuyama ◽  
S Saga
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Blood Vessels ◽  
Biological Significance ◽  
Basal Layer ◽  
Collagen Type I ◽  
Surrounding Tissue ◽  
Collagen Molecule ◽  
Type I ◽  
Chicken Tissues

We examined the tissue distribution of heat-shock protein MW 47,000 D, hsp47, which binds to native and denatured collagen including Types I, III, and IV, in various chicken tissues by Western blotting and immunohistochemical methods. hsp47 was located on fibrocytes or fibroblasts in the connective tissue in various organs, chondrocytes in the cartilage, smooth muscle cells in the gastrointestinal tract and blood vessels, vitamin A storage cells in sinusoidal area of liver, endothelial cells in blood vessels, and epithelial cells of renal glomeruli, tubules, and basal layer of epidermis. These cells also co-expressed a certain type of collagen molecule. Furthermore, in developing embryos, fibroblasts and chondrocytes expressed hsp47 before the deposition of collagen Type I or Type II in the surrounding tissue. These results indicate that the binding of hsp47 to collagen molecules has important biological significance.

scholarly journals Pirfenidone inhibits TGF-β1-induced over-expression of collagen type I and heat shock protein 47 in A549 cells

2012 ◽  
Vol 12 (1) ◽  
Author(s):  
Keiko Hisatomi ◽  
Hiroshi Mukae ◽  
Noriho Sakamoto ◽  
Yuji Ishimatsu ◽  
Tomoyuki Kakugawa ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Collagen Type ◽  
A549 Cells ◽  
Collagen Type I ◽  
Type I ◽  
Heat Shock Protein 47 ◽  
Over Expression ◽  
Tgf Β1

Changes in Matrix Components in the Developing Human Meniscus

2020 ◽  
Vol 49 (1) ◽  
pp. 207-214
Author(s):  
William Fedje-Johnston ◽  
Ferenc Tóth ◽  
Melissa Albersheim ◽  
Cathy S. Carlson ◽  
Kevin G. Shea ◽  
...  
Keyword(s):  
Blood Vessels ◽  
Cell Density ◽  
Skeletal Maturity ◽  
Skeletal Development ◽  
Collagen Type I ◽  
Type I ◽  
Cellular Density ◽  
Meniscal Healing ◽  
Proteoglycan Content ◽  
Safranin O

Background: Treatment of meniscal tears is necessary to maintain the long-term health of the knee joint. Morphological elements, particularly vascularity, that play an important role in meniscal healing are known to change during skeletal development. Purpose: To quantitatively evaluate meniscal vascularity, cellularity, collagen, and proteoglycan content by age and location during skeletal development. Study Design: Descriptive laboratory study. Methods: Medial and lateral menisci from 14 male and 7 female cadavers aged 1 month to 11 years were collected and evaluated. For each meniscus, histologic and immunohistologic techniques were used to establish the ratio of the area of proteoglycan (safranin O) positivity to the total area (proteoglycan ratio), collagen type I and type II immunostaining positivity, number of blood vessels, and cell density. These features were evaluated over the entire meniscus and also separately in 5 circumferential segments: anterior root, anterior horn, body, posterior horn, and posterior root. Additionally, cell density and number of blood vessels were examined in 3 radial regions: inner, middle, and periphery. Results: Age was associated with a decrease in meniscal vessel count and cell density, while the proteoglycan ratio increased with skeletal maturity. Differences in vessel counts, cellular density, and proteoglycan ratio in different anatomic segments as well as in the inner, middle, and peripheral regions of the developing menisci were also observed. Collagen immunostaining results were inconsistent and not analyzed. Conclusion: The cellularity and vascularity of the developing meniscus decrease with age and the proteoglycan content increases with age. All of these parameters are influenced by location within the meniscus. Clinical Relevance: Age and location differences in meniscal morphology, particularly in the number of blood vessels, are expected to influence meniscal healing.

Chaperones and protein folding in the archaea

2009 ◽  
Vol 37 (1) ◽  
pp. 46-51 ◽  
Author(s):  
Andrew T. Large ◽  
Martin D. Goldberg ◽  
Peter A. Lund
Keyword(s):  
Protein Folding ◽  
Heat Shock ◽  
Gene Transfer ◽  
Horizontal Gene Transfer ◽  
Heat Shock Protein ◽  
Haloferax Volcanii ◽  
Functional Specialization ◽  
Type I ◽  
Type Ii ◽  
Shock Proteins

A survey of archaeal genomes for the presence of homologues of bacterial and eukaryotic chaperones reveals several interesting features. All archaea contain chaperonins, also known as Hsp60s (where Hsp is heat-shock protein). These are more similar to the type II chaperonins found in the eukaryotic cytosol than to the type I chaperonins found in bacteria, mitochondria and chloroplasts, although some archaea also contain type I chaperonin homologues, presumably acquired by horizontal gene transfer. Most archaea contain several genes for these proteins. Our studies on the type II chaperonins of the genetically tractable archaeon Haloferax volcanii have shown that only one of the three genes has to be present for the organisms to grow, but that there is some evidence for functional specialization between the different chaperonin proteins. All archaea also possess genes for prefoldin proteins and for small heat-shock proteins, but they generally lack genes for Hsp90 and Hsp100 homologues. Genes for Hsp70 (DnaK) and Hsp40 (DnaJ) homologues are only found in a subset of archaea. Thus chaperone-assisted protein folding in archaea is likely to display some unique features when compared with that in eukaryotes and bacteria, and there may be important differences in the process between euryarchaea and crenarchaea.

scholarly journals COMPARATIVE ESTIMATION OF HEAT SHOCK PROTEIN 70 (HSP 70) EXPRESSION IN HEALTH, GINGIVITIS AND PERIODONTITIS.

2020 ◽  
Vol 9 (1) ◽  
Author(s):  
Dhivya Darshani D ◽  
Nithya anand ◽  
Dr. Vidyarani Shyamsundar ◽  
Dr.Bagavad Gita
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Periodontal Diseases ◽  
Maxillofacial Surgery ◽  
Basal Layer ◽  
Gingival Tissue ◽  
Oral And Maxillofacial Surgery ◽  
Hsp 70 ◽  
Tissue Samples

Background: Although periodontal bacteria are the causative agents of periodontitis, subsequent progression and disease severity are thought to be determined by a host's immune responses. HSPs may be expressed during periodontal diseases. Objective: To compare the HSP 70 expression within layers of epithelium and connective tissue and correlate the expression of HSP 70 with the severity of periodontal disease. Materials & Methods: The study population comprised of 25 patients with periodontitis, and 23 patients with gingivitis and 21 controls with healthy gingival; tissue samples collected from the Department of Periodontology /Oral and Maxillofacial Surgery respectively. An immunohistochemical analysis was done for HSP 70 expression. Results: One way ANOVA results indicate a statistically significant expression in basal layer for mild inflammation (mean=2.36) and intensity in stratum spinosum for mild (mean=2.27) and minimum (mean=2.39) inflammation. An overall greater HSP 70 expression is noticed in periodontitis group (total IRIDI = 25.41) however not statistically significant Conclusion: We elucidated that there was significant HSP 70 expression in stratum basale and spinosum for mild inflammation that did not increase with severity of inflammation. The overall expression of HSP70 is insignificantly elevated in periodontitis compared to health & gingivitis. Statistical analysis used: One way Analysis of Variance (ANOVA), Mann Whitney U test and Kruskal Wallis Test. Keywords:  Heat shock protein 70 (HSP 70), Immunohistochemistry (IHC), Porphyromonas gingivalis.

scholarly journals GmDNJ1, a type‐I heat shock protein 40 (HSP40), is responsible for both Growth and heat tolerance in soybean

Plant Direct ◽  
2021 ◽  
Vol 5 (1) ◽  
Author(s):  
Kwan‐Pok Li ◽  
Cheuk‐Hon Wong ◽  
Chun‐Chiu Cheng ◽  
Sau‐Shan Cheng ◽  
Man‐Wah Li ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Tolerance ◽  
Type I
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